Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH.
a secondary alcohol + NAD(+) = a ketone + H(+) + NADH.
ethanol + NAD(+) = acetaldehyde + H(+) + NADH.
Some members of this group oxidize only primary alcohols; others act also on secondary alcohols.
May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55.
a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH.
a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH.
The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+).
The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.
L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH.
L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH.
D-1-amino-2-propanol:NAD(2) oxidoreductase
Also converts diacetyl into acetoin with NADH as reductant.
(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH.
glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH.
NAD(+) + propane-1,2-diol 1-phosphate = H(+) + hydroxyacetone phosphate + NADH.
glycerol-3-phosphate dehydrogenase (NAD(+))
alpha-glycerol phosphate dehydrogenase (NAD)
alpha-glycerophosphate dehydrogenase (NAD)
glycerol-3-phosphate dehydrogenase (NAD)
L-alpha-glycerol phosphate dehydrogenase
NAD-alpha-glycerophosphate dehydrogenase
NAD-dependent glycerol-3-phosphate dehydrogenase
NAD-dependent glycerol phosphate dehydrogenase
NADH-dihydroxyacetone phosphate reductase
NAD-L-glycerol-3-phosphate dehydrogenase
NAD-linked glycerol 3-phosphate dehydrogenase
Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH.
Also acts as an L-erythrulose reductase.
NAD(+) + xylitol = D-xylulose + H(+) + NADH.
NADP(+) + xylitol = H(+) + L-xylulose + NADPH.
D-arabinitol + NAD(+) = D-xylulose + H(+) + NADH.
L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH.
L-arabinitol 2-dehydrogenase (ribulose forming)
L-arabinitol + NAD(+) = H(+) + L-ribulose + NADH.
This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals.
It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol.
Enzymes from different organisms or tissues display different substrate specificity.
The enzyme is specific to NAD(+) and can not use NADP(+).
L-iditol + NAD(+) = H(+) + keto-L-sorbose + NADH.
H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+).
Also converts xylitol into L-xylulose and L-glucitol into L-fructose.
D-iditol + NAD(+) = H(+) + keto-D-sorbose + NADH.
NAD(+) + xylitol = H(+) + L-xylulose + NADH.
L-glucitol + NAD(+) = H(+) + keto-L-fructose + NADH.
Also converts other alditols containing an L-threo-configuration adjacent to a primary alcohol group into the corresponding sugars.
The enzyme from Agrobacterium rubrum C58 is part of D-altritol and galactitol degradation pathways.
galactitol + NAD(+) = H(+) + keto-D-tagatose + NADH.
D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate + H(+) + NADH.
myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose.
L-gulonate + NADP(+) = aldehydo-D-glucuronate + H(+) + NADPH.
L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + H(+) + NADPH.
an alditol + NAD(+) = an aldose + H(+) + NADH.
an alditol + NADP(+) = an aldose + H(+) + NADPH.
galactitol + NADP(+) = D-galactose + H(+) + NADPH.
galactitol + NAD(+) = D-galactose + H(+) + NADH.
L-arabinitol + NAD(+) = H(+) + L-arabinose + NADH.
L-arabinitol + NADP(+) = H(+) + L-arabinose + NADPH.
H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate.
The Neurospora enzyme also catalyzes the reactions of EC 3.5.4.19 and EC 3.6.1.31.
H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH.
quinate/shikimate dehydrogenase (NAD(+))
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD(+) as a cofactor.
While the enzyme can act on both quinate and shikimate, activity is higher with the former.
L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH.
In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10.
NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH.
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
glycolate + NAD(+) = glyoxylate + H(+) + NADH.
Also oxidizes other (S)-2-hydroxymonocarboxylic acids.
NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme.
(S)-lactate + NAD(+) = H(+) + NADH + pyruvate.
(R)-lactate + NAD(+) = H(+) + NADH + pyruvate.
(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH.
Also oxidizes other 3-hydroxymonocarboxylic acids.
(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH.
3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH.
(S)-3-hydroxy-2-methylpropanoate + NAD(+) = (S)-methylmalonate semialdehyde + H(+) + NADH.
(R)-mevalonate + NAD(+) = H(+) + mevaldate + NADH.
(R)-mevalonate + NADP(+) = H(+) + mevaldate + NADPH.
hydroxymethylglutaryl-CoA reductase (NADPH)
3-hydroxy-3-methylglutaryl-coenzyme A reductase
The enzyme is inactivated by EC 2.7.11.31 and reactivated by EC 3.1.3.47.
(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH.
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacylhydrolipoate.
Some enzymes act, more slowly, with NADP(+).
Broad specificity to acyl chain-length (cf. EC 1.1.1.211).
a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH.
a (3R)-3-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) + NADPH.
(3R)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH.
Also oxidizes some other 2-hydroxydicarboxylic acids.
(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate.
malate dehydrogenase (oxaloacetate-decarboxylating)
Unlike EC 1.1.1.39, this enzyme can also decarboxylate oxaloacetate, cf. EC 1.1.1.40.
(S)-malate + NAD(+) = CO2 + NADH + pyruvate.
Does not decarboxylate added oxaloacetate.
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+))
The enzyme catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate, cf. EC 1.1.1.38 and EC 1.1.1.39.
(S)-malate + NADP(+) = CO2 + NADPH + pyruvate.
nicotinamide adenine dinucleotide isocitrate dehydrogenase
Unlike EC 1.1.1.42, oxalosuccinate cannot be used as a substrate.
In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD(+)-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP(+)-linked enzyme that is found in both mitochondria and cytoplasm.
The enzyme from some species can also use NADP(+) but much more slowly.
D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH.
dual-cofactor-specific isocitrate dehydrogenase
isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase
isocitrate dehydrogenase (NADP-dependent)
triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase
Unlike EC 1.1.1.41, oxalosuccinate can be used as a substrate.
The enzyme from some species can also use NAD(+) but much more slowly.
D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH.
6-phospho-D-gluconate + NADP(+) = 6-phospho-2-dehydro-D-gluconate + H(+) + NADPH.
6-phospho-D-gluconate + NAD(+) = 6-phospho-2-dehydro-D-gluconate + H(+) + NADH.
phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating)
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions.
6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH.
L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH.
alpha-L-arabinopyanose + NAD(+) = H(+) + L-arabinono-1,4-lactone + NADH.
This enzyme has similar activity with either NAD(+) or NADP(+).
D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH.
D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH.
This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose.
D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH.
glucose-6-phosphate dehydrogenase (NADP(+))
The enzyme catalyzes a step of the pentose phosphate pathway.
The enzyme is specific for NADP(+), cf. EC 1.1.1.363 and EC 1.1.1.388.
D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH.
3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)
3alpha-hydroxysteroid 3-dehydrogenase (B-specific)
3alpha-hydroxysteroid dehydrogenase (B-specific)
The enzyme acts on androsterone and other 3alpha-hydroxysteroids and on 9-, 11- and 15-hydroxyprostaglandin.
Si-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.213).
a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) + NADH.
a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH.
3(or 17)beta-hydroxysteroid dehydrogenase
Also acts on other 3beta- or 17beta-hydroxysteroids (cf. EC 1.1.1.209).
NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH.
NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADPH.
3alpha-hydroxycholanate dehydrogenase (NAD(+))
Also acts on other 3alpha-hydroxysteroids with an acidic side-chain.
lithocholate + NAD(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADH.
3alpha(or 20beta)-hydroxysteroid dehydrogenase
The 3alpha-hydroxy group or 20beta-hydroxy group of pregnane and androstane steroids can act as donor.
androstan-3alpha,17beta-diol + NAD(+) = 17beta-hydroxyandrostanone + H(+) + NADH.
5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH.
Also acts on saturated primary alcohols.
allyl alcohol + NADP(+) = acrolein + H(+) + NADPH.
NADP(+) + propane-1,2-diol = (S)-lactaldehyde + H(+) + NADPH.
NAD(+) + ribitol = D-ribulose + H(+) + NADH.
D-mannonate + NAD(+) = H(+) + keto-D-fructuronate + NADH.
D-mannonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH.
D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH.
3-hydroxypropanoate + NAD(+) = 3-oxopropanoate + H(+) + NADH.
(R)-glycerate + NADP(+) = 2-hydroxy-3-oxopropanoate + H(+) + NADPH.
(R)-glycerate + NAD(+) = 2-hydroxy-3-oxopropanoate + H(+) + NADH.
4-hydroxybutanoate + NAD(+) = H(+) + NADH + succinate semialdehyde.
The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids.
The mammalian enzyme is bifunctional and also catalyzes EC 1.1.1.270.
The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, it is Si-specific with respect to NAD(P)(+).
17beta-estradiol + NAD(+) = estrone + H(+) + NADH.
17beta-estradiol + NADP(+) = estrone + H(+) + NADPH.
testosterone 17beta-dehydrogenase (NADP(+))
Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal.
Also acts, more slowly, on 9-hydroxynonanoate and 11-hydroxyundecanoate.
10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + H(+) + NADH.
D-mannitol + NAD(+) = D-fructose + H(+) + NADH.
D-gluconate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH.
D-gluconate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH.
Reduces aliphatic aldehydes of chain length from C2 to C14, with greatest activity on C4, C6 and C8 aldehydes.
glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH.
Acts, less rapidly, on other long-chain alcohols.
NAD(+) + octan-1-ol = H(+) + NADH + octanal.
(R)-1-aminopropan-2-ol + NAD(+) = aminoacetone + H(+) + NADH.
This enzyme catalyzes the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol.
It can also catalyze the irreversible reduction of diacetyl to (S)-acetoin.
(S,S)-butane-2,3-diol + NAD(+) = (S)-acetoin + H(+) + NADH.
(R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + H(+) + NADH.
(S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + H(+) + NADH.
methylglyoxal reductase (NADH-dependent)
This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, by its coenzyme requirement, reaction direction, and enantiomeric preference.
(R)-lactaldehyde + NAD(+) = H(+) + methylglyoxal + NADH.
Also reduces hydroxypyruvate to glycerate.
glycolate + NADP(+) = glyoxylate + H(+) + NADPH.
Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
NADP(+) + propan-2-ol = acetone + H(+) + NADPH.
(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH.
(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate.
D-malate dehydrogenase (decarboxylating)
(R)-malate + NAD(+) = CO2 + NADH + pyruvate.
(R)-3,3-dimethylmalate + NAD(+) = 3-methyl-2-oxobutanoate + CO2 + NADH.
(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH.
alpha-keto-beta-hydroxylacyl reductoisomerase
dihydroxyisovalerate dehydrogenase (isomerizing)
The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382 and EC 1.1.1.383).
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH.
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH.
(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD(+) oxidoreductase (decarboxylating)
2-hydroxy-3-carboxyadipate dehydrogenase
3-carboxy-2-hydroxyadipate:NAD(+) oxidoreductase (decarboxylating)
3-carboxy-2-hydroxyadipate dehydrogenase
Forms part of the lysine biosynthesis pathway in fungi.
(2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH.
3-hydroxy-3-methylglutaryl coenzyme A reductase
beta-hydroxy-beta-methylglutaryl CoA-reductase
beta-hydroxy-beta-methylglutaryl coenzyme A reductase
hydroxymethylglutaryl coenzyme A reductase
(R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
A group of enzymes with broad specificity toward primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity toward short-chain aliphatic alcohols.
an aromatic primary alcohol + NAD(+) = an aromatic aldehyde + H(+) + NADH.
Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found.
an aromatic primary alcohol + NADP(+) = an aromatic aldehyde + H(+) + NADPH.
oxaloglycolate reductase (decarboxylating)
Also reduces hydroxypyruvate to D-glycerate and glyoxylate to glycolate.
(R)-glycerate + CO2 + NAD(+) = 2-hydroxy-3-oxosuccinate + 2 H(+) + NADH.
(R)-glycerate + CO2 + NADP(+) = 2-hydroxy-3-oxosuccinate + 2 H(+) + NADPH.
NAD(+) + tartrate = 2-hydroxy-3-oxosuccinate + H(+) + NADH.
(2R,3S)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) + NADH.
(2R,3R)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + H(+) + NADH.
glycerol-3-phosphate dehydrogenase [NAD(P)(+)]
glycerol 3-phosphate dehydrogenase (NAD(P))
glycerol 3-phosphate dehydrogenase (NADP)
glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate))
L-glycerol-3-phosphate:NAD(P) oxidoreductase
The enzyme from Escherichia coli shows specificity for the B side of NADPH.
NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADPH.
Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis.
The reaction occurs predominantly in the direction of reduction.
The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.
(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH.
Substrates contain an aromatic ring with a pyruvate side chain.
The most active substrates are halogenated derivatives.
Compounds with hydroxy or amino groups in the 3 or 5 position are inactive.
3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD(+) = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + H(+) + NADH.
(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADH.
3-hydroxybenzyl alcohol + NADP(+) = 3-hydroxybenzaldehyde + H(+) + NADPH.
(R)-2-hydroxyoctadecanoate + NAD(+) = 2-oxooctadecanoate + H(+) + NADH.
(S)-2-hydroxyoctadecanoate + NAD(+) = 2-oxooctadecanoate + H(+) + NADH.
3-oxoacyl-[acyl-carrier-protein] reductase
Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.
a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH.
palmitoyldihydroxyacetone-phosphate reductase
Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate.
1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-hexadecanoylglycerone 3-phosphate + H(+) + NADPH.
1-O-alkylglycerone 3-phosphate + H(+) + NADPH = 1-O-alkyl-sn-glycero-3-phosphate + NADP(+).
D-3-oxosphinganine:B-NADPH oxidoreductase
NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH.
Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine.
This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex.
In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH.
The enzyme, isolated from animals, is specific for 4-oxo-L-proline and cis-4-hydroxy-L-proline.
It has no activity with trans-4-hydroxy-L-proline.
cis-4-hydroxy-L-proline + NAD(+) = 4-oxo-L-proline + H(+) + NADH.
all-trans-retinol dehydrogenase (NAD(+))
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD(+)/NADH as cofactors.
Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form.
No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315).
Also active with 3alpha-hydroxysteroids.
all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH.
all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH.
(R)-pantoate + NAD(+) = (R)-4-dehydropantoate + H(+) + NADH.
The enzyme acts on the hemiacetal form of the substrate.
NAD(+) + pyridoxal = 4-pyridoxolactone + H(+) + NADH.
carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH.
(R)-4-hydroxyphenyllactate dehydrogenase
The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan.
The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn(2+) and can also use NADPH with lower activity.
(R)-3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) + NADH.
3-(indol-3-yl)lactate + NAD(+) = H(+) + indole-3-pyruvate + NADH.
(S)-3-(imidazol-5-yl)lactate + NAD(+) = 3-(imidazol-5-yl)pyruvate + H(+) + NADH.
(S)-3-(imidazol-5-yl)lactate + NADP(+) = 3-(imidazol-5-yl)pyruvate + H(+) + NADPH.
3(20)alpha-hydroxysteroids are also oxidized, more slowly.
(S)-indan-1-ol + NAD(+) = H(+) + indan-1-one + NADH.
(S)-indan-1-ol + NADP(+) = H(+) + indan-1-one + NADPH.
L-xylose + NADP(+) = H(+) + L-xylono-1,4-lactone + NADPH.
D-apiitol + NAD(+) = aldehydo-D-apiose + H(+) + NADH.
Also acts, more slowly, on D-xylose and other pentoses.
D-ribose + H2O + NADP(+) = D-ribonate + 2 H(+) + NADPH.
D-arabinose + NAD(+) = D-arabinono-1,4-lactone + H(+) + NADH.
Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.
D-arabinose + NADP(+) = D-arabinono-1,4-lactone + H(+) + NADPH.
Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose.
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH.
Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose.
an aldopyranose + NAD(+) = aldono-1,5-lactone + H(+) + NADH.
Acts on L-fucose, D-arabinose and L-xylose.
The animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose.
a D-threo-aldose + NAD(+) = a D-threo-aldono-1,5-lactone + H(+) + NADH.
keto-L-sorbose + NADP(+) = 5-dehydro-D-fructose + H(+) + NADPH.
D-fructose + NADP(+) = 5-dehydro-D-fructose + H(+) + NADPH.
2-deoxy-D-gluconate + NAD(+) = 3-dehydro-2-deoxy-D-gluconate + H(+) + NADH.
2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase
2-keto-3-deoxy-D-gluconate dehydrogenase
2-dehydro-3-deoxy-D-gluconate + NADP(+) = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + H(+) + NADPH.
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
The enzyme from Pseudomonas acts equally well on NAD(+) or NADP(+), while those from Erwinia chrysanthemi and Escherichia coli are more specific for NAD(+).
2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH.
L-threonate + NAD(+) = 3-dehydro-D-erythronate + H(+) + NADH.
3-dehydro-L-gulonate + NAD(+) = 2,3-dioxo-L-gulonate + H(+) + NADH.
3-dehydro-L-gulonate + NADP(+) = 2,3-dioxo-L-gulonate + H(+) + NADPH.
D-mannonate + NAD(+) = D-mannuronate + H(+) + NADH.
D-mannonate + NADP(+) = D-mannuronate + H(+) + NADPH.
Also uses the corresponding deoxynucleoside diphosphate derivative as a substrate.
GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate + 3 H(+) + 2 NADH.
In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase.
dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH.
Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5.
dTDP-6-deoxy-beta-L-talose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH.
GDP-6-deoxy-alpha-D-talose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.
GDP-6-deoxy-alpha-D-talose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH.
UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = 3 H(+) + 2 NADH + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate.
The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD(+) and NADP(+) as electron acceptor (cf. EC 1.1.1.405).
D-ribitol 5-phosphate + NADP(+) = D-ribulose 5-phosphate + H(+) + NADPH.
D-ribitol 5-phosphate + NAD(+) = D-ribulose 5-phosphate + H(+) + NADH.
D-mannitol + NADP(+) = D-fructose + H(+) + NADPH.
D-sorbitol 6-phosphate + NAD(+) = beta-D-fructose 6-phosphate + H(+) + NADH.
15-hydroxyprostaglandin dehydrogenase (NAD(+))
Acts on prostaglandins E2, F2alpha and B1, but not on prostaglandin D2 (cf. EC 1.1.1.196 and EC 1.1.1.197).
NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + NADH.
5D-5-O-methyl-chiro-inositol + NADP(+) = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + H(+) + NADPH.
1D-5-O-methyl-myo-inositol + NAD(+) = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + H(+) + NADH.
Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.
NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde.
3beta-hydroxy-Delta(5)-steroid dehydrogenase
3beta-hydroxy-5-ene steroid dehydrogenase
Acts on 3beta-hydroxyandrost-5-en-17-one to form androst-4-ene-3,17-dione and on 3beta-hydroxypregn-5-en-20-one to form progesterone.
a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-steroid + H(+) + NADH.
3beta-hydroxyandrost-5-en-17-one + NAD(+) = androst-5-ene-3,17-dione + H(+) + NADH.
an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) + NADPH.
a 16alpha-hydroxysteroid + NADP(+) = a 16-oxosteroid + H(+) + NADPH.
a 16alpha-hydroxysteroid + NAD(+) = a 16-oxosteroid + H(+) + NADH.
17alpha-estradiol + NAD(+) = estrone + H(+) + NADH.
17alpha-estradiol + NADP(+) = estrone + H(+) + NADPH.
Re-specific with respect to NAD(P)(+) (cf. EC 1.1.1.62).
(17R,20S)-17,20-dihydroxypregn-4-en-3-one + NAD(+) = 17alpha-hydroxyprogesterone + H(+) + NADH.
(17R,20S)-17,20-dihydroxypregn-4-en-3-one + NADP(+) = 17alpha-hydroxyprogesterone + H(+) + NADPH.
21-hydroxysteroid dehydrogenase (NAD(+))
Acts on a number of 21-hydroxycorticosteroids.
NAD(+) + pregnan-21-ol = H(+) + NADH + pregnan-21-al.
21-hydroxysteroid dehydrogenase (NADP(+))
21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase
21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide phosphate)
NADP(+) + pregnan-21-ol = H(+) + NADPH + pregnan-21-al.
3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase
3alpha-hydroxy-5beta-androstan-17-one + NAD(+) = 5beta-androstane-3,17-dione + H(+) + NADH.
sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)
This enzyme catalyzes the final step in the de novo synthesis of tetrahydrobiopterin from GTP.
The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin.
L-erythro-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH + sepiapterin.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH.
(S)-ureidoglycolate + NAD(+) = H(+) + N-carbamoyl-2-oxoglycine + NADH.
(S)-ureidoglycolate + NADP(+) = H(+) + N-carbamoyl-2-oxoglycine + NADPH.
glycerol + NADP(+) = dihydroxyacetone + H(+) + NADPH.
(3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH.
Catalyzes the oxidation of the 7alpha-hydroxy group of bile acids and alcohols both in their free and conjugated forms.
The Bacteroides fragilis and Clostridium enzymes can also utilize NADP(+).
cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADH.
dihydrobunolol + NADP(+) = bunolol + H(+) + NADPH.
NAD(+) is also utilized, but more slowly.
D-threitol + NADP(+) = D-erythrulose + H(+) + NADPH.
4-Methylcyclohexanol and cyclohexanol can also act as substrates.
cyclopentanol + NAD(+) = cyclopentanone + H(+) + NADH.
The liver enzyme acts on long-chain alcohols from C8 to C16.
The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids.
hexadecan-1-ol + NAD(+) = H(+) + hexadecanal + NADH.
Acts on a variety of 2-alkyn-1-ols, and also on 1,4-butanediol.
NADP(+) also acts as acceptor, but more slowly.
2-butyne-1,4-diol + NAD(+) = 4-hydroxy-2-butynal + H(+) + NADH.
hydroxycyclohexanecarboxylate dehydrogenase
Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate.
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD(+) = (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + H(+) + NADH.
hydroxymalonate + NAD(+) = H(+) + NADH + oxomalonate.
2-dehydropantolactone reductase (Re-specific)
2-dehydropantolactone reductase (A-specific)
2-dehydropantoyl-lactone reductase (A-specific)
The enzyme from Saccharomyces cerevisiae differs from that from Escherichia coli (EC 1.1.1.214), which is specific for the Si-face of NADP, and in receptor requirements from EC 1.1.99.26.
(R)-pantolactone + NADP(+) = 2-dehydropantolactone + H(+) + NADPH.
(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH.
3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)
3beta-hydroxy-4alpha-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating)
3beta-hydroxy-4beta-methylcholestenecarboxylate 3-dehydrogenase (decarboxylating)
3beta-hydroxy-4beta-methylcholestenoate dehydrogenase
sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating)
The enzyme participates in the biosynthesis of several important sterols such as ergosterol and cholesterol.
It is part of a three enzyme system that removes methyl groups from the C-4 position of steroid molecules.
The first enzyme, EC 1.14.18.9, catalyzes three successive oxidations of the methyl group, resulting in a carboxyl group; the second enzyme, EC 1.1.1.170, catalyzes an oxidative decarboxylation that results in a reduction of the 3beta-hydroxy group at the C-3 carbon to an oxo group; and the last enzyme, EC 1.1.1.270, reduces the 3-oxo group back to a 3beta-hydroxyl.
If a second methyl group remains at the C-4 position, this enzyme also catalyzes its epimerization from 4beta to 4alpha orientation, so it could serve as a substrate for a second round of demethylation.
a 3beta-hydroxysteroid-4alpha-carboxylate + NADP(+) = a 3-oxosteroid + CO2 + NADPH.
a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(+) = a 3-oxosteroid + CO2 + NADH.
4beta-methylzymosterol-4alpha-carboxylate + NADP(+) = 3-dehydro-4-methylzymosterol + CO2 + NADPH.
2-hydroxyadipate + NAD(+) = 2-oxoadipate + H(+) + NADH.
L-rhamnofuranose + NAD(+) = H(+) + L-rhamnono-1,4-lactone + NADH.
Also oxidizes, more slowly, the cis isomer and 2-hydroxycyclohexanone.
NAD(+) + trans-cyclohexane-1,2-diol = 2-hydroxycyclohexan-1-one + H(+) + NADH.
D-xylose + NAD(+) = D-xylono-1,5-lactone + H(+) + NADH.
Catalyzes the oxidation of the 12alpha-hydroxy group of bile acids, both in their free and conjugated form.
cholate + NADP(+) = 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + H(+) + NADPH.
glycerol-3-phosphate 1-dehydrogenase (NADP(+))
NADP(+) + sn-glycerol 3-phosphate = D-glyceraldehyde 3-phosphate + H(+) + NADPH.
3-hydroxy-2-methylbutyryl-CoA dehydrogenase
2-methyl-3-hydroxybutyryl-CoA dehydrogenase
Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA.
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methyl-3-oxobutanoyl-CoA + H(+) + NADH.
D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)
The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose.
D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH.
cholest-5-ene-3beta,7alpha-diol 3beta-dehydrogenase
3beta-hydroxy-Delta(5)-C27-steroid oxidoreductase
Highly specific for 3beta-hydroxy-C27-steroids with Delta(5)-double bond.
7alpha-hydroxycholesterol + NAD(+) = 7alpha-hydroxycholest-4-en-3-one + H(+) + NADH.
Also acts, more slowly on farnesol but not on nerol.
The enzyme produces a mixture known as citral, which includes geranial and neral.
It is still not known whether neral is produced directly by the enzyme, or by isomerization of geranial.
(2E)-geraniol + NADP(+) = (2E)-geranial + H(+) + NADPH.
Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin, and prostaglandins E and F, reducing them to the corresponding alcohol.
Si-specific with respect to NADPH (cf. EC 1.1.1.2).
The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound.
In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced.
an L-glycol + NADP(+) = a 2-hydroxycarbonyl + H(+) + NADPH.
an L-glycol + NAD(+) = a 2-hydroxycarbonyl + H(+) + NADH.
thymidine-diphosphate-galactose dehydrogenase
dTDP-D-galactose + H2O + 2 NADP(+) = dTDP-D-galacturonate + 3 H(+) + 2 NADPH.
guanosine diphosphate-4-keto-D-rhamnose reductase
The enzyme, which operates in the opposite direction to that shown, forms a mixture of GDP-alpha-D-rhamnose and its C-4 epimer, GDP-6-deoxy-alpha-D-talose.
GDP-alpha-D-rhamnose + NAD(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADH.
GDP-alpha-D-rhamnose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.
Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2.
Also catalyzes the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone.
NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin D2.
Reduces prostaglandin E2 to prostaglandin F2alpha.
A number of other 9-oxo- and 15-oxo-prostaglandin derivatives can also be reduced to the corresponding hydroxy compounds.
NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin E2.
indole-3-ethanol + NAD(+) = H(+) + indole-3-acetaldehyde + NADH.
indole-3-ethanol + NADP(+) = H(+) + indole-3-acetaldehyde + NADPH.
a long-chain primary fatty alcohol + H2O + 2 NAD(+) = a long-chain fatty acid + 3 H(+) + 2 NADH.
5-amino-6-(5-phosphoribosylamino)uracil reductase
5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH.
Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.
(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH.
Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194).
(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH.
(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) + NADPH.
(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde + H(+) + NADPH.
15-hydroxyprostaglandin-D dehydrogenase (NADP(+))
prostaglandin-D 15-dehydrogenase (NADP(+))
prostaglandin-D 15-dehydrogenase (NADP+)
Specific for prostaglandins D (cf. EC 1.1.1.141 and EC 1.1.1.197).
NADP(+) + prostaglandin D2 = 15-oxoprostaglandin D2 + H(+) + NADPH.
15-hydroxyprostaglandin dehydrogenase (NADP(+))
Acts on prostaglandins E2, F2alpha and B1, but not on prostaglandin D2 (cf. EC 1.1.1.141 and EC 1.1.1.196).
NADP(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) + NADPH.
(1R,2S,4R)-borneol + NAD(+) = (1R,4R)-camphor + H(+) + NADH.
(6R)-2-acetyl-6-(3-acetyl-2,4,6-trihydroxy-5-methylphenyl)-3-hydroxy-6-methylcyclohexa-2,4-dien-1-one + NAD(+) = (S)-usnate + 2 H(+) + NADH.
NADP-dependent D-sorbitol-6-phosphate dehydrogenase
In the reverse reaction, acts also on D-galactose 6-phosphate and, more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate.
D-sorbitol 6-phosphate + NADP(+) = aldehydo-D-glucose 6-phosphate + H(+) + NADPH.
7beta-hydroxysteroid dehydrogenase (NADP(+))
NADP-dependent 7beta-hydroxysteroid dehydrogenase
Catalyzes the oxidation of the 7beta-hydroxy group of bile acids such as ursodeoxycholate.
a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) + NADPH.
NAD(+) + propane-1,3-diol = 3-hydroxypropanal + H(+) + NADH.
The enzyme, characterized from the bacterium Agrobacterium fabrum, participates in oxidative degradation pathways for galacturonate and glucuronate.
The enzyme can only accept the beta anomeric form of the substrate.
The 1,5 lactone product is rather stable at cytosolic pH and does not hydrolyze spontaneously at a substantial rate.
beta-D-galacturonate + NAD(+) = D-galactaro-1,5-lactone + H(+) + NADH.
beta-D-glucuronate + NAD(+) = D-glucaro-1,5-lactone + H(+) + NADH.
The enzyme acts on the hydroxy group of the hydrated derivative of the substrate.
Also oxidizes other tropan-3alpha-ols, but not the corresponding beta-derivatives.
Represents, along with EC 1.1.1.236, a branch point in tropane alkaloid metabolism.
Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines.
Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific.
NADP(+) + tropine = H(+) + NADPH + tropinone.
Acts on a number of other cyclohexanols and cyclohexenols.
(-)-menthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH.
(+)-neomenthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH.
3(or 17)alpha-hydroxysteroid dehydrogenase
Acts on the 3alpha-hydroxy group of androgens of the 5alpha-androstane series; and also, more slowly, on the 17alpha-hydroxyl group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51).
androsterone + NADP(+) = 5alpha-androstan-3,17-dione + H(+) + NADPH.
androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH.
3beta-(or 20alpha)-hydroxysteroid dehydrogenase
5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADPH.
long-chain-3-hydroxyacyl-CoA dehydrogenase
This enzyme was purified from the mitochondrial inner membrane.
The enzyme has a preference for long-chain substrates, and activity with C16 substrates was 6- to 15-fold higher than with C4 substrates (cf. EC 1.1.1.35).
a long-chain (3S)-3-hydroxy fatty acyl-CoA + NAD(+) = a long-chain 3-oxo-fatty acyl-CoA + H(+) + NADH.
3-oxoacyl-[acyl-carrier-protein] reductase (NADH)
Forms part of the fatty acid synthase system in plants.
a (3R)-hydroxyacyl-[ACP] + NAD(+) = a 3-oxoacyl-[ACP] + H(+) + NADH.
3alpha-hydroxysteroid dehydrogenase (Re-specific)
3alpha-hydroxysteroid dehydrogenase (A-specific)
The enzyme acts on multiple 3alpha-hydroxysteroids.
Re-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.50).
Enzymes whose stereo-specificity with respect to NAD(+) or NADP(+) is not known are described by EC 1.1.1.357.
2-dehydropantolactone reductase (Si-specific)
2-dehydropantolactone reductase (B-specific)
2-dehydropantoyl-lactone reductase (B-specific)
The Escherichia coli enzyme differs from that from Saccharomyces cerevisiae (EC 1.1.1.168), which is specific for the Re-face of NADP, and in receptor requirements from EC 1.1.99.26.
Also acts on L-idonate, D-galactonate and D-xylonate.
D-gluconate + NADP(+) = 2-dehydro-D-gluconate + H(+) + NADPH.
Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol.
(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH.
benzyl-2-methyl-hydroxybutyrate dehydrogenase
benzyl 2-methyl-3-hydroxybutyrate dehydrogenase
Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise highly specific.
benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP(+) = benzyl 2-methyl-3-oxobutanoate + H(+) + NADPH.
Also acts on some other alkaloids, including codeine, normorphine and ethylmorphine, but only very slowly on 7,8-saturated derivatives such as dihydromorphine and dihydrocodeine.
In the reverse direction, also reduces naloxone to the 6alpha-hydroxy analog.
Activated by 2-sulfanylethan-1-ol (2-mercaptoethanol).
morphine + NAD(+) = H(+) + morphinone + NADH.
morphine + NADP(+) = H(+) + morphinone + NADPH.
This plant enzyme, involved in the biosynthesis of anthocyanidins, is known to act on (+)-dihydrokaempferol, (+)-taxifolin, and (+)-dihydromyricetin, although some enzymes may act only on a subset of these compounds.
Each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol.
NAD(+) can act instead of NADP(+), but more slowly.
a (2R,3S,4S)-leucoanthocyanidin + NADP(+) = a (2R,3R)-dihydroflavonol + H(+) + NADPH.
(2R,3S,4S)-3,4-leucopelargonidin + NADP(+) = (2R,3R)-dihydrokaempferol + H(+) + NADPH.
6-pyruvoyl tetrahydropterin (2'-oxo)reductase
6-pyruvoyl-tetrahydropterin 2'-reductase
6-lactoyl-5,6,7,8-tetrahydropterin + NADP(+) = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + NADPH.
Oxidizes vomifoliol to dehydrovomifoliol; involved in the metabolism of abscisic acid in Corynebacterium sp.
(6S,9R)-vomifoliol + NAD(+) = (6S)-6-hydroxy-3-oxo-alpha-ionone + H(+) + NADH.
Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and (+)-trans-pulegol.
Involved in the biosynthesis of menthol and related monoterpenes in peppermint (Mentha piperita) leaves.
(1S,6R)-isopiperitenol + NAD(+) = (6R)-isopiperitenone + H(+) + NADH.
Involved in the biosynthesis of mannitol in celery (Apium graveolens) leaves.
D-mannitol 1-phosphate + NADP(+) = D-mannose 6-phosphate + H(+) + NADPH.
Chlordecone, an organochlorine pesticide, is 1,1a,3,3a,4,5,5a,5b,6-decachlorooctahydro-1,3,4-metheno-2H-cyclobuta[cd]pentalen-2-one.
chlordecone alcohol + NADP(+) = chlordecone + H(+) + NADPH.
4-hydroxycyclohexanecarboxylate dehydrogenase
The enzyme from Corynebacterium cyclohexanicum is highly specific for the trans-4-hydroxy derivative.
NAD(+) + trans-4-hydroxycyclohexanecarboxylate = 4-oxocyclohexanecarboxylate + H(+) + NADH.
(1S,2R,4S)-borneol + NAD(+) = (1S,4S)-camphor + H(+) + NADH.
Involved in the biosynthesis of (+)-3-thujone and (-)-3-isothujone.
(1S,3R,5S)-sabinol + NAD(+) = (1S,5S)-sabinone + H(+) + NADH.
diethyl 2-methyl-3-oxosuccinate reductase
Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate; and on the corresponding dimethyl esters.
diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP(+) = diethyl 2-methyl-3-oxosuccinate + H(+) + NADPH.
3alpha-hydroxyglycyrrhetinate dehydrogenase
Highly specific to 3alpha-hydroxy derivatives of glycyrrhetinate and its analogs.
3alpha-hydroxyglycyrrhetinate + NADP(+) = 3-oxoglycyrrhetinate + H(+) + NADPH.
15-hydroxyprostaglandin-I dehydrogenase (NADP(+))
NADP(+) + prostaglandin I2 = 15-dehydro-prostaglandin I2 + H(+) + NADPH.
15-hydroxyicosatetraenoate dehydrogenase
(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + NAD(+) = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADH.
(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + NADP(+) = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADPH.
Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine.
an N-acyl-D-mannosamine + NAD(+) = an N-acyl-D-mannosaminolactone + H(+) + NADH.
Involved in the biosynthesis of 3-deoxyanthocyanidins from flavanones such as naringenin or eriodictyol.
(2S)-flavan-4-ol + NADP(+) = (2S)-flavanone + H(+) + NADPH.
Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic deoxycoformycin.
coformycin + NADP(+) = 8-oxocoformycin + H(+) + NADPH.
pseudotropine forming tropinone reductase
Represents, along with EC 1.1.1.206, a branch point in tropane alkaloid metabolism.
NADP(+) + pseudotropine = H(+) + NADPH + tropinone.
The enzyme participates in the biosynthesis of rosmarinic acid.
It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.
(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NADP(+) = 3-(4-hydroxyphenyl)pyruvate + H(+) + NADPH.
(2R)-3-(3,4-dihydroxyphenyl)lactate + NAD(+) = 3-(3,4-dihydroxyphenyl)pyruvate + H(+) + NADH.
(2R)-3-(3,4-dihydroxyphenyl)lactate + NADP(+) = 3-(3,4-dihydroxyphenyl)pyruvate + H(+) + NADPH.
Acts on a number of bile acids, both in their free and conjugated forms.
3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP(+) = 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + H(+) + NADPH.
3alpha-(17beta)-hydroxysteroid dehydrogenase (NAD(+))
Also acts on other 17beta-hydroxysteroids, on the 3alpha-hydroxy group of pregnanes and bile acids.
Different from EC 1.1.1.50 or EC 1.1.1.213.
Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine.
Anomeric specificity was tested with N-acetyl-D-glucosamine, and it was shown that the enzyme is specific for the alpha anomer.
H2O + N-acetyl-alpha-D-glucosamine + NAD(+) = 2 H(+) + N-acetyl-D-glucosaminate + NADH.
2-exo-hydroxy-1,8-cineole + NAD(+) = 6-oxocineole + H(+) + NADH.
(1S,5R)-carveol + NADP(+) = (R)-carvone + H(+) + NADPH.
methanol + NAD(+) = formaldehyde + H(+) + NADH.
Also oxidizes some other alicyclic alcohols and diols.
cyclohexanol + NAD(+) = cyclohexanone + H(+) + NADH.
Catalyzes the reversible reduction of codeinone to codeine, which is a direct precursor of morphine in the opium poppy plant, Papaver somniferum.
codeine + NADP(+) = codeinone + H(+) + NADPH.
Catalyzes the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.
(7S)-salutaridinol + NADP(+) = H(+) + NADPH + salutaridine.
D-arabinitol 2-dehydrogenase (ribulose-forming)
D-arabinitol + NAD(+) = D-ribulose + H(+) + NADH.
The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway.
galactitol 1-phosphate + NAD(+) = H(+) + keto-D-tagatose 6-phosphate + NADH.
Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces 1,3,8-trihydroxynaphthalene to vermelone.
Involved with EC 4.2.1.94 in the biosynthesis of melanin in pathogenic fungi.
NADP(+) + scytalone = H(+) + NADPH + naphthalene-1,3,6,8-tetrol.
Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108.
(S)-carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH.
The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation.
The enzyme is specific for NAD(+) and does not use NADP(+).
D-mannitol + NAD(+) = D-mannose + H(+) + NADH.
Involved in the pathway for fluorene metabolism in Arthrobacter sp.
9H-fluoren-9-ol + NADP(+) = 9H-fluoren-9-one + H(+) + NADPH.
9H-fluoren-9-ol + NAD(+) = 9H-fluoren-9-one + H(+) + NADH.
4-(hydroxymethyl)benzenesulfonate dehydrogenase
Involved in the toluene-4-sulfonate degradation pathway in Comamonas testosteroni.
4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-formylbenzenesulfonate + H(+) + NADH.
Involved in the cyclohexanol degradation pathway in Acinetobacter NCIB 9871.
6-hydroxyhexanoate + NAD(+) = 6-oxohexanoate + H(+) + NADH.
Involved in the anaerobic pathway of benzoate degradation in bacteria.
3-hydroxy-6-carboxyhexanoyl-CoA + NAD(+) = 3-oxo-6-carboxyhexanoyl-CoA + H(+) + NADH.
Studies on the effects of growth-stage and nutrient supply on the stereochemistry of sulcatone reduction in Clostridia pasteurianum, C. tyrobutyricum and Lactobacillus brevis suggest that there may be at least two sulcatone reductases with different stereospecificities.
NAD(+) + sulcatol = H(+) + NADH + sulcatone.
glycerol-1-phosphate dehydrogenase [NAD(P)(+)]
Responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea.
It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes.
The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP-unsaturated archaeol.
The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine.
Activity of the enzyme is stimulated by K(+).
NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH.
NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADPH.
4-hydroxythreonine-4-phosphate dehydrogenase
4-(phosphohydroxy)-L-threonine dehydrogenase
NAD(+)-dependent threonine 4-phosphate dehydrogenase
The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.
4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl phosphate + CO2 + NADH.
Also reduces pyridine-3-aldehyde and 2,3-butanedione.
Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.
1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH.
The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate.
L-idonate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH.
L-idonate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH.
The enzyme purified from Saccharomyces cerevisiae catalyzes the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.
3-methylbutanol + NADP(+) = 3-methylbutanal + H(+) + NADPH.
3-methylbutanol + NAD(+) = 3-methylbutanal + H(+) + NADH.
The enzymes from the Gram-negative bacteria Actinobacillus actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens.
The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism's S-layer.
The enzyme from E. coli O52 has a higher catalytic efficiency with NADH than with NADPH.
dTDP-alpha-D-fucose + NAD(+) = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(+) + NADH.
dTDP-alpha-D-fucose + NADP(+) = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(+) + NADPH.
1-deoxy-D-xylulose-5-phosphate reductoisomerase
1-deoxyxylulose-5-phosphate reductoisomerase
The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.
The mechanism has been shown to be a retroaldol/aldol reaction.
2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase
Highly specific for (R)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.269, which is highly specific for the (S)-enantiomer.
Forms component III of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
(R)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH.
2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase
Highly specific for (S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, which is highly specific for the (R)-enantiomer.
Forms component IV of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
(2S)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH.
The enzyme acts on multiple 3beta-hydroxysteroids.
Participates in the biosynthesis of zemosterol and cholesterol, where it catalyzes the reaction in the opposite direction to that shown.
The mammalian enzyme is bifunctional and also catalyzes EC 1.1.1.62.
a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH.
4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP(+) = 4alpha-methyl-5alpha-cholest-7-en-3-one + H(+) + NADPH.
3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-methylzymosterol + NADP(+).
Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH.
This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyzes a reversible stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids.
The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency.
a (2R)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + H(+) + NADPH.
(R)-2-hydroxy-4-methylpentanoate + NADP(+) = 4-methyl-2-oxopentanoate + H(+) + NADPH.
Also acts on related alkaloids with an endo-aldehyde group such as vellosimine (same stereochemistry at C-16) but only slight activity with exo-aldehydes (epimeric at C-16).
Detected in many cell suspension cultures of plants from the family Apocynaceae.
10-deoxysarpagine + NADP(+) = H(+) + NADPH + vellosimine.
2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
The enzyme is involved in the catabolism of 2,5-didehydrogluconate.
2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH.
Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds.
(1R,5S)-carveol + NAD(+) = (S)-carvone + H(+) + NADH.
NAD(+) cannot replace NADP(+) (cf. EC 1.1.1.387).
L-serine + NADP(+) = aminoacetaldehyde + CO2 + NADPH.
3beta-hydroxy-5beta-steroid dehydrogenase
3beta-hydroxysteroid 5beta-oxidoreductase
3beta-hydroxysteroid 5beta-progesterone oxidoreductase
3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-3,20-dione + H(+) + NADPH.
3beta-hydroxy-5alpha-steroid dehydrogenase
3beta-hydroxy-5alpha-pregnane-20-one + NADP(+) = 5alpha-pregnane-3,20-dione + H(+) + NADPH.
Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy acid esters.
The (R)- symbol is allotted on the assumption that no substituents change the order of priority from O-3>C-2>C-4.
A subunit of Saccharomyces cerevisiae EC 2.3.1.86.
ethyl (R)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + H(+) + NADPH.
Also acts on 4-oxo- and 5-oxo-fatty acids and their esters.
ethyl (S)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + H(+) + NADPH.
GDP-4-dehydro-6-deoxy-D-mannose reductase
Differs from EC 1.1.1.187 in that the only product formed is GDP-alpha-D-rhamnose (GDP-6-deoxy-alpha-D-mannose).
D-rhamnose is a constituent of lipopolysaccharides of Gram-negative plant and human pathogenic bacteria.
quinate/shikimate dehydrogenase [NAD(P)(+)]
This is the second shikimate dehydrogenase enzyme found in Escherichia coli.
It can use both quinate and shikimate as substrates and either NAD(+) or NADP(+) as acceptor.
The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate.
L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH.
NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH.
methylglyoxal reductase (NADPH-dependent)
The enzyme from the yeast Saccharomyces cerevisiae catalyzes the reduction of a keto group in a number of compounds, forming enantiopure products.
Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde), 3-methylbutanal, hexane-2,5-dione and 3-chloro-1-phenylpropan-1-one.
The enzyme differs from EC 1.1.1.78 which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.
(S)-lactaldehyde + NADP(+) = H(+) + methylglyoxal + NADPH.
S-(hydroxymethyl)glutathione dehydrogenase
formaldehyde dehydrogenase (glutathione)
glutathione-dependent formaldehyde dehydrogenase
NAD- and glutathione-dependent formaldehyde dehydrogenase
NAD-dependent formaldehyde dehydrogenase
The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22.
Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC 3.1.2.12.
Also specifically reduces S-nitrosylglutathione.
NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione.
NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-formylglutathione.
3''-deamino-3''-oxonicotianamine reductase
2'-deoxymugineate + NADP(+) = 3''-deamino-3''-oxonicotianamine + H(+) + NADPH.
2'-deoxymugineate + NAD(+) = 3''-deamino-3''-oxonicotianamine + H(+) + NADH.
isocitrate--homoisocitrate dehydrogenase
homoisocitrate--isocitrate dehydrogenase
Unlike EC 1.1.1.41 and EC 1.1.1.87, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrate.
May play a role in both the lysine and glutamate biosynthesis pathways.
NADP(+)-dependent D-arabinitol dehydrogenase
The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction.
This enzyme carries out the reactions of both EC 1.1.1.11 and EC 1.1.1.250, but unlike them, uses NADP(+) rather than NAD(+) as cofactor.
D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant.
D-arabinitol + NADP(+) = D-xylulose + H(+) + NADPH.
D-arabinitol + NADP(+) = D-ribulose + H(+) + NADPH.
NADP(+) cannot replace NAD(+) and short-chain alcohols such as ethanol, isopropanol, butanol and cyclohexanol cannot replace xanthoxin as substrate.
Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14, EC 1.13.11.51 and EC 1.14.13.93.
2-cis,4-trans-xanthoxin + NAD(+) = 2-cis-(+)-abscisic aldehyde + H(+) + NADH.
The reaction occurs predominantly in the reverse direction.
This enzyme can also convert D-fructose into D-mannitol, but more slowly.
D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH.
This enzyme catalyzes a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate.
The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD(+).
In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyzes the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid.
4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH.
Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri.
(S)-2-hydroxymethylglutarate + NAD(+) = 2-formylglutarate + H(+) + NADH.
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Present in some but not all Rhizobium species.
Differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263).
In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose.
Also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone.
Does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones.
1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH.
Carries out the first step in the conversion of chlorophyll b to chlorophyll a.
Involved in chlorophyll degradation, which occurs during leaf senescence and it also forms part of the chlorophyll cycle, which interconverts chlorophyll a and b in response to changing light conditions.
While both chlorophyll a and chlorophyll b are found in higher plants, only breakdown products derived from chlorophyll a are found in the end products, i.e. non-fluorescent chlorophyll catabolites (NCCs).
The transition from chlorophyll b, which contains a formyl group on C7, to chlorophyll a, which contains a methyl group on C7, proceeds through the intermediate 7(1)-hydroxychlorophyll.
Another enzyme, which requires ferredoxin but has not been characterized fully, is required to complete the conversion.
7(1)-hydroxychlorophyllide a + NAD(+) = chlorophyllide b + H(+) + NADH.
7(1)-hydroxychlorophyllide a + NADP(+) = chlorophyllide b + H(+) + NADPH.
7(1)-hydroxychlorophyll a + NAD(+) = chlorophyll b + H(+) + NADH.
7(1)-hydroxychlorophyll a + NADP(+) = chlorophyll b + H(+) + NADPH.
The rice phytoalexin momilactone A is a diterpenoid secondary metabolite that is involved in the defense mechanism of the plant.
Momilactone A is produced in response to attack by a pathogen through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation.
The enzyme, which catalyzes the last step in the biosynthesis of momilactone A, can use both NAD(+) and NADP(+) but activity is higher with NAD(+).
3beta-hydroxy-9beta-pimara-7,15-dien-19,6beta-olide + NAD(+) = H(+) + momilactone A + NADH.
3beta-hydroxy-9beta-pimara-7,15-dien-19,6beta-olide + NADP(+) = H(+) + momilactone A + NADPH.
This enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 forms part of the carveol and dihydrocarveol degradation pathway.
Accepts all eight stereoisomers of menth-8-en-2-ol as substrate, although some isomers are converted faster than others.
The preferred substrates are (+)-neoisodihydrocarveol, (+)-isodihydrocarveol, (+)-dihydrocarveol and (-)-isodihydrocarveol.
dihydrocarveol + NAD(+) = dihydrocarvone + H(+) + NADH.
(1R,2R,4R)-dihydrocarveol + NAD(+) = (1R,4R)-dihydrocarvone + H(+) + NADH.
(1S,2S,4S)-dihydrocarveol + NAD(+) = (1S,4S)-dihydrocarvone + H(+) + NADH.
(1S,2R,4S)-neodihydrocarveol + NAD(+) = (1S,4S)-dihydrocarvone + H(+) + NADH.
(1R,2S,4R)-neodihydrocarveol + NAD(+) = (1R,4R)-dihydrocarvone + H(+) + NADH.
(1R,2S,4S)-neoisodihydrocarveol + NAD(+) = (1R,4S)-isodihydrocarvone + H(+) + NADH.
(1R,2R,4S)-isodihydrocarveol + NAD(+) = (1R,4S)-isodihydrocarvone + H(+) + NADH.
(1S,2S,4R)-isodihydrocarveol + NAD(+) = (1S,4R)-isodihydrocarvone + H(+) + NADH.
(1S,2R,4R)-neoisodihydrocarveol + NAD(+) = (1S,4R)-isodihydrocarvone + H(+) + NADH.
While the enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 can use both (1S,2S,4R)- and (1R,2R,4S)-menth-8-ene-1,2-diol as substrate, activity is higher with (1S,2S,4R)-menth-8-ene-1,2-diol as substrate.
(1R,2R,4S)-limonene-1,2-diol + NAD(+) = (1R,4S)-1-hydroxylimonen-2-one + H(+) + NADH.
(1S,2S,4R)-limonene-1,2-diol + NAD(+) = (1S,4R)-1-hydroxylimonen-2-one + H(+) + NADH.
3-hydroxypropionate dehydrogenase (NADP(+))
3-hydroxypropanoate dehydrogenase (NADP(+))
Catalyzes the reduction of 3-oxopropanoate to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively.
The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the upstream reaction in the pathway, EC 1.2.1.75.
Different from EC 1.1.1.59 by cofactor preference.
3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + H(+) + NADPH.
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyzes only the reduction of oxaloacetate, and can use NAD(+) and NADP(+) with similar specific activity.
NADP(H)-dependent retinol dehydrogenase/reductase
Greater catalytic efficiency in the reductive direction.
This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary beta-carotene by EC 1.13.11.63.
Km-values for NADP(+) and NADPH are at least 800-fold lower than those for NAD(+) and NADH.
This enzyme differs from EC 1.1.1.105 which prefers NAD(+) and NADH.
all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH.
This enzyme participates in arabinitol catabolism.
The enzyme also converts D-arabinitol 5-phosphate to D-ribulose 5-phosphate at a lower rate.
D-arabinitol 1-phosphate + NAD(+) = D-xylulose 5-phosphate + H(+) + NADH.
2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase
The reaction proceeds in the opposite direction.
A step in riboflavin biosynthesis, NADPH and NADH function equally well as reductant.
Differs from EC 1.1.1.193 since it does not catalyze the reduction of 5-amino-6-ribosylaminopyrimidine-2,4(1H,3H)-dione 5'-phosphate.
2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NAD(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADH.
2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADPH.
diacetyl reductase [(R)-acetoin forming]
The reaction is catalyzed in the reverse direction.
This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76).
While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible.
This enzyme has been reported in the yeast Saccharomyces cerevisiae.
(R)-acetoin + NAD(+) = diacetyl + H(+) + NADH.
diacetyl reductase [(S)-acetoin forming]
This enzyme has been reported in the bacteria Geobacillus stearothermophilus, Enterobacter aerogenes and Klebsiella pneumoniae.
(S)-acetoin + NAD(+) = diacetyl + H(+) + NADH.
UDP-glucuronic acid oxidase (UDP-4-keto-hexauronic acid decarboxylating)
The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13.
NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose.
S-(hydroxymethyl)mycothiol dehydrogenase
mycothiol-dependent formaldehyde dehydrogenase
NAD/factor-dependent formaldehyde dehydrogenase
S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol.
This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.
NAD(+) + S-(hydroxymethyl)mycothiol = H(+) + NADH + S-formylmycothiol.
Xylose reductases catalyze the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway.
Most of the enzymes exhibit a strict requirement for NADPH (cf. EC 1.1.1.431).
However, a few D-xylose reductases, such as those from Neurospora crassa, Yamadazyma tenuis, Scheffersomyces stipitis, and the thermophilic fungus Chaetomium thermophilum, have dual coenzyme specificity, though they still prefer NADPH to NADH.
Very rarely the enzyme prefers NADH (cf. EC 1.1.1.430).
NAD(+) + xylitol = D-xylose + H(+) + NADH.
NADP(+) + xylitol = D-xylose + H(+) + NADPH.
dihydroxypropanesulfonate 3-dehydrogenase
The enzyme is involved in degradation of (R)-2,3-dihydroxypropanesulfonate.
(2R)-3-sulfopropanediol + H2O + 2 NAD(+) = (2R)-3-sulfolactate + 3 H(+) + 2 NADH.
The enzyme from Streptomyces viridochromogenes catalyzes a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate.
The preferred cofactor is NADH, lower activity with NADPH.
2-hydroxyethylphosphonate + NAD(+) = H(+) + NADH + phosphonoacetaldehyde.
This enzyme, isolated from the bacterium Chromohalobacter salexigens DSM 3043, acts only on the (S)-enantiomer of 3-sulfolactate.
Combined with EC 1.1.1.338, it provides a racemase system that converts (2S)-3-sulfolactate to (2R)-3-sulfolactate, which is degraded further by EC 4.4.1.24.
(2S)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) + NADH.
The enzyme is involved in degradation of ethylbenzene.
(S)-1-phenylethanol + NAD(+) = acetophenone + H(+) + NADH.
2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD(+) can replace NADP(+), but with lower affinity.
The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate.
However, later studies showed that the substrate is the hemiacetal form, and the product is 2-oxo-2H-pyran-4,6-dicarboxylate.
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) = 2-oxo-2H-pyran-4,6-dicarboxylate + H(+) + NADPH.
Catalyzes the reaction only in the opposite direction.
The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyze this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD).
The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433.
2-hydroxyethane-1-sulfonate + NADP(+) = H(+) + NADPH + sulfoacetaldehyde.
This enzyme, abundant in the retinal pigment epithelium, catalyzes the reduction of 11-cis-retinol to 11-cis-retinal while the substrate is bound to the retinal-binding protein.
This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin.
The enzyme can also accept other cis forms of retinol.
11-cis-retinol--[retinol-binding protein] + NAD(+) = 11-cis-retinal--[retinol-binding protein] + H(+) + NADH.
11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH.
The enzyme catalyzes a step in the ascorbate biosynthesis in higher plants (Smirnoff-Wheeler pathway).
The activity with NADP(+) is less than 10% of the activity with NAD(+).
L-galactose + NAD(+) = H(+) + L-galactono-1,4-lactone + NADH.
The biosynthesis of raucaffrinoline from perakine is a side route of the ajmaline biosynthesis pathway.
The enzyme is a member of the aldo-keto reductase enzyme superfamily from higher plants.
NADP(+) + raucaffrinoline = H(+) + NADPH + perakine.
The enzyme acts in the opposite direction.
The enzymes from the plants Ocimum basilicum (sweet basil), Clarkia breweri and Petunia hybrida only accept coniferyl acetate and form eugenol.
The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate.
The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH.
a carboxylate + eugenol + NADP(+) = a coniferyl ester + NADPH.
acetate + eugenol + NADP(+) = (E)-coniferyl acetate + NADPH.
In Ocimum basilicum (sweet basil), Clarkia breweri, and Petunia hybrida only isoeugenol is formed.
However in Pimpinella anisum (anise) only anol is formed in vivo, although the cloned enzyme does produce isoeugenol.
acetate + NADP(+) + trans-isoeugenol = (E)-coniferyl acetate + NADPH.
acetate + NADP(+) + trans-anol = NADPH + trans-coumaryl acetate.
The enzyme also reduces 1-phenylpropane-1,2-dione.
The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency.
(S)-benzoin + NADP(+) = benzil + H(+) + NADPH.
2-hydroxy-1-phenyl-1-propanone + NADP(+) = 1-phenyl-1,2-propanedione + H(+) + NADPH.
The enzyme from the bacterium Xanthomonas oryzae is able to reduce enantioselectively only one of the two carbonyl groups of benzil to give optically active (R)-benzoin.
(R)-benzoin + NADP(+) = benzil + H(+) + NADPH.
Isolated from the plant Foeniculum vulgare (fennel).
(1S,2S,4R)-endo-fenchol + NAD(+) = (1S,4R)-fenchone + H(+) + NADH.
(1S,2S,4R)-endo-fenchol + NADP(+) = (1S,4R)-fenchone + H(+) + NADPH.
Isolated from the plant Tanacetum vulgare (tansy).
(+)-thujan-3-ol + NADP(+) = (+)-thujan-3-one + H(+) + NADPH.
(+)-thujan-3-ol + NAD(+) = (+)-thujan-3-one + H(+) + NADH.
The enzyme catalyzes the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol.
Also acts on geraniol, nerol and citronellol.
The recommended numbering of geraniol gives 8-hydroxygeraniol as the substrate rather than 10-hydroxygeraniol.
(6E)-8-hydroxygeraniol + 2 NADP(+) = (6E)-8-oxogeranial + 2 H(+) + 2 NADPH.
sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
This enzyme, isolated from the bacterium Chlorobium tepidum, catalyzes the final step in the de novo synthesis of tetrahydrobiopterin from GTP.
L-threo-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH + sepiapterin.
L-threo-tetrahydrobiopterin + 2 NADP(+) = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH.
The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
10-hydroxy-alpha-humulene + NAD(+) = H(+) + NADH + zerumbone.
Isolated from Pseudomonas putida, and involved in degradation of (+)-camphor.
(1R,4R,5R)-5-hydroxycamphor + NAD(+) = (1R,4R)-bornane-2,5-dione + H(+) + NADH.
The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyzes the reduction of 'nicotine blue' to its hydroquinone form (the opposite direction from that shown).
Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway.
The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species.
The enzyme possesses a slight preference for NADH over NADPH.
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin.
2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy-scyllo-inosose + H(+) + NADPH.
2-deoxy-scyllo-inosamine + NAD(+) = 3-amino-2,3-dideoxy-scyllo-inosose + H(+) + NADH.
very-long-chain 3-ketoacyl-CoA reductase
very-long-chain beta-ketoacyl-CoA reductase
The second component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs.
The enzyme is active with substrates with chain length of C16 to C34, depending on the species.
a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH.
Isolated from the plants Forsythia intermedia and Podophyllum peltatum.
An intermediate lactol is detected in vitro.
(-)-secoisolariciresinol + 2 NAD(+) = (-)-matairesinol + 2 H(+) + 2 NADH.
The enzyme catalyzes a step in the pathway of ergot alkaloid biosynthesis in certain fungi.
chanoclavine-I + NAD(+) = chanoclavine-I aldehyde + H(+) + NADH.
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase
decaprenylphospho-beta-D-ribofuranose 2'-epimerase
The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, in the epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis-decaprenylphospho-beta-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
NAD(+) + trans,octa-cis-decaprenylphospho-beta-D-arabinofuranose = H(+) + NADH + trans,octa-cis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose.
The enzyme from the plant Erythroxylum coca catalyzes the penultimate step in the biosynthesis of cocaine.
In vivo the reaction proceeds in the opposite direction.
With NADH instead of NADPH the reaction rate is reduced to 14%.
The enzyme also reduces tropinone, nortropinone and 6-hydroxytropinone but with lower reaction rates.
ecgonine methyl ester + NADP(+) = ecgonone methyl ester + H(+) + NADPH.
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalyzing the next step the pathway (EC 2.6.1.98).
The enzyme also possesses an EC 1.1.99.2 activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD(+).
The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD(+) as tightly and do not require 2-oxoglutarate to function.
NAD(+) + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate = H(+) + NADH + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate.
UDP-N-acetyl-D-mannosamine dehydrogenase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea.
The enzyme has no activity with NADP(+).
H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-mannosamine = 3 H(+) + 2 NADH + UDP-N-acetyl-alpha-D-mannosaminouronate.
L-2-hydroxycarboxylate dehydrogenase (NAD(+))
The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple L-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate.
Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH.
(2R)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) + NADH.
(2R)-3-sulfolactate dehydrogenase (NADP(+))
The enzyme from the bacterium Chromohalobacter salexigens can only utilize NADP(+).
It functions both biosynthetically in coenzyme M biosynthesis and degradatively, in the degradation of sulfolactate.
It can not use (S)-malate and (S)-lactate.
(2R)-3-sulfolactate + NADP(+) = 3-sulfopyruvate + H(+) + NADPH.
dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD(+))
The enzyme has been characterized from the bacterium Aggregatibacter actinomycetemcomitans, in which it participates in the biosynthesis of the serotype c-specific polysaccharide antigen.
dTDP-6-deoxy-beta-L-talose + NAD(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADH.
1-deoxy-11beta-hydroxypentalenate dehydrogenase
1-deoxy-11beta-hydroxypentalenic acid dehydrogenase
Isolated from the bacterium Streptomyces avermitilis and present in many other Streptomyces species.
Part of the pathway for pentalenolactone biosynthesis.
1-deoxy-11beta-hydroxypentalenate + NAD(+) = 1-deoxy-11-oxopentalenate + H(+) + NADH.
Isolated from Yersinia pseudotuberculosis and Salmonella enterica.
CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH.
The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria.
Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi).
CDP-alpha-D-paratose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H(+) + NADPH.
phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)
The enzyme catalyzes both the oxidation and decarboxylation of 6-phospho-D-gluconate.
In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway.
6-phospho-D-gluconate + NAD(+) = CO2 + D-ribulose 5-phosphate + NADH.
dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)(+)]
The enzyme works equally well with NAD(+) and NADP(+).
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain.
The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate).
a (2R)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH.
(R)-2-hydroxy-4-methylpentanoate + NAD(+) = 4-methyl-2-oxopentanoate + H(+) + NADH.
2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
The enzyme is involved in ketogluconate metabolism, and catalyzes the reaction in vivo in the reverse direction to that shown.
It is used in the commercial microbial production of ascorbate.
2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate + H(+) + NADPH.
The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol.
The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol.
(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH.
This plant enzyme participates in the biosynthesis of the pterocarpan phytoalexins medicarpin, maackiain, and several forms of glyceollin.
The enzyme has a strict stereo specificity for the 3R-isoflavanones.
a (3R,4R)-4,2'-dihydroxyisoflavan + NADP(+) = a (3R)-2'-hydroxyisoflavanone + H(+) + NADPH.
(3R,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol + NADP(+) = (3R)-vestitone + H(+) + NADPH.
Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.
(1'S)-averantin + NADP(+) = H(+) + NADPH + norsolorinic acid.
The enzyme from the bacterium Escherichia coli is specific for NAD(+).
phosphogluconate dehydrogenase [NAD(P)(+)-dependent, decarboxylating]
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions.
Unlike EC 1.1.1.44, it is not specific for NADP(+) and can accept both cofactors with similar efficiency.
Isolated from the aflatoxin-producing mold Aspergillus parasiticus.
5'-oxoaverantin will spontaneously form averufin by intramolecular ketalisation.
(1'S,5'S)-5'-hydroxyaverantin + NAD(+) = (S)-5'-oxoaverantin + H(+) + NADH.
(1'S,5'R)-5'-hydroxyaverantin + NAD(+) = (S)-5'-oxoaverantin + 2 H(+) + NADH.
Isolated from the mold Aspergillus parasiticus.
Involved in a metabolic grid that leads to aflatoxin biosynthesis.
(2S)-versicolorone + NADP(+) = 1'-hydroxyversicolorone + H(+) + NADPH.
(3S)-versiconol acetate + NADP(+) = (2S,3S)-versiconal hemiacetal acetate + H(+) + NADPH.
(S)-versiconol + NADP(+) = (2S-3S)-versiconal hemiacetal + H(+) + NADPH.
The enzyme from the prune mite Carpoglyphus lactis also acts on geraniol with greater activity (cf. 1.1.1.347).
Unlike EC 1.1.1.216, this enzyme cannot use NADP(+) as cofactor.
(2E,6E)-farnesol + NAD(+) = (2E,6E)-farnesal + H(+) + NADH.
Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of kanamycin B to kanamycin A.
2'-dehydrokanamycin A + H(+) + NADPH = kanamycin A + NADP(+).
The enzyme is involved in biosynthesis of L-colitose, a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides, where it catalyzes the reaction in the reverse direction.
The enzyme also performs the NAD(P)H-dependent epimerisation at C-5 of the sugar.
The enzyme from Yersinia pseudotuberculosis is Si-specific with respect to NAD(P)H.
GDP-beta-L-colitose + NADP(+) = GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + H(+) + NADPH.
GDP-beta-L-colitose + NAD(+) = GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + H(+) + NADH.
The enzyme acts on multiple 3alpha-hydroxysteroids, such as androsterone and 5 alpha-dihydrotestosterone.
The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation.
This entry stands for enzymes whose stereo-specificity with respect to NAD(+) or NADP(+) is not known (cf. EC 1.1.1.50 and EC 1.1.1.213).
The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5).
This entry covers enzymes whose stereo specificity for NADP(+) is not known (cf. EC 1.1.1.168 and EC 1.1.1.214).
The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity toward aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD(+) and NADP(+) with similar catalytic efficiency.
It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
an aldopyranose + NADP(+) = aldono-1,5-lactone + H(+) + NADPH.
D-galactose + NAD(+) = D-galactono-1,5-lactone + H(+) + NADH.
dual-specific glucose/galactose dehydrogenase
The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway.
It shows 20-fold higher activity with NADP(+) compared to NAD(+).
The oxidation of D-glucose and D-galactose is catalyzed at a comparable rate (cf. EC 1.1.1.119 and EC 1.1.1.120).
The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
D-glucose 6-phosphate + NAD(+) = 3-dehydro-D-glucose 6-phosphate + H(+) + NADH.
The enzyme is involved in the synthesis of the aklavinone aglycone, a common precursor for several anthracycline antibiotics including aclacinomycins, daunorubicin and doxorubicin.
The enzyme from the Gram-negative bacterium Streptomyces sp. C5 produces daunomycin.
aklavinone + NADP(+) = aklaviketone + 2 H(+) + NADPH.
glucose-6-phosphate dehydrogenase [NAD(P)(+)]
The enzyme from the Gram-positive bacterium Leuconostoc mesenteroides prefers NADP(+) while the enzyme from the Gram-negative bacterium Gluconacetobacter xylinus prefers NAD(+).
D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADH.
dTDP-4-dehydro-6-deoxy-alpha-D-gulose 4-ketoreductase
The enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II.
dTDP-6-deoxy-alpha-D-allose + NAD(+) = dTDP-4-dehydro-6-deoxy-alpha-D-allose + H(+) + NADH.
dTDP-6-deoxy-alpha-D-allose + NADP(+) = dTDP-4-dehydro-6-deoxy-alpha-D-allose + H(+) + NADPH.
The enzyme from plants is involved in ascorbic acid (vitamin C) biosynthesis.
The enzyme from the fungus Trichoderma reesei (Hypocrea jecorina) is involved in a eukaryotic degradation pathway of D-galacturonate.
It is also active with D-glucuronate and glyceraldehyde.
Neither enzyme shows any activity with NADH.
L-galactonate + NADP(+) = aldehydo-D-galacturonate + H(+) + NADPH.
Involved in the catabolism of ascorbate (vitamin C) to tartrate.
No activity is observed with NADP(+) (cf. EC 1.1.1.264).
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose reductase
Part of the biosynthesis of UDP-N-acetyl-L-fucosamine.
Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus.
H(+) + NADPH + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose = NADP(+) + UDP-2-acetamido-2,6-dideoxy-beta-L-talose.
H(+) + NADH + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose = NAD(+) + UDP-2-acetamido-2,6-dideoxy-beta-L-talose.
6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
The enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria such as Thauera aromatica.
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD(+) = 6-oxocyclohex-1-ene-1-carbonyl-CoA + H(+) + NADH.
The enzyme, found in the bacterium Bacillus subtilis, also catalyzes the reaction of EC 1.1.1.18 and can also use D-glucose and D-xylose.
It shows trace activity with D-ribose and D-fructose.
It is part of a myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
1D-chiro-inositol + NAD(+) = H(+) + NADH + scyllo-inosine.
scyllo-inositol 2-dehydrogenase (NAD(+))
The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP(+) (cf. EC 1.1.1.371).
It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.
NAD(+) + scyllo-inositol = H(+) + NADH + scyllo-inosose.
scyllo-inositol 2-dehydrogenase (NADP(+))
The enzyme, found in the bacterium Bacillus subtilis, has no activity with NAD(+) (cf. EC 1.1.1.370).
NADP(+) + scyllo-inositol = H(+) + NADPH + scyllo-inosose.
The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina).
It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal.
The reaction is only observed in the direction of glyceraldehyde reduction.
glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH.
The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
(2S)-3-sulfopropanediol + NAD(+) = (2S)-3-sulfolactaldehyde + H(+) + NADH.
NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + NADH + UDP-2-acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose.
L-2-hydroxycarboxylate dehydrogenase [NAD(P)(+)]
The enzyme from the archaeon Methanocaldococcus jannaschii catalyzes the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates).
The enzyme can use both NADH and NADPH, although activity is higher with NADPH.
The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP(+).
The same organism also possesses an NAD(+)-specific enzyme with similar activity, cf. EC 1.1.1.337.
a (2S)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + H(+) + NADPH.
The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP(+) over NAD(+).
In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.
The enzyme is specific for alpha-L-arabinopyranose.
alpha-L-arabinopyanose + NADP(+) = H(+) + L-arabinono-1,4-lactone + NADPH.
The enzyme from the archaeon Thermoplasma acidophilum is part of the non-phosphorylative degradation pathway for L-rhamnose.
The enzyme differs in cofactor specificity from EC 1.1.1.173, which is specific for NAD(+).
L-rhamnofuranose + NADP(+) = H(+) + L-rhamnono-1,4-lactone + NADPH.
The enzyme, which occurs in the bacteria Azotobacter vinelandii and Sphingomonas sp. SKA58, is part of the non-phosphorylative degradation pathway for L-rhamnose.
The enzyme differs in cofactor specificity from EC 1.1.1.173, which is specific for NAD(+) and EC 1.1.1.377.
The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate.
The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31).
The enzyme transfers the pro-R hydrogen from NADH.
(R)-mandelate + NAD(+) = H(+) + NADH + phenylglyoxylate.
The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.
L-gulonate + NAD(+) = H(+) + keto-D-fructuronate + NADH.
The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids.
The highest activity is seen with L-allo-threonine and D-threonine.
The enzyme from E. coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate.
The enzyme has no activity with NAD(+) or L-threonine (cf. EC 1.1.1.103).
L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH.
The enzyme, characterized from the bacteria Thermacetogenium phaeum and Desulfococcus oleovorans and from the archaeon Archaeoglobus fulgidus, is specific for NADH (cf. EC 1.1.1.86 and EC 1.1.1.383).
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH.
The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency (cf. EC 1.1.1.86 and EC 1.1.1.382).
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose 3-oxidoreductase
dTDP-4-keto-2,6-dideoxy-D-glucose 3-oxidoreductase
The enzyme is involved in the biosynthesis of several deoxysugars, including L-digitoxose, L- and D-olivose, L-oliose, D-mycarose and forosamine.
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH.
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin.
L-dihydroanticapsin + NAD(+) = H(+) + L-anticapsin + NADH.
The enzyme is involved in pheromone production by the pine engraver beetle, Ips pini.
(4R)-ipsdienol + NADP(+) = H(+) + ipsdienone + NADPH.
(4R)-ipsdienol + NAD(+) = H(+) + ipsdienone + NADH.
The enzyme, purified from the bacterium Pseudomonas aeruginosa, also shows activity with L-threonine (cf. EC 1.1.1.103).
The enzyme has only very low activity with NADP(+) (cf. EC 1.1.1.276).
L-serine + NAD(+) = aminoacetaldehyde + CO2 + NADH.
glucose-6-phosphate dehydrogenase (NAD(+))
The enzyme from the archaeon Haloferax volcanii is specific for NAD(+).
2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase
The enzyme, characterized from agarose-degrading bacteria, is involved in a degradation pathway for 3,6-anhydro-alpha-L-galactopyranose, a major component of the polysaccharides of red macroalgae.
2-dehydro-3-deoxy-L-galactonate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH.
The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway.
Activity with NADP(+) is only 4% of that with NAD(+).
6-sulfo-D-quinovose + NAD(+) = 6-deoxy-6-sulfo-D-glucono-1,5-lactone + H(+) + NADH.
3beta-hydroxycholanate 3-dehydrogenase (NAD(+))
This bacterial enzyme is involved, along with EC 1.1.1.52 or EC 1.1.1.392, in the modification of secondary bile acids to form 3beta-bile acids (also known as iso-bile acids).
The enzyme catalyzes the reaction in the reduction direction in vivo.
3-oxo-5beta-cholan-24-oate + H(+) + NADH = isolithocholate + NAD(+).
3alpha-hydroxycholanate dehydrogenase (NADP(+))
This bacterial enzyme is involved in the modification of secondary bile acids to form 3beta-bile acids (also known as iso-bile acids) via a 3-oxo intermediate.
The enzyme catalyzes a reversible reaction in vitro.
lithocholate + NADP(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADPH.
3beta-hydroxycholanate 3-dehydrogenase (NADP(+))
3-oxo-5beta-cholan-24-oate + H(+) + NADPH = isolithocholate + NADP(+).
The enzyme from the bacterium Stigmatella aurantiaca catalyzes the final step in the conversion of aurachin C to aurachin B.
In vivo the enzyme catalyzes the reduction of 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline-1-oxide to form 2-methyl-1-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline-3,4-diol (note that the reactions written above proceed from right to left), which then undergoes a spontaneous dehydration to form aurachin B.
aurachin B + H2O + NAD(+) = 4-hydroxy-2-methyl-3-oxo-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH.
3alpha-hydroxybile acid CoA 3-dehydrogenase
This bacterial enzyme is involved in the 7-dehydroxylation process associated with bile acid degradation.
The enzyme has very little activity with unconjugated bile acid substrates.
It has similar activity with choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA.
a 3alpha-hydroxy bile acid CoA + NAD(+) = a 3-oxo bile acid CoA + H(+) + NADH.
choloyl-CoA + NAD(+) = 7alpha,12alpha-dihydroxy-3-oxochol-24-oyl-CoA + H(+) + NADH.
chenodeoxycholoyl-CoA + NAD(+) = 7alpha-hydroxy-3-oxochol-24-oyl-CoA + H(+) + NADH.
deoxycholoyl-CoA + NAD(+) = 12alpha-hydroxy-3-oxocholan-24-oyl-CoA + H(+) + NADH.
lithocholoyl-CoA + NAD(+) = 3-oxocholan-24-oyl-CoA + H(+) + NADH.
The enzyme, together with EC 1.3.7.15 and EC 4.2.1.165, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a.
The enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a.
The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD(+) = bacteriochlorophyllide a + H(+) + NADH.
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + NAD(+) = 3-acetyl-3-devinylchlorophyllide a + H(+) + NADH.
The enzyme, characterized from the bacterium Streptomyces griseus, participates in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial EC 6.1.1.2.
(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD(+) = (R)-3-(indol-3-yl)-2-oxobutanoate + H(+) + NADH.
2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase
4-hydroxy-3-glutathionyl-3-methylbut-1-ene dehydrogenase
The enzyme, characterized from the bacterium Rhodococcus sp. AD45, is involved in isoprene degradation.
2-glutathionyl-2-methylbut-3-en-1-ol + H2O + 2 NAD(+) = 2-glutathionyl-2-methylbut-3-enoate + 3 H(+) + 2 NADH.
The enzyme catalyzes a reversible reaction.
The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate.
The SerA enzyme from Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95.
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH.
This bacterial enzyme is involved in the degradation pathways of the alkene 2-methylpropene and the fuel oxygenate methyl tert-butyl ether (MTBE), a widely occurring groundwater contaminant.
2-methylpropane-1,2-diol + NAD(+) = 2-hydroxy-2-methylpropanal + H(+) + NADH.
2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD(+))
2-keto-3-deoxy-L-rhamnonate dehydrogenase
The enzyme, characterized from the bacteria Sphingomonas sp. SKA58 and Sulfobacillus thermosulfidooxidans, is involved in the non-phosphorylative degradation pathway for L-rhamnose.
It does not show any detectable activity with NADP(+) or with other aldoses.
2-dehydro-3-deoxy-L-rhamnonate + NAD(+) = 2,4-didehydro-3-deoxy-L-rhamnonate + H(+) + NADH.
The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism.
D-erythritol 1-phosphate + NADP(+) = D-erythrulose 1-phosphate + H(+) + NADPH.
The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of D-threitol.
D-threitol + NAD(+) = D-erythrulose + H(+) + NADH.
The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.
2,3,5,6-tetrachlorohydroquinone + H(+) + NAD(+) = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH.
ribitol-5-phosphate 2-dehydrogenase (NADP(+))
The enzyme, characterized in bacteria, is specific for NADP.
It is part of the synthesis pathway of CDP-ribitol.
In Haemophilus influenzae it is part of a multifunctional enzyme also catalyzing EC 2.7.7.40.
galactitol 2-dehydrogenase (L-tagatose-forming)
The enzyme, characterized in the bacterium Rhodobacter sphaeroides has a wide substrate specificity.
In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde.
The enzyme does show activity with D-tagatose (cf. EC 1.1.1.16).
galactitol + NAD(+) = H(+) + keto-L-tagatose + NADH.
The enzyme, characterized in Agrobacterium fabrum C58, also has low activity with D-mannitol and D-arabitol.
It is part of a D-altritol degradation pathway.
D-altritol + NAD(+) = H(+) + keto-D-tagatose + NADH.
The enzyme, characterized from bacteria, is involved in a pathway for D-threonate catabolism.
4-O-phospho-D-threonate + NAD(+) = CO2 + dihydroxyacetone phosphate + NADH.
The enzyme, characterized from bacteria, is involved in a pathway for D-erythronate catabolism.
4-phospho-D-erythronate + NAD(+) = CO2 + dihydroxyacetone phosphate + NADH.
The enzyme, characterized from bacteria, is involved in D-erythronate catabolism.
D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) + NADH.
The enzyme, characterized from bacteria, is involved in L-threonate catabolism.
L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH.
The enzyme, found in certain bacterial species, is part of a pathway for the production of olefins.
a (2R,3S)-2-alkyl-3-hydroxyalkanoate + NADP(+) = an (R)-2-alkyl-3-oxoalkanoate + H(+) + NADPH.
A-factor type gamma-butyrolactone 1'-reductase (1S-forming)
The enzyme, which is found in bacteria that produce virginiae-butanolide (VB) type gamma-butyrolactone autoregulators, reduces its substrate stereospecifically, forming a hydroxyl group in the (S) configuration.
a (3R,4R)-3-[(1S)-1-hydroxyalkyl]-4-(hydroxymethyl)oxolan-2-one + NADP(+) = a (3R,4R)-3-alkanoyl-4-(hydroxymethyl)oxolan-2-one + H(+) + NADPH.
The enzyme, reported from the human gut bacteria Escherichia coli and Bacteroides vulgatus, participates in an L-galactonate degradation pathway.
L-galactonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH.
The enzyme, characterized from the plant Papaver somniferum (opium poppy), catalyzes the last step in the biosynthesis of the isoquinoline alkaloid noscapine.
NAD(+) + narcotine hemiacetal = H(+) + NADH + noscapine.
isopyridoxal dehydrogenase (5-pyridoxolactone-forming)
The enzyme, characterized from the bacterium Arthrobacter sp Cr-7, participates in the degradation of pyridoxine.
The enzyme also catalyzes the activity of EC 1.2.1.102.
isopyridoxal + NAD(+) = 5-pyridoxolactone + H(+) + NADH.
3beta-hydroxysteroid-4beta-carboxylate 3-dehydrogenase (decarboxylating)
This bacterial enzyme participates in the biosynthesis of bacterial sterols.
Together with EC 1.14.13.246 (SdmA) it forms an enzyme system that removes one methyl group from the C-4 position of 4,4-dimethylated steroid molecules.
SdmA catalyzes three successive oxidations of the C-4beta methyl group, turning it into a carboxylate group; SdmB is a bifunctional enzyme that catalyzes two different activities.
As EC 1.1.1.417 it catalyzes an oxidative decarboxylation that results in reduction of the 3beta-hydroxy group at the C-3 carbon to an oxo group.
As EC 1.1.1.270, it reduces the 3-oxo group back to a 3beta-hydroxyl.
Since the remaining methyl group at C-4 is in an alpha orientation, it cannot serve as a substrate for a second round of demethylation by this system.
a 3beta-hydroxy-4alpha-methylsteroid-4beta-carboxylate + NAD(+) = a 4alpha-methyl-3-oxosteroid + CO2 + NADH.
a 3beta-hydroxy-4alpha-methylsteroid-4beta-carboxylate + NADP(+) = a 4alpha-methyl-3-oxosteroid + CO2 + NADPH.
4beta-carboxy-4alpha-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NAD(+) = 3-dehydro-4alpha-methylzymosterol + CO2 + NADH.
4beta-carboxy-4alpha-methyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 3-dehydro-4alpha-methylzymosterol + CO2 + NADPH.
plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)
3beta-hydroxysteroid dehydrogenases/C-4 decarboxylase
The enzyme, found in plants, catalyzes multiple reactions during plant sterol biosynthesis.
Unlike the fungal/animal enzyme EC 1.1.1.170 the plant enzyme is specific for NAD(+).
4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(24(1))-en-3beta-ol + NAD(+) = CO2 + cycloeucalenone + NADH.
The enzyme, characterized from the plant Nepeta mussinii, binds an NAD(+) cofactor.
It also catalyzes the activity of EC 5.5.1.34.
cis-cis-nepetalactol + NAD(+) = cis-cis-nepetalactone + H(+) + NADH.
cis-trans-nepetalactol + NAD(+) = cis-trans-nepetalactone + H(+) + NADH.
The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.
D-apiofuranose + NAD(+) = D-apionolactone + H(+) + NADH.
The enzyme, characterized from several bacterial species, participates in the degradation of D-apionate.
The reaction involves migration of a hydroxymethyl group from position 3 to position 2 and oxidation of the 3-hydroxyl group.
Stereospecificity of the product, 3-oxoisoapionate, has not been determined.
D-apionate + NAD(+) = 3-oxoisoapionate + H(+) + NADH.
The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters.
It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity.
In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial.
The enzyme exhibits a strict anti-Prelog enantioselectivity.
When acting on diketones, it catalyzes the reduction of only the keto group closest to the ring, with no further reduction to the diol.
(1S,2S)-pseudoephedrine + NAD(+) = (S)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.
(1S,2R)-ephedrine + NAD(+) = (R)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.
(S)-phenylacetylcarbinol + NAD(+) = 1-phenyl-1,2-propanedione + H(+) + NADH.
It exhibits a strict enantioselectivity and accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity.
(1R,2S)-ephedrine + NAD(+) = (S)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.
(1R,2R)-pseudoephedrine + NAD(+) = (R)-2-methylamino-1-phenylpropan-1-one + H(+) + NADH.
(R)-phenylacetylcarbinol + NAD(+) = 1-phenyl-1,2-propanedione + H(+) + NADH.
D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,4-lactone-forming)
The enzyme, which participates in the degradation of D-xylose, has been characterized from several halophilic archaeal species.
D-xylofuranose + NADP(+) = D-xylono-1,4-lactone + H(+) + NADPH.
1,6-anhydro-beta-D-glucose dehydrogenase
Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning.
This enzyme is present only in bacteria, and has been characterized from Arthrobacter sp. I-552 and Pseudarthrobacter phenanthrenivorans.
levoglucosan + NAD(+) = 3-dehydrolevoglucosan + H(+) + NADH.
UDP-N-acetyl-alpha-D-quinovosamine dehydrogenase
The enzyme participates in the biosynthesis of N-acetyl-alpha-D-quinovosamine, a 6-deoxy sugar that is present in the O antigens of many Gram-negative bacteria, including Pseudomonas aeruginosa serotypes O6 and O10, Rhizobium etli, and Brucella abortus.
NADP(+) + UDP-N-acetyl-alpha-D-quinovosamine = H(+) + NADPH + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.
NAD(+) + UDP-N-acetyl-alpha-D-quinovosamine = H(+) + NADH + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.
The enzyme from the archaeon Saccharolobus solfataricus is tetrameric and contains zinc.
In contrast to EC 1.1.1.116 and EC 1.1.1.117, this enzyme is specific for NADP(+).
4-methylthio 2-oxobutanoate reductase (NADH)
4-methylthio 2-oxobutyric acid reductase
The substrate of this enzyme is formed as an intermediate during L-methionine salvage from S-methyl-5'-thioadenosine, which is formed during the biosynthesis of polyamines.
The human enzyme also functions as a transcriptional co-regulator that downregulates the expression of many tumor-suppressor genes, thus providing a link between gene repression and the methionine salvage pathway.
A similar, but NADP-specific, enzyme is involved in dimethylsulfoniopropanoate biosynthesis in algae and phytoplankton.
(2R)-2-hydroxy-4-(methylsulfanyl)butanoate + NAD(+) = 4-methylsulfanyl-2-oxobutanoate + H(+) + NADH.
(2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase
The enzyme, purified from the bacterium Thauera aromatica, is involved in an anaerobic toluene degradation pathway.
(2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA + NAD(+) = (S)-2-benzoylsuccinyl-CoA + H(+) + NADH.
Catalyzes the oxidation of carveol to carvone, with a strong stereoselectivity since it efficiently converts only the (6S)-stereoisomers, of which (-)-(4R,6S)-trans-carveol is the better substrate.
Displays a broad substrate specificity with a preference for substituted cyclohexanols, and does not catalyze the oxidation of primary or short chain aliphatic secondary alcohols.
Is also able, albeit more slowly, to oxidize limonene-1,2-diol into 1-hydroxy-2-oxolimonene.
(1S,5R)-carveol + NAD(+) = (R)-carvone + H(+) + NADH.
(1S,5S)-carveol + NAD(+) = (S)-carvone + H(+) + NADH.
The enzyme from Methanocaldococcus jannaschii also catalyzes the reaction of EC 1.1.1.85 and EC 1.1.1.83.
(2R,3S)-3-methylmalate + NAD(+) = 2-oxobutanoate + CO2 + NADH.
4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate semialdehyde.
a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH.
Acts on polyols with a D-lyxo configuration, such as D-mannitol and D-sorbitol.
D-mannitol + 2 Fe(III)-[cytochrome c] = D-fructose + 2 Fe(II)-[cytochrome c] + 2 H(+).
L-lactate ferricytochrome c oxidoreductase
(S)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + pyruvate.
D-lactate ferricytochrome c oxidoreductase
(R)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + pyruvate.
D-lactate dehydrogenase (cytochrome c-553)
The enzyme from the sulfate-reducing bacterium Desulfovibrio vulgaris can also act on (R)-2-hydroxybutanoate.
(R)-lactate + 2 Fe(III)-[cytochrome c553] = 2 Fe(II)-[cytochrome c553] + 2 H(+) + pyruvate.
polyvinyl alcohol dehydrogenase (cytochrome)
The enzyme is involved in bacterial polyvinyl alcohol degradation.
Some Gram-negative bacteria degrade polyvinyl alcohol by importing it into the periplasmic space, where it is oxidized by polyvinyl alcohol dehydrogenase, an enzyme that is coupled to the respiratory chain via cytochrome c.
a polyvinyl alcohol + 2n Fe(III)-[cytochrome c] = an oxidized polyvinyl alcohol + 2n Fe(II)-[cytochrome c] + 2n H(+).
A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria.
It uses the novel specific cytochrome cL as acceptor.
Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde.
Activity is stimulated by ammonia or methylamine.
It is usually assayed with phenazine methosulfate.
Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+).
2 Fe(III)-[cytochrome cL] + methanol = 2 Fe(II)-[cytochrome cL] + formaldehyde + 2 H(+).
A periplasmic PQQ-containing quinoprotein.
Occurs in Pseudomonas and Rhodopseudomonas.
The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor.
Acts on a wide range of primary and secondary alcohols, but not methanol.
It has a homodimeric structure (contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)).
It is routinely assayed with phenazine methosulfate as electron acceptor.
Activity is stimulated by ammonia or amines.
a primary alcohol + 2 Fe(III)-[cytochrome c] = an aldehyde + 2 Fe(II)-[cytochrome c] + 2 H(+).
This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation.
It contains both pyrroloquinoline quinone (PQQ) and heme c prosthetic groups.
butan-1-ol + 2 Fe(III)-[cytochrome c] = butanal + 2 Fe(II)-[cytochrome c] + 2 H(+).
lanthanide-dependent methanol dehydrogenase
Isolated from the bacterium Methylacidiphilum fumariolicum and many Methylobacterium species.
The higher lanthanides show decreasing activity with Sm(3+), Eu(3+) and Gd(3+).
The lanthanide is coordinated by the enzyme and pyrroloquinoline quinone.
Shows little activity with Ca(2+), the required cofactor of EC 1.1.2.7.
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2.
Also oxidizes D-galactose, D-mannose, maltose, lactose and cellobiose.
D-galactose + O2 = D-galactono-1,5-lactone + H2O2.
D-cellobiose + O2 = D-cellobiono-1,5-lactone + H2O2.
D-maltose + O2 = D-maltobiono-1,5-lactone + H2O2.
beta-lactose + O2 = H2O2 + lactobiono-1,5-lactone.
Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyze the first two steps in the degradation of cholesterol.
The enzyme catalyzes the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta(5) position to the Delta(6) position (cf. EC 5.3.3.1).
cholesterol + O2 = cholest-5-en-3-one + H2O2.
Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2.
The product spontaneously isomerizes to L-ascorbate.
While most higher animals can synthesize ascorbic acid, primates and guinea pigs cannot.
L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate.
D-galactose + O2 = D-galacto-hexodialdose + H2O2.
Also oxidizes D-xylose, L-sorbose and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.
D-glucose + O2 = 2-dehydro-D-glucose + H2O2.
Also acts on D-glucose, D-galactose and D-xylose, but not on D-fructose.
2,6-dichloroindophenol can act as acceptor.
keto-L-sorbose + O2 = 5-dehydro-D-fructose + H2O2.
The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor.
The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism.
The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.
a primary alcohol + O2 = an aldehyde + H2O2.
4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O.
Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids; the B form preferentially oxidizes long-chain and aromatic hydroxy acids.
The rat isoenzyme B also acts as EC 1.4.3.2.
a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2.
ecdysone + O2 = 3-dehydroecdysone + H2O2.
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyze the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine.
In plants, the first reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either EC 1.1.99.1 or EC 1.1.3.17.
The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in those plants, animals and bacteria that use two separate enzymes.
choline + H2O + 2 O2 = glycine betaine + H(+) + 2 H2O2.
Acts on secondary alcohols with five or more carbons, and polyvinyl alcohols with molecular mass over 300 Da.
a secondary alcohol + O2 = a ketone + H2O2.
4-hydroxymandelate oxidase (decarboxylating)
The enzyme from the bacterium Pseudomonas putida is involved in the degradation of mandelate.
(S)-4-hydroxymandelate + H(+) + O2 = 4-hydroxybenzaldehyde + CO2 + H2O2.
Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
a long-chain primary fatty alcohol + O2 = a long-chain fatty aldehyde + H2O2.
O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H2O2.
The product differs from thiamine in replacement of -CH2-CH2-OH by -CH2-COOH; the two-step oxidation proceeds without the release of the intermediate aldehyde from the enzyme.
H2O + 2 O2 + thiamine = H(+) + 2 H2O2 + thiamine acetate.
(2S)-2-hydroxyphytanate + O2 = 2-oxophytanate + H2O2.
Other purine and pyrimidine nucleosides (as well as 2'-deoxyribonucleosides) are substrates, but ribose and nucleotides are not substrates.
The overall reaction takes place in two separate steps, with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction.
Differs from EC 1.1.3.39 as it produces water rather than hydrogen peroxide.
inosine + O2 = 9-riburonosylhypoxanthine + H(+) + H2O.
The enzyme, found in bacteria, also acts more slowly on N-acetyl-D-mannosamine.
H2O + N-acetyl-D-glucosamine + O2 = H(+) + H2O2 + N-acetyl-D-glucosaminate.
H2O + N-acetyl-D-galactosamine + O2 = H(+) + H2O2 + N-acetyl-D-galactosaminate.
a polyvinyl alcohol + n O2 = an oxidized polyvinyl alcohol + n H2O2.
D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H(+) + H2O2.
4-hydroxy-2-methoxybenzyl alcohol oxidase
Converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes.
The allyl group of 4-allylphenols is also converted into the -CH=CH-CH2OH group.
4-hydroxy-3-methoxy-benzenemethanol + O2 = H2O2 + vanillin.
Other purine and pyrimidine nucleosides (as well as 2'-deoxyribonucleosides and arabinosides) are substrates, but ribose and nucleotides are not substrates.
The 5'-dehydro nucleoside is being released from the enzyme to serve as substrate for the second reaction.
Differs from EC 1.1.3.28 as it produces hydrogen peroxide rather than water.
adenosine + H2O + 2 O2 = 9-riburonosyladenine + H(+) + 2 H2O2.
Also catalyzes the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate.
The enzyme from the snails Helix aspersa and Arion ater is found in a specialized tubular organelle that has been termed the mannosome.
D-sorbitol + O2 = D-sorbopyranose + H2O2.
While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly.
prosolanapyrone II oxidase/prosolanapyrone III cycloisomerase
The enzyme is involved in the biosynthesis of the phytotoxin solanapyrone by some fungi.
The bifunctional enzyme catalyzes the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to (-)-solanapyrone A (cf. EC 5.5.1.20).
O2 + prosolanapyrone II = H2O2 + prosolanapyrone III.
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
Works in combination with EC 2.6.1.93 to replace the 6-hydroxy group of paromamine with an amino group.
The enzyme from the bacterium Streptomyces fradiae also catalyzes EC 1.1.3.44.
O2 + paromamine = 6'-oxoparomamine + H2O2.
Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family.
Works in combination with EC 2.6.1.95 to replace the 6'''-hydroxy group of 6'''-hydroxyneomycin C with an amino group.
6'''-deamino-6'''-hydroxyneomycin C + O2 = 6'''-deamino-6'''-oxoneomycin C + H2O2.
This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins.
The enzyme utilizes the same active site to catalyze the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14).
aclacinomycin N + O2 = aclacinomycin A + H2O2.
The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.
(S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate + H2O2.
The enzyme, characterized from the bacterium Methylovorus sp. strain MP688, is involved in the degradation and detoxification of 5-(hydroxymethyl)furfural.
The enzyme acts only on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation.
The enzyme has a broad substrate range that overlaps with EC 1.1.3.7.
5-hydroxymethylfurfural + 2 H2O + 3 O2 = 2,5-dicarboxyfuran + 2 H(+) + 3 H2O2.
3-deoxy-alpha-D-manno-octulosonate 8-oxidase
The enzyme, characterized from the bacterium Shewanella oneidensis, is involved in the formation of 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus.
3-deoxy-alpha-D-manno-oct-2-ulosonate + O2 = 3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + H2O2.
The enzyme, characterized from the millipede Chamberlinius hualienensis, is segregated from its substrate, which is contained in special sacs.
The sacs are ruptured during defensive behavior, allowing the enzyme and substrate to mix in special reaction chambers leading to production of the defensive chemical benzoyl cyanide.
(R)-mandelonitrile + O2 = benzoyl cyanide + H2O2.
With a quinone or similar compound as acceptor
quinoprotein glucose dehydrogenase (PQQ, quinone)
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase
glucose dehydrogenase (pyrroloquinoline-quinone)
Integral membrane protein containing PQQ as prosthetic group.
It also contains bound ubiquinone and Mg(2+) or Ca(2+).
Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate.
Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed 'propeller' structure.
Catalyzes a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm.
Oxidizes other monosaccharides including the pyranose forms of pentoses.
a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-lactone.
FAD-dependent glycerol-3-phosphate dehydrogenase
flavin-linked glycerol-3-phosphate dehydrogenase
An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis.
In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane.
In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain.
This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix.
Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9.
a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate.
a menaquinone + sn-glycerol 3-phosphate = a menaquinol + dihydroxyacetone phosphate.
a ubiquinone + sn-glycerol 3-phosphate = a ubiquinol + dihydroxyacetone phosphate.
sn-glycerol 3-phosphate + ubiquinone-8 = dihydroxyacetone phosphate + ubiquinol-8.
Vitamin K and several other quinones can act as acceptors.
(S)-malate + a quinone = a quinol + oxaloacetate.
(S)-malate + a menaquinone = a menaquinol + oxaloacetate.
pyrroloquinoline quinone-dependent alcohol dehydrogenase
Only described in acetic acid bacteria where it is involved in acetic acid production.
Electron acceptor is membrane ubiquinone.
A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain.
The enzyme has two additional subunits, one of which contains three molecules of heme c.
It does not require amines for activation.
It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes.
It is assayed with phenazine methosulfate or with ferricyanide.
a ubiquinone + ethanol = a ubiquinol + acetaldehyde.
This enzyme oxidizes a wide variety of cyclic alcohols.
Some minor enzyme activity is found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols.
The enzyme is unable to catalyze the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols.
This enzyme differs from EC 1.1.5.5, which shows activity with ethanol.
a cyclic alcohol + a quinone = a cyclic ketone + a quinol.
quinate/shikimate dehydrogenase (quinone)
NAD(P)(+)-independent quinate dehydrogenase
a quinone + L-quinate = 3-dehydroquinate + a quinol.
a quinone + D-glucose = a quinol + D-glucono-1,5-lactone.
(R)-lactate, (R)-malate and meso-tartrate are good substrates.
Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD(+) and NADP(+) are not acceptors.
a (2R)-2-hydroxycarboxylate + a quinone = a 2-oxocarboxylate + a quinol.
a quinone + butan-1-ol = a quinol + butanal.
The enzyme is a peripheral membrane dehydrogenase that participates in respiration.
Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
(R)-lactate + a quinone = a quinol + pyruvate.
The enzyme, characterized from the bacterium Escherichia coli, contains an FAD cofactor that is not covalently attached.
It is bound to the cytoplasmic membrane and is coupled to the membrane quinone pool.
(S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a quinol.
The enzyme, characterized from the bacterium Gluconobacter japonicus, is a heterotrimer composed of an FAD-containing large subunit, a small subunit, and a heme c-containing subunit, which is responsible for anchoring the complex to the cytoplasmic membrane and for transferring the electrons to ubiquinone.
a ubiquinone + keto-D-fructose = 5-dehydro-D-fructose + a ubiquinol.
membrane-bound quinoprotein inositol dehydrogenase
myo-inositol + pyrroloquinoline quinone = H(+) + pyrroloquinoline quinol + scyllo-inosose.
A molybdenum-flavin-iron-sulfur protein that is involved in the anaerobic pathway of phenol metabolism in bacteria.
A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor.
benzoyl-CoA + H2O + oxidized 2[4Fe-4S]-[ferredoxin] = 4-hydroxybenzoyl-CoA + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin].
Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate.
Usually assayed with phenazine methosulfate or ferricyanide.
a primary alcohol + 2 oxidized [azurin] = an aldehyde + 2 H(+) + 2 reduced [azurin].
glucose-6-phosphate dehydrogenase (coenzyme-F420)
coenzyme F420-dependent glucose-6-phosphate dehydrogenase
F420-dependent glucose-6-phosphate dehydrogenase
The enzyme is very specific for D-glucose 6-phosphate.
No activity with NAD(+), NADP(+), flavin adenine dinucleotide and flavin mononucleotide.
D-glucose 6-phosphate + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420-(gamma-L-Glu)(n).
decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase
decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase
The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.1.333 in the epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis-decaprenylphospho-beta-D-arabinofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
FAD + H(+) + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose = FADH2 + trans,octa-cis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose.
a quinol + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = a quinone + reduced coenzyme F420-(gamma-L-Glu)(n).
secondary-alcohol dehydrogenase (coenzyme-F420)
F420-dependent secondary alcohol dehydrogenase
The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyzes the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
a secondary alcohol + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = a ketone + reduced coenzyme F420-(gamma-L-Glu)(n).
ribonucleoside-triphosphate reductase (formate)
anaerobic ribonucleoside-triphosphate reductase
The enzyme, which is expressed in the bacterium Escherichia coli during anaerobic growth, contains an iron sulfur center.
The active form of the enzyme contains an oxygen-sensitive glycyl (1-amino-2-oxoethan-1-yl) radical that is generated by the activating enzyme NrdG via chemistry involving S-adenosylmethionine (SAM) and a [4Fe-4S] cluster.
The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical.
The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl (1lambda(4)-disulfan-1-yl) radical bridge between methionine and cysteine residues.
Oxidation of formate by the thiosulfuranyl radical results in the release of CO2 and regeneration of the thiyl radical.
a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O.
serine-type anaerobic sulfatase-maturating enzyme
A bacterial radical S-adenosyl-L-methionine (AdoMet) enzyme that contains three [4Fe-4S] clusters.
The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity.
While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7.
L-seryl-[sulfatase] + S-adenosyl-L-methionine = 3-oxo-L-alanyl-[sulfatase] + 5'-deoxyadenosine + H(+) + L-methionine.
In plants, the first reaction is catalyzed by EC 1.14.15.7 whereas in animals and many bacteria, it is catalyzed by either EC 1.1.99.1 or EC 1.1.3.17.
The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria.
(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2.
A + D-gluconate = 2-dehydro-D-gluconate + AH2.
2-dehydro-D-gluconate + A = 2,5-didehydro-D-gluconate + AH2.
The enzyme from the archaeon Archaeoglobus fulgidus cannot utilize NAD(+), cytochrome C, methylene blue or dimethylnaphthoquinone as acceptors.
In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.
Catalyzes hydrogen transfer from C3 or C4 (S)-2-hydroxy acids to 2-oxo acids.
Contains tightly bound nicotinamide nucleotide in its active center.
This prosthetic group cannot be removed without denaturation of the protein.
(S)-lactate + oxaloacetate = (S)-malate + pyruvate.
A + keto-L-sorbose = 5-dehydro-D-fructose + AH2.
The enzymes from members of the Rhizobiaceae family (such as Agrobacterium tumefaciens) act on disaccharides that contain a glucose moiety at the non-reducing end, such as sucrose, trehalose, leucrose, palatinose, trehalulose, and maltitol, forming the respective 3'-keto derivatives. cf. EC 1.1.2.11.
A + sucrose = 3-dehydro-alpha-D-glucosyl beta-D-fructofuranoside + AH2.
2,6-dichloroindophenol and phenazine methosulfate can act as acceptors.
Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-beta-D-mannose.
The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group.
It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones, and molecular oxygen, and one-electron oxidants, including semiquinone species, iron(II) complexes, and the model acceptor cytochrome c.
2,6-dichloroindophenol can act as acceptor in vitro.
A + D-cellobiose = AH2 + D-cellobiono-1,5-lactone.
Acts on C3-C16 linear-chain saturated primary alcohols, C4-C7 aldehydes and on non-ionic surfactants containing polyethylene glycol residues, such as Tween 40 and 60, but not on methanol and only very slowly on ethanol.
A + a primary alcohol = AH2 + an aldehyde.
Also acts, more slowly, on a number of other polyols including D-sorbitol, D-arabinitol, meso-erythritol, adonitol and propylene glycol.
(S)-3-hydroxybutanoate + 2-oxoglutarate = (R)-2-hydroxyglutarate + acetoacetate.
2-oxoglutarate + 4-hydroxybutanoate = (R)-2-hydroxyglutarate + succinate semialdehyde.
2,6-dichloroindophenol and methylene blue can act as acceptors.
3-hydroxycyclohexanone + A = AH2 + cyclohexane-1,3-dione.
(R)-pantoyllactone dehydrogenase (flavin)
2-dehydropantolactone reductase (flavin)
2-dehydropantoyl-lactone reductase (flavin)
Phenazine methosulfate (PMS) can act as acceptor.
The enzyme has been studied in Nocardia asteroides and shown to be membrane-bound and induced by 1,2-propanediol.
(R)-pantolactone + A = 2-dehydropantolactone + AH2.
D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities.
The ketose substrate must be in the open-chain form.
The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form.
Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates.
The enzyme from Zymomonas mobilis contains tightly bound NADP(+).
D-fructose + D-glucose = D-glucono-1,5-lactone + D-sorbitol.
quinone-dependent pyranose dehydrogenase
A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor.
1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor.
Unlike EC 1.1.3.10, this fungal enzyme does not interact with O2 and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars.
D-glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3.
The enzyme also acts on 1->4-alpha- and 1->4-beta-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10.
Sugars are oxidized in their pyranose but not in their furanose form.
pyranose + acceptor = pyranos-2-ulose + reduced acceptor.
pyranose + acceptor = pyranos-3-ulose + reduced acceptor.
pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.
a pyranoside + acceptor = a pyranosid-3-ulose + reduced acceptor.
a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced acceptor.
Has broad substrate specificity, with 2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as substrates.
Branching in a substrate at the C-3 position results in loss of activity.
The enzyme from Proteus sp. is inactivated by oxygen.
A + a (2R)-2-hydroxycarboxylate = a 2-oxocarboxylate + AH2.
While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme.
Transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone.
It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy.
Has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate.
It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate.
Esters of mandelate, such as methyl (S)-mandelate, are also substrates.
(S)-mandelate + A = AH2 + phenylglyoxylate.
The product, 1-dehydro-L-sorbose, is an intermediate in bacterial 2-keto-L-gulonic-acid formation.
The activity of this membrane-bound enzyme is stimulated by Fe(III) or Co(2+) but is inhibited by Cu(2+).
Highly specific for L-sorbose as other sugars, such as glucose, mannitol and sorbitol, are not substrates.
Phenazine methosulfate and DCIP can act as artificial acceptors.
A + L-sorbopyranose = 1-dehydro-L-sorbose + AH2.
soluble quinoprotein glucose dehydrogenase
Soluble periplasmic enzyme containing PQQ as prosthetic group, bound to a calcium ion.
It is assayed with Wurster's Blue or phenazine methosulfate.
It has negligible sequence or structure similarity to other quinoproteins.
It catalyzes an exceptionally high rate of oxidation of a wide range of aldose sugars, including D-glucose, galactose, arabinose and xylose, and also the disaccharides lactose, cellobiose and maltose.
It has been described only in Acinetobacter calcoaceticus.
A + D-glucose = AH2 + D-glucono-1,5-lactone.
Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD(+)/NADH cofactor that does not dissociate during the catalytic process.
Instead, the cofactor is regenerated by a second substrate or electron carrier.
While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA) can serve this function in vitro.
The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol.
ethanol + N,N-dimethyl-4-nitrosoaniline = 4-(hydroxylamino)-N,N-dimethylaniline + acetaldehyde.
methanol dehydrogenase (nicotinoprotein)
Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process.
The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis.
These enzymes are decameric, and possess a 5-fold symmetry.
Some of the enzymes can also dismutate formaldehyde to methanol and formate.
2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent)
Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family.
The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme.
2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + H(+) + L-methionine.
The enzyme has no activity with NAD(+) or NADP(+), and was assayed in vitro using artificial electron acceptors.
It has lower activity with (R)-lactate, (R)-2-hydroxybutyrate and meso-tartrate, and no activity with the (S) isomers.
(R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2.
(R)-2-hydroxyglutarate--pyruvate transhydrogenase
The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4 and is active with oxaloacetate as electron acceptor forming (R)-malate.
(R)-2-hydroxyglutarate + pyruvate = (R)-lactate + 2-oxoglutarate.
(R)-2-hydroxyglutarate + oxaloacetate = (R)-malate + 2-oxoglutarate.
3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine reductase
This enzyme is involved in the biosynthesis of vindoline and vindorosine in the plant Catharanthus roseus (Madagascar periwinkle).
In vivo, it functions in the direction of reduction.
It has no activity with 3-epoxylated compounds, which can form spontaneously from its unstable substrates.
(3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + A = (3R)-1,2-didehydro-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + AH2.
(3R)-3-hydroxy-2,3-dihydrotabersonine + A = (3R)-1,2-didehydro-3-hydroxy-2,3-dihydrotabersonine + AH2.
The enzyme, characterized from the bacteria Pseudomonas sp. MA-1 and Mesorhizobium loti, participates in the degradation of pyridoxine (vitamin B6).
The enzyme has been assayed in vitro in the presence of the artificial electron acceptor dichloroindophenol (DCPIP).
4-pyridoxate + A = 5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + AH2.
Acting on the aldehyde or oxo group of donors
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH.
acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH.
an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH.
acetaldehyde + H2O + NADP(+) = acetate + 2 H(+) + NADPH.
benzaldehyde + H2O + NADP(+) = benzoate + 2 H(+) + NADPH.
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine.
This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria.
In contrast, different enzymes are involved in the first reaction.
In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17.
In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157.
betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH.
glyceraldehyde-3-phosphate dehydrogenase (NADP(+))
D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-phosphoglycerate + 2 H(+) + NADPH.
acetaldehyde dehydrogenase (acetylating)
Also acts, more slowly, on glycolaldehyde, propanal and butanal.
In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39.
The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87.
Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols.
NADP(+) can replace NAD(+) but the rate of reaction is much slower.
acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH.
L-aspartate-beta-semialdehyde dehydrogenase
L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH.
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH.
glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH.
3-oxopropanoate + H2O + NADP(+) = 2 H(+) + malonate + NADPH.
3-oxopropanoate + H2O + NAD(+) = 2 H(+) + malonate + NADH.
succinate-semialdehyde dehydrogenase [NAD(P)(+)]
H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate.
H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate.
CoA + glyoxylate + NADP(+) = H(+) + NADPH + oxalyl-CoA.
malonate-semialdehyde dehydrogenase (acetylating)
3-oxopropanoate + CoA + NADP(+) = acetyl-CoA + CO2 + NADPH.
3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH.
gamma-guanidinobutyraldehyde dehydrogenase
The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates.
The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54).
As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate.
4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH.
The enzyme, characterized from multiple Pseudomonas strains, participates in L-lysine degradation.
Unlike earlier claims, it prefers NADP(+) to NAD(+).
5-oxopentanoate + H2O + NADP(+) = glutarate + 2 H(+) + NADPH.
glycolaldehyde + H2O + NAD(+) = glycolate + 2 H(+) + NADH.
(S)-lactaldehyde + H2O + NAD(+) = (S)-lactate + 2 H(+) + NADH.
2-oxoaldehyde + H2O + NAD(+) = a 2-oxocarboxylate + 2 H(+) + NADH.
succinate-semialdehyde dehydrogenase (NAD(+))
This enzyme participates in the degradation of glutamate and 4-aminobutyrate.
It is similar to EC 1.2.1.79 and EC 1.2.1.16 but is specific for NAD(+).
branched-chain alpha-keto acid dehydrogenase system
2-oxoisovalerate dehydrogenase (acylating)
branched-chain alpha-keto acid dehydrogenase complex
This enzyme system catalyzes the oxidative decarboxylation of branched-chain alpha-keto acids derived from L-leucine, L-isoleucine, and L-valine to branched-chain acyl-CoAs.
It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, EC 1.2.1.105, EC 1.4.1.27 and EC 2.3.1.190.
With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).
The reaction catalyzed by this system is the sum of three activities: EC 1.2.4.4, EC 2.3.1.168 and EC 1.8.1.4.
The system also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate.
3-methyl-2-oxobutanoate + CoA + NAD(+) = 2-methylpropanoyl-CoA + CO2 + NADH.
(S)-3-methyl-2-oxopentanoate + CoA + NAD(+) = 2-methylbutanoyl-CoA + CO2 + NADH.
4-methyl-2-oxopentanoate + CoA + NAD(+) = 3-methylbutanoyl-CoA + CO2 + NADH.
2,5-dioxopentanoate + H2O + NADP(+) = 2-oxoglutarate + 2 H(+) + NADPH.
methylmalonate-semialdehyde dehydrogenase (CoA acylating)
methylmalonate-semialdehyde dehydrogenase (acylating)
Also converts 3-oxopropanoate into acetyl-CoA.
The reaction occurs in two steps with the decarboxylation process preceding CoA-binding.
Bicarbonate rather than CO2 is released as a final product.
2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA.
benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH.
Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
an aromatic aldehyde + H2O + NAD(+) = an aromatic carboxylate + 2 H(+) + NADH.
The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group.
The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain.
The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
AMP + an aromatic aldehyde + diphosphate + NADP(+) = an aromatic carboxylate + ATP + H(+) + NADPH.
L-aminoadipate-semialdehyde dehydrogenase
2-aminoadipate semialdehyde dehydrogenase
2-aminoadipic semialdehyde dehydrogenase
alpha-aminoadipate-semialdehyde dehydrogenase
L-alpha-aminoadipate delta-semialdehyde oxidoreductase
(S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
(S)-2-amino-6-oxohexanoate + H2O + NADP(+) = 2 H(+) + L-2-aminoadipate + NADPH.
(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-aminoadipate + NADH.
aminomuconate-semialdehyde dehydrogenase
Also acts on 2-hydroxymuconate semialdehyde.
2-aminomuconate 6-semialdehyde + H2O + NAD(+) = (2Z,4E)-2-aminomuconate + 2 H(+) + NADH.
(R)-4-dehydropantoate + H2O + NAD(+) = (R)-3,3-dimethylmalate + 2 H(+) + NADH.
Acts on both the 11-trans- and 13-cis-forms of retinal.
H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate.
all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH.
N-acetyl-gamma-glutamyl-phosphate reductase
N-acetyl-glutamate semialdehyde dehydrogenase
N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH.
2-phenylacetaldehyde + H2O + NAD(+) = 2-phenylacetate + 2 H(+) + NADH.
Glutamyl-gamma-semialdehyde dehydrogenase
L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH.
Also acts, more slowly, on octadecanoyl-CoA.
CoA + hexadecanal + NAD(+) = H(+) + hexadecanoyl-CoA + NADH.
Also acts on a number of substituted cinnamoyl esters of coenzyme A.
(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH.
(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH.
(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH.
(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) + NADPH.
formaldehyde + H2O + NAD(+) = formate + 2 H(+) + NADH.
4-trimethylammoniobutyraldehyde dehydrogenase
4-(trimethylamino)butanal + H2O + NAD(+) = 4-(trimethylamino)butanoate + 2 H(+) + NADH.
a long-chain fatty aldehyde + H2O + NAD(+) = a long-chain fatty acid + 2 H(+) + NADH.
2-oxoaldehyde + H2O + NADP(+) = a 2-oxocarboxylate + 2 H(+) + NADPH.
Together with EC 6.2.1.19 forms a fatty acid reductase system which produces the substrate of EC 1.14.14.3, thus being part of the bacterial luciferase system.
a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain fatty acyl-CoA + H(+) + NADPH.
The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly.
CoA + NADP(+) + pyruvate = acetyl-CoA + CO2 + NADPH.
The Euglena enzyme can also use NAD(+) as acceptor, but more slowly.
2-oxoglutarate + CoA + NADP(+) = CO2 + NADPH + succinyl-CoA.
4-hydroxyphenylacetaldehyde dehydrogenase
With EC 4.2.1.87, brings about the metabolism of octopamine in Pseudomonas.
(4-hydroxyphenyl)acetaldehyde + H2O + NAD(+) = 4-hydroxyphenylacetate + 2 H(+) + NADH.
Involved in the degradation of arginine in Pseudomonas putida (cf. EC 1.2.1.19).
4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2 H(+) + NADH.
Also acts on acetaldehyde, but more slowly.
butanal + CoA + NAD(+) = butanoyl-CoA + H(+) + NADH.
butanal + CoA + NADP(+) = butanoyl-CoA + H(+) + NADPH.
phenylglyoxylate dehydrogenase (acylating)
The enzyme from Azoarcus evansii is specific for phenylglyoxylate.
2-oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate.
CoA + NAD(+) + phenylglyoxylate = benzoyl-CoA + CO2 + NADH.
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating)
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
triosephosphate dehydrogenase (NAD(P)(+))
NAD(+) and NADP(+) can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 and EC 1.2.1.13, which are NAD(+)- and NADP(+)-dependent, respectively.
5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
carboxymethylhydroxymuconic semialdehyde dehydrogenase
Involved in the tyrosine degradation pathway in Arthrobacter sp.
2-hydroxy-5-carboxymethylmuconate semialdehyde + H2O + NAD(+) = (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate + 2 H(+) + NADH.
4-hydroxymuconic-semialdehyde dehydrogenase
Involved in the 4-nitrophenol degradation pathway.
cis,trans-4-hydroxymuconate semialdehyde + H2O + NAD(+) = 2 H(+) + maleylacetate + NADH.
Involved in the toluene-4-sulfonate degradation pathway.
4-formylbenzenesulfonate + H2O + NAD(+) = 4-sulfobenzoate + 2 H(+) + NADH.
Last step in the cyclohexanol degradation pathway in Acinetobacter sp.
6-oxohexanoate + H2O + NADP(+) = 2 H(+) + hexanedioate + NADPH.
4-hydroxybenzaldehyde dehydrogenase (NAD(+))
The bacterial enzyme (characterized from an unidentified denitrifying bacterium) is involved in an anaerobic toluene degradation pathway.
The plant enzyme is involved in formation of 4-hydroxybenzoate, a cell wall-bound phenolic acid that plays a major role in plant defense against pathogens.
4-hydroxybenzaldehyde + H2O + NAD(+) = 4-hydroxybenzoate + 2 H(+) + NADH.
Involved in the naphthalene degradation pathway in some bacteria.
H2O + NAD(+) + salicylaldehyde = 2 H(+) + NADH + salicylate.
H2O + NAD(+) + vanillin = 2 H(+) + NADH + vanillate.
Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes.
(E)-coniferaldehyde + H2O + NADP(+) = (E)-ferulate + 2 H(+) + NADPH.
(E)-coniferaldehyde + H2O + NAD(+) = (E)-ferulate + 2 H(+) + NADH.
The enzyme from Streptomyces cattleya has a high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde.
fluoroacetaldehyde + H2O + NAD(+) = fluoroacetate + 2 H(+) + NADH.
Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants.
However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine.
This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium.
Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH.
succinylglutamate-semialdehyde dehydrogenase
N-succinylglutamate 5-semialdehyde dehydrogenase
succinylglutamic semialdehyde dehydrogenase
This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine.
This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA.
The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.11, EC 1.2.1.71 and EC 3.5.1.96.
H2O + N-succinyl-L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + N-succinyl-L-glutamate + NADH.
Was originally thought to be an EC 1.2.1.12, but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate.
Forms part of the pyridoxal-5'-phosphate coenzyme biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5.
D-erythrose 4-phosphate + H2O + NAD(+) = 4-phospho-D-erythronate + 2 H(+) + NADH.
Part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth.
At physiological concentrations, NAD(+) cannot be replaced by NADP(+).
Specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
H2O + NAD(+) + sulfoacetaldehyde = 2 H(+) + NADH + sulfoacetate.
Abietic acid is the principle component of conifer resin.
This enzyme catalyzes the last step of the pathway of abietic acid biosynthesis in Abies grandis (grand fir).
The activity has been demonstrated in cell-free stem extracts of A. grandis, was present in the cytoplasm, and required NAD(+) as cofactor.
The enzyme is expressed constitutively at a high level, and is not inducible by wounding of the plant tissue.
abieta-7,13-dien-18-al + H2O + NAD(+) = abieta-7,13-dien-18-oate + 2 H(+) + NADH.
malonyl CoA reductase (malonate semialdehyde-forming)
Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and some thermoacidophilic archaea, respectively.
The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits.
The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the next reaction in the pathway, EC 1.1.1.298.
3-oxopropanoate + CoA + NADP(+) = H(+) + malonyl-CoA + NADPH.
succinate-semialdehyde dehydrogenase (acetylating)
coenzyme-A-dependent succinate-semialdehyde dehydrogenase
Catalyzes the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde.
The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation, and in Metallosphaera sedula, where it participates in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea.
CoA + NADP(+) + succinate semialdehyde = H(+) + NADPH + succinyl-CoA.
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP(+))
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
This enzyme catalyzes a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
(3Z)-6-oxohex-3-enoyl-CoA + H2O + NADP(+) = cis-3,4-dehydroadipyl-CoA + 2 H(+) + NADPH.
The enzyme is involved in phenanthrene degradation.
2-formylbenzoate + H2O + NAD(+) = 2 H(+) + NADH + phthalate.
succinate-semialdehyde dehydrogenase (NADP(+))
It is similar to EC 1.2.1.24 and EC 1.2.1.16 but is specific for NADP(+).
The enzyme from Escherichia coli is 20-fold more active with NADP(+) than NAD(+).
long-chain acyl-[acyl-carrier-protein] reductase
fatty acyl-[acyl-carrier-protein] reductase
Catalyzes the reaction in the opposite direction.
This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyzes the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde.
Together with EC 4.1.99.5, it is involved in alkane biosynthesis.
The natural substrates of the enzyme are C16 to C18 activated fatty acids.
a long-chain fatty aldehyde + holo-[ACP] + NADP(+) = a long-chain fatty acyl-[ACP] + H(+) + NADPH.
a long-chain fatty aldehyde + holo-[ACP] + NAD(+) = a long-chain fatty acyl-[ACP] + H(+) + NADH.
sulfoacetaldehyde dehydrogenase (acylating)
The enzyme is involved in degradation of sulfoacetate.
In this pathway the reaction is catalyzed in the reverse direction.
The enzyme is specific for sulfoacetaldehyde and NADP(+).
CoA + NADP(+) + sulfoacetaldehyde = H(+) + NADPH + sulfoacetyl-CoA.
Neurosporaxanthin is responsible for the orange color of of Neurospora.
4'-apo-beta-carotenal + H2O + NAD(+) = 2 H(+) + NADH + neurosporaxanthin.
3-succinoylsemialdehyde-pyridine dehydrogenase
The enzyme has been characterized from the soil bacterium Pseudomonas sp. HZN6.
It participates in the nicotine degradation pathway.
4-oxo-4-(pyridin-3-yl)butanal + H2O + NADP(+) = 4-oxo-4-(pyridin-3-yl)butanoate + 2 H(+) + NADPH.
alcohol-forming fatty acyl-CoA reductase
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba).
The alcohol is formed by a four-electron reduction of fatty acyl-CoA.
Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released.
The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+).
2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) + octadecan-1-ol.
2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2 NADP(+).
2-hydroxymuconate-6-semialdehyde dehydrogenase
This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2), and is an intermediate in the bacterial degradation of several aromatic compounds.
Activity with NAD(+) is more than 10-fold higher than with NADP(+).
(2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O + NAD(+) = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + 2 H(+) + NADH.
(2E)-geranial + H2O + NAD(+) = geranate + 2 H(+) + NADH.
propanal dehydrogenase (CoA-propanoylating)
The enzyme forms a bifunctional complex with EC 4.1.3.43, with a tight channel connecting the two subunits.
Also acts, more slowly, on glycolaldehyde and butanal.
In Pseudomonas species the enzyme forms a bifunctional complex with EC 4.1.3.39.
The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.10.
NADP(+) can replace NAD(+) with a much slower rate.
CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA.
L-glutamate gamma-semialdehyde dehydrogenase
Delta(1)-pyrroline-5-carboxylate dehydrogenase
This enzyme catalyzes the irreversible oxidation of glutamate-gamma-semialdehyde to glutamate as part of the proline degradation pathway.
(S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde.
In many bacterial species, both activities are carried out by a single bifunctional enzyme.
The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate.
NADP(+) can also act as acceptor, but with lower activity.
H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH.
(S)-1-pyrroline-5-carboxylate + 2 H2O + NAD(+) = H(+) + L-glutamate + NADH.
(S)-1-pyrroline-5-carboxylate + 2 H2O + NADP(+) = H(+) + L-glutamate + NADPH.
(3R,5S)-1-pyrroline-3-hydroxy-5-carboxylate + 2 H2O + NADP(+) = (4S)-4-hydroxy-L-glutamate + H(+) + NADPH.
(3R,5S)-1-pyrroline-3-hydroxy-5-carboxylate + 2 H2O + NAD(+) = (4S)-4-hydroxy-L-glutamate + H(+) + NADH.
D-glyceraldehyde dehydrogenase (NADP(+))
The enzyme from the archaea Thermoplasma acidophilum and Picrophilus torridus is involved in the non-phosphorylative Entner-Doudoroff pathway, cf. EC 1.2.99.8.
D-glyceraldehyde + H2O + NADP(+) = (R)-glycerate + 2 H(+) + NADPH.
glyceraldehyde-3-phosphate dehydrogenase [NAD(P)(+)]
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax (cf. EC 1.2.1.9).
D-glyceraldehyde 3-phosphate + H2O + NAD(+) = (2R)-3-phosphoglycerate + 2 H(+) + NADH.
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyzes EC 3.3.2.12.
Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway.
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + H2O + NADP(+) = 3-oxo-5,6-didehydrosuberyl-CoA + 2 H(+) + NADPH.
3,6-anhydro-alpha-L-galactose dehydrogenase
The enzyme, characterized from the marine bacterium Vibrio sp. EJY3, is involved in a degradation pathway for 3,6-anhydro-alpha-L-galactose, a major component of the polysaccharides produced by red macroalgae, such as agarose and porphyran.
3,6-anhydro-alpha-L-galactopyranose + H2O + NAD(+) = 3,6-anhydro-L-galactonate + 2 H(+) + NADH.
3,6-anhydro-alpha-L-galactopyranose + H2O + NADP(+) = 3,6-anhydro-L-galactonate + 2 H(+) + NADPH.
Invoved in juvenile hormone production in insects.
The enzyme was described from the corpora allata of Drosophila melanogaster (fruit fly), Manduca sexta (tobacco hornworm) and Aedes aegypti (dengue mosquito).
(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+) + NADH.
This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyzes the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis.
An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain.
Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate.
Different from EC 1.2.1.31 which catalyzes a similar transformation in the opposite direction without ATP hydrolysis.
(S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP(+) = ATP + H(+) + L-2-aminoadipate + NADPH.
4-hydroxybenzaldehyde dehydrogenase (NADP(+))
Involved in the aerobic pathway for degradation of toluene, 4-methylphenol, and 2,4-xylenol by several Pseudomonas strains.
The enzyme is also active with 4-hydroxy-3-methylbenzaldehyde.
4-hydroxybenzaldehyde + H2O + NADP(+) = 4-hydroxybenzoate + 2 H(+) + NADPH.
(2S)-3-sulfolactaldehyde + H2O + NADP(+) = (2S)-3-sulfolactate + 2 H(+) + NADPH.
(2S)-3-sulfolactaldehyde + H2O + NAD(+) = (2S)-3-sulfolactate + 2 H(+) + NADH.
2-hydroxy-2-methylpropanal dehydrogenase
2-hydroxy-2-methylpropanal + H2O + NAD(+) = 2-hydroxy-2-methylpropanoate + 2 H(+) + NADH.
4-(gamma-glutamylamino)butanal dehydrogenase
The enzyme, characterized from the bacterium Escherichia coli, is involved in a putrescine catabolic pathway.
It has a broad substrate range, and can also catalyze the activities of EC 1.2.1.19 and EC 1.2.1.24.
4-(gamma-L-glutamylamino)butanal + H2O + NAD(+) = 4-(gamma-L-glutamylamino)butanoate + 2 H(+) + NADH.
4-(gamma-L-glutamylamino)butanal + H2O + NADP(+) = 4-(gamma-L-glutamylamino)butanoate + 2 H(+) + NADPH.
5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase
5-formyl-3-hydroxy-2-methylpyridine-4-carboxylate + H2O + NAD(+) = 5-hydroxy-6-methylpyridine-3,4-dicarboxylate + 2 H(+) + NADH.
The enzyme, characterized from the ascomycete fungus Aspergillus flavus, is specific for L-tyrosine.
It contains three domains - an adenylation domain, a peptidyl-carrier protein (PCP) domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group.
The enzyme activates its substrate to an adenylate form, followed by a transfer to the PCP domain.
The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to the aldehyde.
AMP + diphosphate + L-tyrosinal + NADP(+) = ATP + H(+) + L-tyrosine + NADPH.
isopyridoxal dehydrogenase (5-pyridoxate-forming)
The enzyme also catalyzes the activity of EC 1.1.1.416.
H2O + isopyridoxal + NAD(+) = 5-pyridoxate + 2 H(+) + NADH.
[amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase
The enzyme participates in an L-lysine biosynthesis in certain species of archaea and bacteria.
[amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH.
The pyruvate dehydrogenase system (PDH) is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, EC 1.2.1.105, EC 1.4.1.27 and EC 2.3.1.190.
With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3).
The reaction catalyzed by this system is the sum of three activities: EC 1.2.4.1, EC 2.3.1.12, and EC 1.8.1.4.
The mammalian system also includes E3 binding protein, which is involved in the interaction between the E2 and E3 subunits.
CoA + NAD(+) + pyruvate = acetyl-CoA + CO2 + NADH.
The 2-oxoglutarate dehydrogenase system is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, EC 1.2.1.104, EC 1.4.1.27 and EC 2.3.1.190.
This enzyme system converts 2-oxoglutarate to succinyl-CoA and produces NADH and CO2 in a complicated series of irreversible reactions.
The reaction catalyzed by this system is the sum of three activities: EC 1.2.4.2, EC 2.3.1.61 and EC 1.8.1.4.
2-oxoglutarate + CoA + NAD(+) = CO2 + NADH + succinyl-CoA.
[amino-group carrier protein]-5-phospho-L-glutamate reductase
The enzyme participates in an L-arginine biosynthesis pathway in certain species of archaea and bacteria.
In some organisms the enzyme is bifunctional and also catalyzes the activity of EC 1.2.1.103.
[amino-group carrier protein]-C-terminal-gamma-(L-glutamyl-5-semialdehyde)-L-glutamate + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-gamma-(5-phospho-L-glutamyl)-L-glutamate + H(+) + NADPH.
glyceraldehyde-3-phosphate dehydrogenase (arsenate-transferring)
The enzyme, discovered in bacteria, is very similar to EC 1.2.1.12.
However, the gene encoding it is located in arsenic resistance islands in the chromosome, next to a gene (arsJ) that encodes a transporter that removes the product, 1-arsono-3-phosphoglycerate, from the cell.
Together the two proteins form an arsenic detoxification system.
arsenate + D-glyceraldehyde 3-phosphate + NAD(+) = 1-arsono-3-phospho-D-glycerate + H(+) + NADH.
hexadecanal dehydrogenase (acylating, NADP dependent)
CoA + hexadecanal + NADP(+) = H(+) + hexadecanoyl-CoA + NADPH.
a fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+).
2 Fe(III)-[cytochrome b1] + formate = CO2 + 2 Fe(II)-[cytochrome b1] + H(+).
The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides.
The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11).
an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2.
all-trans-retinal + H2O + O2 = all-trans-retinoate + H(+) + H2O2.
Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin.
FADH is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate.
H(+) + O2 + phosphate + pyruvate = acetyl phosphate + CO2 + H2O2.
glyoxylate + H2O + O2 = H(+) + H2O2 + oxalate.
CoA + H(+) + O2 + pyruvate = acetyl-CoA + CO2 + H2O2.
Has a preference for aldehydes having an indole-ring structure as substrate.
May play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild-type Arabidopsis thaliana.
While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly.
H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate + H(+) + H2O2.
H2O + O2 + pyridoxal = 4-pyridoxate + H(+) + H2O2.
Acts on benzaldehyde, vanillin and a number of other aromatic aldehydes, but not on aliphatic aldehydes or sugars.
an aromatic aldehyde + H2O + O2 = an aromatic carboxylate + H(+) + H2O2.
Involved in tyrosine degradation pathway in Arthrobacter sp.
2 3-(4-hydroxyphenyl)pyruvate + O2 = 2 4-hydroxyphenylacetate + 2 CO2.
Acts on both (+)- and (-)-abscisic aldehyde.
Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288, EC 1.13.11.51 and EC 1.14.13.93.
While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde as substrates, but more slowly.
2-cis-(+)-abscisic aldehyde + H2O + O2 = 2-cis-(+)-abscisate + H(+) + H2O2.
The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis.
glyoxal + H2O + O2 = glyoxylate + H(+) + H2O2.
H2O + methylglyoxal + O2 = H(+) + H2O2 + pyruvate.
pyruvate dehydrogenase (acetyl-transferring)
pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating)
It is a component (in multiple copies) of EC 1.2.1.104 in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4.
It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2.
oxoglutarate dehydrogenase (succinyl-transferring)
It is a component of EC 1.2.1.105 in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4.
It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2.
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)
2-oxoisovalerate (lipoate) dehydrogenase
3-methyl-2-oxobutanoate dehydrogenase (lipoamide)
alpha-keto-alpha-methylvalerate dehydrogenase
alpha-ketoisocaproic-alpha-keto-alpha-methylvaleric dehydrogenase
branched-chain (-2-oxoacid) dehydrogenase (BCD)
branched-chain 2-keto acid dehydrogenase
branched-chain alpha-keto acid dehydrogenase
branched-chain alpha-oxo acid dehydrogenase
dehydrogenase, 2-oxoisovalerate (lipoate)
It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine.
It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4.
It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2.
This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone.
a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2.
Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde.
a quinone + an aldehyde + H2O = a carboxylate + a quinol + H(+).
molybdoenzyme carbon monoxide dehydrogenase
This enzyme, found in carboxydotrophic bacteria, catalyzes the oxidation of CO to CO2 under aerobic conditions.
The enzyme belongs to the xanthine oxidoreductase family.
The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor.
alpha-ketobutyrate-ferredoxin oxidoreductase
The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate.
This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity.
For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7.
CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
2-oxobutanoate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + propanoyl-CoA + 2 reduced [2Fe-2S]-[ferredoxin].
2-ketoglutarate ferredoxin oxidoreductase
2-oxoglutarate ferredoxin oxidoreductase
alpha-ketoglutarate-ferredoxin oxidoreductase
For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.7.
2-oxoglutarate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + succinyl-CoA.
carbon-monoxide dehydrogenase (ferredoxin)
This prokaryotic enzyme catalyzes the reversible reduction of CO2 to CO.
The electrons are transferred to redox proteins such as ferredoxin.
In purple sulfur bacteria and methanogenic archaea it catalyzes the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively.
In acetogenic and sulfate-reducing microbes it catalyzes the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, with which the enzyme forms a tight complex in those organisms.
In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2 which catalyze the overall reaction: CO + H2O = CO2 + H2.
CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
tungsten-containing aldehyde ferredoxin oxidoreductase
Catalyzes the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids.
However, it does not oxidize glyceraldehyde 3-phosphate (see EC 1.2.7.6).
Can use ferredoxin or methylviologen but not NAD(P)(+) as electron acceptor.
an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
glyceraldehyde-3-phosphate Fd oxidoreductase
glyceraldehyde-3-phosphate ferredoxin reductase
Thought to function in place of glyceraldehyde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus.
Specific for glyceraldehyde-3-phosphate.
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = (2R)-3-phosphoglycerate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
3-methyl-2-oxobutanoate synthase (ferredoxin)
branched-chain ketoacid ferredoxin reductase
branched-chain oxo acid ferredoxin reductase
The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters.
Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, and 2-oxobutanoate.
This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity.
For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3.
3-methyl-2-oxobutanoate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-methylpropanoyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
indolepyruvate ferredoxin oxidoreductase
3-(indol-3-yl)pyruvate synthase (ferredoxin)
Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and 4-hydroxyphenylpyruvate as substrates.
This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity.
CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] = (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
oxalate + oxidized 2[4Fe-4S]-[ferredoxin] = 2 CO2 + reduced 2[4Fe-4S]-[ferredoxin].
For example, see EC 1.2.7.3 and EC 1.2.7.7.
a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
The enzyme catalyzes a reversible reaction in methanogenic archaea, and is involved in methanogenesis from CO2 as well as the oxidation of coenzyme M to CO2.
The reaction is endergonic, and is driven by coupling with the soluble CoB-CoM heterodisulfide reductase via electron bifurcation.
H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin].
Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP(+) by reaction with a second formaldehyde, yielding methanol.
The enzyme from Mycobacterium sp. DSM 3803 also catalyzes the reactions of EC 1.1.99.36 and EC 1.1.99.37.
Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors.
2 formaldehyde + H2O = formate + H(+) + methanol.
In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols.
A + an aldehyde + H2O = a carboxylate + AH2 + H(+).
aldehyde dehydrogenase (FAD-independent)
glyceraldehyde dehydrogenase (FAD-containing)
The enzyme from the archaeon Sulfolobus acidocaldarius catalyzes the oxidation of D-glyceraldehyde in the nonphosphorylative Entner-Doudoroff pathway.
With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde.
It is not known which acceptor is utilized in vivo.
A + D-glyceraldehyde + H2O = (R)-glycerate + AH2 + H(+).
The enzyme has been described from the bacteria Methylomonas sp. 16a and Bacillus indicus.
A + all-trans-4,4'-diapolycopen-4-al + H2O = AH2 + all-trans-4,4'-diapolycopen-4-oate + H(+).
2 A + all-trans-4,4'-diapolycopene-4,4'-dial + 2 H2O = 2 AH2 + all-trans-4,4'-diapolycopene-4,4'-dioate + 2 H(+).
The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth.
Since then the enzyme was found in additional organisms including Alcaligenes eutrophus, Pseudomonas strains and Escherichia coli.
5,6-dihydrouracil + NAD(+) = H(+) + NADH + uracil.
5,6-dihydrothymine + NAD(+) = H(+) + NADH + thymine.
dihydropyrimidine dehydrogenase (NADP(+))
5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil.
5,6-dihydrothymine + NADP(+) = H(+) + NADPH + thymine.
The enzyme from human efficiently catalyzes the reduction of progesterone, androstenedione, 17alpha-hydroxyprogesterone and testosterone to 5beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent.
The bile acid intermediates 7alpha,12alpha-dihydroxy-4-cholesten-3-one and 7alpha-hydroxy-4-cholesten-3-one can also act as substrates.
5beta-cholestan-3-one + NADP(+) = cholest-4-en-3-one + H(+) + NADPH.
4,5beta-dihydrocortisone + NADP(+) = cortisone + H(+) + NADPH.
5beta-dihydrotestosterone + NADP(+) = H(+) + NADPH + testosterone.
Iron or zinc can replace manganese to some extent.
23,24-dihydrocucurbitacin B + NADP(+) = cucurbitacin B + H(+) + NADPH.
23,24-dihydrocucurbitacin B + NAD(+) = cucurbitacin B + H(+) + NADH.
NAD(+) + succinate = fumarate + H(+) + NADH.
(2R,3S)-tartrate + NAD(+) = dihydroxyfumarate + H(+) + NADH.
The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA.
In Escherichia coli, cis-specific and trans-specific enzymes exist (cf. EC 1.3.1.37 and EC 1.3.1.38).
a 2,3-saturated acyl-CoA + NADP(+) = a 2,3-dehydroacyl-CoA + H(+) + NADPH.
enoyl-[acyl-carrier-protein] reductase (NADH)
NADH-enoyl acyl carrier protein reductase
The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety.
The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18.
The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH.
enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
One of the activities of EC 2.3.1.86, an enzyme found in yeasts (Ascomycota and the Basidiomycota).
Catalyzes the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16.
The yeast enzyme is Si-specific with respect to NADP(+).
Cf. EC 1.3.1.39 and EC 1.3.1.104 which describes enzymes whose stereo-specificity toward NADPH is not known.
a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH.
3-(2-hydroxyphenyl)propanoate + NAD(+) = H(+) + NADH + trans-2-coumarate.
chorismate mutase--prephenate dehydrogenase
This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate.
NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH.
NADP(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADPH.
The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit.
The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides.
Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP(+) (EC 1.3.1.15) as electron acceptor.
The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
(S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate.
Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NAD(+) (EC 1.3.1.14) as electron acceptor.
(S)-dihydroorotate + NADP(+) = H(+) + NADPH + orotate.
3-nitropropanoate + NADP(+) = 3-nitroacrylate + H(+) + NADPH.
3-methyloxindole + NADP(+) = 3-methyleneoxindole + H(+) + NADPH.
kynurenate-7,8-dihydrodiol dehydrogenase
7,8-dihydro-7,8-dihydroxykynurenate + NAD(+) = 7,8-dihydroxykynurenate + H(+) + NADH.
cis-1,2-dihydrobenzene-1,2-diol dehydrogenase
cis-1,2-dihydrobenzene-1,2-diol + NAD(+) = catechol + H(+) + NADH.
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD(+) = 3-methylcatechol + H(+) + NADH.
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + H(+) + NADPH.
(1S,2S)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + H(+) + NADPH.
7-dehydrocholesterol dehydrogenase/cholesterol oxidase
The enzyme is part of the cholesterol biosynthesis pathway.
cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH.
3-oxo-5alpha-steroid 4-dehydrogenase (NADP(+))
The enzyme catalyzes the conversion of assorted 3-oxo-Delta(4) steroids into their corresponding 5alpha form.
Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone.
Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22alpha)-hydroxy-campest-4-en-3-one.
a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH.
5alpha-pregnane-3,20-dione + NADP(+) = H(+) + NADPH + progesterone.
17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = H(+) + NADPH + testosterone.
bilirubin IXalpha + NADP(+) = biliverdin IXalpha + H(+) + NADPH.
bilirubin IXalpha + NAD(+) = biliverdin IXalpha + H(+) + NADH.
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
2-hydro-1,2-dihydroxybenzoate dehydrogenase
3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase
3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase
cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD(+) oxidoreductase
cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+) = catechol + CO2 + NADH.
Specific for long chain 2-trans- and 2-cis-alkenals, with chain length optimum around 14 to 16 carbon atoms.
hexadecanal + NADP(+) = (2E)-hexadecenal + H(+) + NADPH.
2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD(+) = 2,3-dihydroxybenzoate + H(+) + NADH.
cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase
cis-dihydrodiol naphthalene dehydrogenase
cis-naphthalene dihydrodiol dehydrogenase
Also acts, at half the rate, on cis-anthracene dihydrodiol and cis-phenanthrene dihydrodiol.
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+) = H(+) + NADH + naphthalene-1,2-diol.
Acts, in the reverse direction, on a wide range of alkyl and aryl alphabeta-unsaturated carboxylate ions; 2-butenoate was the best substrate tested.
butanoate + NAD(+) = (2E)-2-butenoate + H(+) + NADH.
3-oxoadipate + NAD(+) = H(+) + maleylacetate + NADH.
3-oxoadipate + NADP(+) = H(+) + maleylacetate + NADPH.
light-dependent protochlorophyllide reductase
NADPH-protochlorophyllide oxidoreductase
Catalyzes a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a.
2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]
This bacterial enzyme catalyzes the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA.
The enzyme from Escherichia coli contains FAD, FMN, and an [4Fe-4S] iron sulfur cluster.
a 4,5-saturated-(2E)-enoyl-CoA + NADP(+) = a (2E,4E)-dienoyl-CoA + H(+) + NADPH.
a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(2E)-enoyl-CoA + NADP(+).
Involved in the interconversion of heteroyohimbine alkaloids in Catharanthus roseus.
(19E)-geissoschizine + NADP(+) = 4,21-dehydrogeissoschizine + NADPH.
Not identical with EC 1.3.1.38 (cf. EC 1.3.1.8).
acyl-CoA + NADP(+) = cis-2,3-dehydroacyl-CoA + NADPH + H(+).
Not identical with EC 1.3.1.37 (cf. EC 1.3.1.8).
a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA + NADP(+).
enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific)
This enzyme completes each cycle of fatty acid elongation by catalyzing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein.
It is one of the activities of EC 2.3.1.85.
The mammalian enzyme is Re-specific with respect to NADP(+) (cf. EC 1.3.1.10 and and EC 1.3.1.104).
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase
Broad specificity; reduces a number of compounds produced by Pseudomonas from aromatic hydrocarbons by ring fission.
2,6-dioxo-6-phenylhexanoate + NADP(+) = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H(+) + NADPH.
5,12-dihydroxanthommatin + NAD(+) = H(+) + NADH + xanthommatin.
Involved in the conversion of linolenate into jasmonate in Zea mays.
(1S,2S)-OPC-8 + NADP(+) = (10Z,15Z)-12-oxophytodienoate + H(+) + NADPH.
Arogenate dehydrogenases may utilize NAD(+) (EC 1.3.1.43), NADP(+) (EC 1.3.1.78), or both (EC 1.3.1.79).
NAD(+)-specific enzymes have been reported from some bacteria and plants.
Some enzymes also possess the activity of EC 1.3.1.12.
L-arogenate + NAD(+) = CO2 + L-tyrosine + NADH.
The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) + NADH.
In the reverse reaction, a 2'-hydroxyisoflavone is reduced to an isoflavanone; 2'-hydroxypseudobaptigenin also acts.
Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain.
(3R)-vestitone + NADP(+) = 2'-hydroxyformononetin + 2 H(+) + NADPH.
Some other isoflavones are reduced to the corresponding isoflavanones.
2,3-dihydrobiochanin A + NADP(+) = biochanin A + 2 H(+) + NADPH.
1,2-dihydro-alpha-santonin + NAD(+) = alpha-santonin + H(+) + NADH.
1,2-dihydro-alpha-santonin + NADP(+) = alpha-santonin + H(+) + NADPH.
15-oxo-Delta(13)-prostaglandin reductase
Reduces 15-oxoprostaglandins to 13,14-dihydro derivatives.
The enzyme from placenta is specific for NAD(+).
13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-oxoprostaglandin E2 + H(+) + NADPH.
13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-oxoprostaglandin E2 + H(+) + NADH.
cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase
(3S,4R)-3,4-dihydrophenanthrene-3,4-diol + NAD(+) = H(+) + NADH + phenanthrene-3,4-diol.
2'-hydroxydihydrodaidzein:NADP(+) 2'-oxidoreductase
In the reverse reaction, the 2'-hydroxyisoflavone (2'-hydroxydaidzein) is reduced to an isoflavanone.
Also acts on 2'-hydroxyformononetin and to a small extent on 2'-hydroxygenistein.
Involved in the biosynthesis of the phytoalexin glyceollin.
The isoflavones biochanin A, daidzein and genestein as well as the flavonoids apigenin, kaempferol and quercetin do not act as substrates.
2'-hydroxy-2,3-dihydrodaidzein + NADP(+) = 2'-hydroxydaidzein + 2 H(+) + NADPH.
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase
dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase
Involved in the terephthalate degradation pathway in bacteria.
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD(+) = 3,4-dihydroxybenzoate + CO2 + NADH.
The enzyme, which participates in the aerobic (late cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyzes the reduction of the double bond between C-18 and C-19 of precorrin-6A.
See EC 1.3.1.106 for the corresponding enzyme that participates in the anaerobic cobalamin biosynthesis pathway.
NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A.
cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
biphenyl-2,3-dihydro-2,3-diol dehydrogenase
Catalyzes the second step in the biphenyl degradation pathway in bacteria.
(2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+) = biphenyl-2,3-diol + H(+) + NADH.
Involved in the gallate anaerobic degradation pathway in bacteria.
dihydrophloroglucinol + NADP(+) = 1,3,5-trihydroxybenzene + NADPH.
2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase
Involved in the p-cymene and p-cumate degradation pathways in Pseudomonas putida.
(2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD(+) = 2,3-dihydroxy-p-cumate + H(+) + NADH.
dibenzothiophene dihydrodiol dehydrogenase
Involved in the dibenzothiophene degradation pathway in bacteria.
cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD(+) = 1,2-dihydroxydibenzothiophene + H(+) + NADH.
Involved in the benzoate degradation (anaerobic) pathway in bacteria.
6-carboxyhexanoyl-CoA + NAD(+) = 6-carboxyhex-2-enoyl-CoA + H(+) + NADH.
phthalate 4,5-cis-dihydrodiol dehydrogenase
Involved in the phthalate degradation pathway in bacteria.
cis-4,5-dihydroxycyclohexa-2,6-diene-1,2-dicarboxylate + NAD(+) = 4,5-dihydroxyphthalate + H(+) + NADH.
5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase
Acts in the reverse direction to form part of the 3-methylquinoline degradation pathway in bacteria.
5,6-dihydroxy-3-methyl-5,6-dihydroquinolin-2(1H)-one + NAD(+) = 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + H(+) + NADH.
Involved in the ethylbenzene degradation pathway in bacteria.
cis-1,2-dihydro-3-ethylcatechol + NAD(+) = 3-ethylcatechol + H(+) + NADH.
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase
Involved in the p-xylene degradation pathway in bacteria.
(1R,6S)-1,6-dihydroxy-4-methylcyclohexa-2,4-diene-1-carboxylate + NADP(+) = 4-methylcatechol + CO2 + NADPH.
(1R,6S)-1,6-dihydroxy-4-methylcyclohexa-2,4-diene-1-carboxylate + NAD(+) = 4-methylcatechol + CO2 + NADH.
1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase
Involved in the o-xylene degradation pathway in bacteria.
1,6-dihydroxy-2-methylcyclohexa-2,4-dienecarboxylate + NAD(+) = 3-methylcatechol + CO2 + NADH.
dihydrozeatin + NADP(+) = H(+) + NADPH + zeatin.
Acts on a range of steroids with a 14(15)-double bond.
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH.
sterol Delta(24(28))-methylene reductase
Acts on a range of steroids with a 24(24(1))-double bond.
ergosterol + NADP(+) = ergosta-5,7,22,24(28)-tetraen-3beta-ol + H(+) + NADPH.
Acts on a range of steroids with a 24(25)-double bond, including lanosterol, desmosterol and zymosterol.
lathosterol + NADP(+) = 5alpha-cholesta-7,24-dien-3beta-ol + H(+) + NADPH.
cholesterol + NADP(+) = desmosterol + H(+) + NADPH.
7-dehydrocholesterol + NADP(+) = 7-dehydrodesmosterol + H(+) + NADPH.
5alpha-cholest-8-en-3beta-ol + NADP(+) = H(+) + NADPH + zymosterol.
Forms part of the ajmaline biosynthesis pathway.
17-O-acetylnorajmaline + NADP(+) = 1,2-dihydrovomilenine + 2 H(+) + NADPH.
NAD(P)H-dependent alkenal/one oxidoreductase
Highly specific for 4-hydroxynon-2-enal and non-2-enal.
Alk-2-enals of shorter chain have lower affinities.
Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
an n-alkanal + NAD(+) = an alk-2-enal + H(+) + NADH.
an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH.
3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)
divinyl chlorophyllide a 8-vinyl-reductase
plant-type divinyl chlorophyllide a 8-vinyl-reductase
The enzyme, found in higher plants, green algae, and some phototrophic bacteria, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors.
It can also act on 3,8-divinyl chlorophyllide a.
NADP(+) + protochlorophyllide a = 3,8-divinyl protochlorophyllide a + H(+) + NADPH.
chlorophyllide a + NADP(+) = 3,8-divinyl chlorophyllide a + H(+) + NADPH.
Catalyzes the second of three steps leading to the formation of siroheme from uroporphyrinogen III.
The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4).
In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.
In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction.
NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin.
anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming]
The enzyme participates in the flavonoid biosynthesis pathway found in plants.
It catalyzes the double reduction of anthocyanidins, producing (2R,3R)-flavan-3-ol monomers required for the formation of proanthocyanidins.
While the enzyme from the legume Medicago truncatula can use both NADPH and NADH as reductant, that from the crucifer Arabidopsis thaliana uses only NADPH.
Also, while the substrate preference of the M. truncatula is cyanidin>pelargonidin>delphinidin, the reverse preference is found with the Arabidopsis enzyme. cf. EC 1.3.1.112.
a (2R,3R)-flavan-3-ol + 2 NAD(+) = an anthocyanidin with a 3-hydroxy group + 2 H(+) + 2 NADH.
a (2R,3R)-flavan-3-ol + 2 NADP(+) = an anthocyanidin with a 3-hydroxy group + 2 H(+) + 2 NADPH.
NADP(+)-dependent enzymes usually predominate in higher plants.
The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly.
L-arogenate + NADP(+) = CO2 + L-tyrosine + NADPH.
Enzymes that can utilize both cofactors have been reported from some Proteobacteria, including Burkholderia caryophylli, Burkholderia cepacia, Pseudomonas marginata and Delftia acidovorans.
The Delta(8,9)-double bond of (+)-cis-isopulegone and the Delta(1,2)-double bond of (+-)-piperitone are not substrates.
The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyze the reverse reaction.
(1R,4S)-menthone + NADP(+) = (R)-pulegone + H(+) + NADPH.
(2R,5R)-isomenthone + NADP(+) = (R)-pulegone + H(+) + NADPH.
The reaction occurs in the opposite direction to that shown above.
Participates in the menthol-biosynthesis pathway of Mentha plants.
(+)-Pulegone, (+)-cis-isopulegone and (-)-menthone are not substrates.
Has a preference for NADPH as the reductant, with NADH being a poor substitute.
Highly regioselective for the reduction of the endocyclic 1,2-double bond, and is stereoselective, producing only the 1R-configured product.
(2R,5R)-isopulegone + NADP(+) = (6R)-isopiperitenone + H(+) + NADPH.
This enzyme also acts on geranylgeranyl-chlorophyll a.
Which order the three double bonds are reduced is not known.
3 NADP(+) + phytyl diphosphate = geranylgeranyl diphosphate + 3 H(+) + 3 NADPH.
Catalyzes a step in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea.
The reaction is catalyzed in the opposite direction to that shown.
The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA.
Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16.
NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH.
This enzyme, isolated from the bacterium Rhodobacter sphaeroides, catalyzes (E)-but-2-enoyl-CoA-dependent oxidation of NADPH in the presence of CO2.
When CO2 is absent, the enzyme catalyzes the reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA, but with only 10% of maximal activity (relative to (E)-but-2-enoyl-CoA carboxylation).
(2S)-ethylmalonyl-CoA + NADP(+) = (2E)-butenoyl-CoA + CO2 + NADPH.
short-chain acyl-coenzyme A dehydrogenase
Catalyzes the reaction in the reverse direction.
This enzyme from Streptomyces collinus is specific for (E)-but-2-enoyl-CoA, and is proposed to provide butanoyl-CoA as a starter unit for straight-chain fatty acid biosynthesis.
butanoyl-CoA + NADP(+) = (2E)-butenoyl-CoA + H(+) + NADPH.
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase
2,3-dihydroxy-2,3-dihydro-phenylpropionate dehydrogenase
This enzyme catalyzes a step in the pathway of phenylpropanoid compounds degradation.
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+) = 3-(2,3-dihydroxyphenyl)propanoate + H(+) + NADH.
(2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD(+) = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H(+) + NADH.
tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]
The enzyme specifically modifies uracil(16) and uracil(17) in tRNA.
5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH + uridine(16) in tRNA.
5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH + uridine(16) in tRNA.
5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH + uridine(17) in tRNA.
5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH + uridine(17) in tRNA.
tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
The enzyme specifically modifies uracil(47) in tRNA.
5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH + uridine(47) in tRNA.
5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA.
tRNA-dihydrouridine(20a/20b) synthase [NAD(P)(+)]
The enzyme specifically modifies uracil(20a) and uracil(20b) in tRNA.
5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH + uridine(20a) in tRNA.
5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH + uridine(20a) in tRNA.
5,6-dihydrouridine(20b) in tRNA + NAD(+) = H(+) + NADH + uridine(20b) in tRNA.
5,6-dihydrouridine(20b) in tRNA + NADP(+) = H(+) + NADPH + uridine(20b) in tRNA.
tRNA-dihydrouridine(20) synthase [NAD(P)(+)]
The enzyme specifically modifies uracil(20) in tRNA.
5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH + uridine(20) in tRNA.
5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + uridine(20) in tRNA.
artemisinic aldehyde Delta(11(13)) reductase
In addition to the reduction of artemisinic aldehyde it is also able to a lesser extent to reduce artemisinic alcohol and artemisinic acid.
(11R)-dihydroartemisinic aldehyde + NADP(+) = (+)-artemisinic aldehyde + H(+) + NADPH.
This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs.
a very-long-chain 2,3-saturated fatty acyl-CoA + NADP(+) = a very-long-chain (2E)-enoyl-CoA + H(+) + NADPH.
The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group.
Isolated from human fetal brain tissue but present in all eukaryotes.
In mammalian cells dolichols are predominantly 18-21 isoprene units in length.
di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol + H(+) + NADPH.
The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF).
The ETF is reduced by NADH and transfers the electrons to the active site.
Catalyzes a step in a pathway for L-alanine fermentation to propanoate.
NAD(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADH.
Isolated from the green alga Botryococcus braunii BOT22.
cf. EC 2.5.1.21, where squalene is formed directly from farnesyl diphosphate.
H(+) + NADPH + presqualene diphosphate = diphosphate + NADP(+) + squalene.
Involved in the production of botryococcenes, which are triterpenoid hydrocarbons of isoprenoid origin produced in large amount by this alga.
C30 botryococcene + diphosphate + NADP(+) = H(+) + NADPH + presqualene diphosphate.
UDP-N-acetylenolpyruvoylglucosamine reductase
UDP-N-acetylglucosamine-enoylpyruvate reductase
uridine diphosphoacetylpyruvoylglucosamine reductase
uridine diphospho-N-acetylglucosamine-enolpyruvate reductase
NADH can to a lesser extent replace NADPH.
NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.
The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family.
The enzyme catalyzes the reduction of chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde.
This hydrolyzes spontaneously to form 6,8-dimethyl-6,7-didehydroergoline, which is converted to festuclavine by EC 1.5.1.44.
dihydrochanoclavine-I aldehyde + NADP(+) = chanoclavine-I aldehyde + H(+) + NADPH.
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]
2,3-digeranylgeranylglycerophospholipid reductase
digeranylgeranylglycerophospholipid reductase
The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids.
In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate.
2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 NADP(+) = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + 8 H(+) + 8 NADPH.
2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 NAD(+) = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + 8 H(+) + 8 NADH.
NADPH-dependent alkenal/one oxidoreductase
Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde.
Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones.
Has very low activity with NAD as reductant (cf. EC 1.3.1.74).
1-nitrocyclohexan + NADP(+) = 1-nitrocyclohexene + H(+) + NADPH.
The enzyme acts in the degradation pathway of unsaturated organohalogen compounds by the bacterium Burkholderia sp. WS.
(S)-2-chloropropanoate + NADP(+) = 2-chloroacrylate + H(+) + NADPH.
The enzyme completes each cycle of fatty acid elongation by catalyzing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner.
This entry stands for enzymes whose stereo-specificity with respect to NADP(+) is not known (cf. EC 1.3.1.39, EC 1.3.1.10 and EC 1.3.1.9).
The enzyme was dicovered in strawberry (Fragaria x ananassa), where it produces furaneol, one of the major aroma compounds in the fruits.
It has also been detected in tomato (Solanum lycopersicum) and pineapple (Ananas comosus).
The enzyme can also act on derivatives substituted at the methylene functional group.
The enzyme from the yeast Saccharomyces cerevisiae acts on (2E)-2-ethylidene-4-hydroxy-5-methylfuran-3(2H)-one and produces homofuraneol, an important aroma compound in soy sauce and miso.
4-hydroxy-2,5-dimethyl-furan-3(2H)-one + NADP(+) = 4-hydroxy-5-methyl-2-methylenefuran-3(2H)-one + H(+) + NADPH.
4-hydroxy-2,5-dimethyl-furan-3(2H)-one + NAD(+) = 4-hydroxy-5-methyl-2-methylenefuran-3(2H)-one + H(+) + NADH.
2-ethyl-4-hydroxy-5-methyl-3(2H)-furanone + NADP(+) = (2E)-2-ethylidene-4-hydroxy-5-methylfuran-3(2H)-one + H(+) + NADPH.
The enzyme, which participates in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyzes the reduction of the double bond between C-18 and C-19 of cobalt-precorrin-6A.
The enzyme from the bacterium Bacillus megaterium has no activity with NADPH.
See EC 1.3.1.54 for the corresponding enzyme that participates in the aerobic cobalamin biosynthesis pathway.
Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH.
The enzyme, purified from the California poppy (Eschscholzia californica), is involved in detoxifying the phytoalexin sanguinarine produced by poppy itself (cf. EC 1.5.3.12), when it binds to the cell wall of the poppy cell.
The reaction with NADPH is up to three times faster than that with NADH at low concentrations (<10 uM) of the dinucleotide.
At higher concentrations the reaction with NADPH is inhibited but not that with NADH.
dihydrosanguinarine + NADP(+) = NADPH + sanguinarine.
dihydrosanguinarine + NAD(+) = NADH + sanguinarine.
dihydrochelirubine + NAD(+) = chelirubine + NADH.
dihydrochelirubine + NADP(+) = chelirubine + NADPH.
electron-bifurcating caffeoyl-CoA reductase
The enzyme, characterized from the bacterium Acetobacterium woodii, couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant.
It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
It also reduces 4-coumaroyl-CoA and feruloyl-CoA.
hydrocaffeoyl-CoA + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = (E)-caffeoyl-CoA + 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin].
butanoyl-CoA dehydrogenase complex (NAD(+), ferredoxin)
The enzyme is a complex of a flavin-containing dehydrogenase component (Bcd) and an electron-transfer flavoprotein dimer (EtfAB).
The enzyme complex, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA by NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
butanoyl-CoA + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = (2E)-butenoyl-CoA + 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin].
lactate dehydrogenase (NAD(+),ferredoxin)
The enzyme, isolated from the bacterium Acetobacterium woodii, uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD(+) as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD(+).
lactate + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate.
geranylgeranyl-bacteriochlorophyllide a reductase
The enzyme catalyzes the successive reduction of the geranylgeraniol esterifying group to phytol, reducing three out of four double bonds, and transforming geranylgeranyl bacteriochlorophyllide a via dihydrogeranylgeranyl bacteriochlorophyllide a and tetrahydrogeranylgeranyl bacteriochlorophyllide a to bacteriochlorophyll a.
The enzyme can also accept the pheophytin derivative geranylgeranyl bacteriopheophytin, converting it to bacteriopheophytin a.
bacteriochlorophyll a + 3 NADP(+) = geranylgeranyl-bacteriochlorophyllide a + 3 H(+) + 3 NADPH.
anthocyanidin reductase [(2S)-flavan-3-ol-forming]
The enzyme, characterized from Vitis vinifera (grape), participates in the flavonoid biosynthesis pathway.
It catalyzes the double reduction of anthocyanidins, producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols.
The enzyme catalyzes sequential hydride transfers to C-2 and C-4, respectively.
Epimerization at C-3 is achieved by tautomerization that occurs between the two hydride transfers.
a (2S,3R)-flavan-3-ol + 2 NADP(+) = an anthocyanidin with a 3-hydroxy group + 2 H(+) + 2 NADPH.
a (2S,3S)-flavan-3-ol + 2 NADP(+) = an anthocyanidin with a 3-hydroxy group + 2 H(+) + 2 NADPH.
(4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate reductase
The enzyme, characterized from the bacteria Streptomyces griseus and Streptomyces coelicolor, is involved in the biosynthesis of gamma-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.
a [(3S,4R)-4-alkanoyl-5-oxooxolan-3-yl]methyl phosphate + NADP(+) = a (4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate + H(+) + NADPH.
[(3S,4R)-4-(6-methylheptanoyl)-5-oxooxolan-3-yl]methyl phosphate + NADP(+) = [4-(6-methylheptanoyl)-5-oxo-2H-furan-3-yl]methyl phosphate + H(+) + NADPH.
3-dehydro-bile acid Delta(4,6)-reductase
The enzyme, characterized from the bacterium Clostridium scindens, participates in the bile acid 7alpha-dehydroxylation pathway.
The enzyme catalyzes two subsequent reductions of the double bonds within the bile acid A/B rings, following 7alpha-dehydration.
3-oxocholan-24-oyl-CoA + NAD(+) = 3-oxochol-4-en-24-oyl-CoA + H(+) + NADH.
3-oxochol-4-en-24-oyl-CoA + NAD(+) = 3-oxochol-4,6-dien-24-oyl-CoA + H(+) + NADH.
12alpha-hydroxy-3-oxocholan-24-oyl-CoA + NAD(+) = 12alpha-hydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH.
12alpha-hydroxy-3-oxochol-4-en-24-oyl-CoA + NAD(+) = 12alpha-hydroxy-3-oxochola-4,6-dien-24-oyl-CoA + H(+) + NADH.
The enzyme catalyzes the stereo-specific oxidation of its substrates and has no activity with the 7beta anomers.
7alpha,12alpha-dihydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH.
7alpha-hydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7alpha-hydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH.
7beta-hydroxy-3-oxochol-24-oyl-CoA 4-desaturase
The enzyme catalyzes the stereo-specific oxidation of its substrate and has no activity with the 7alpha anomer.
7beta-hydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7beta-hydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH.
hydroxycinnamoyl-CoA double bond reductase
Isolated from Malus X domestica (apple).
Involved in dihydrochalcone biosynthesis.
dihydro-4-coumaroyl-CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH.
dihydroferuloyl-CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH.
meromycolic acid enoyl-[acyl-carrier-protein] reductase
InhA is a component of the fatty acid synthase (FAS) II system of Mycobacterium tuberculosis, catalyzing an enoyl-[acyl-carrier-protein] reductase step.
The enzyme acts on very long and unsaturated fatty acids that form the meromycolic component of mycolic acids.
It extends FASI-derived C20 fatty acids to form C60 to C90 mycolic acids.
The enzyme, which forms a homotetramer, is the target of the preferred antitubercular drug isoniazid.
a 2,3-saturated meromycolyl-[ACP] + NAD(+) = a trans-Delta(2)-meromycolyl-[ACP] + H(+) + NADH.
This bacterial enzyme can transform various dihydrodiols of chlorobenzenes into the respective catechols, including the dihydrodiols of mono-, di-, tri-, and tetra-chlorinated benzenes.
It also accepts the dihydrodiols of various chlorotoluenes.
Substrates for the enzyme are generated by the broad spectrum EC 1.14.12.26.
(1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD(+) = 3-chlorocatechol + H(+) + NADH.
cyclohexane-1-carbonyl-CoA reductase (NADP(+))
The enzyme, characterized from the bacterium Streptomyces collinus, is involved in a pathway that transforms shikimate to cyclohexane-1-carbonyl-CoA by a series of dehydration and double-bond reduction steps.
Most of the steps in this process occur with the carboxylic acid activated as a coenzyme A thioester.
The enzyme catalyzes three steps in this pathway, also acting on (3R,4R)-3,4-dihydroxy-3,4-dihydrobenzoyl-CoA and (5S)-5-hydroxycyclohex-1-ene-1-carbonyl-CoA.
cyclohexane-1-carbonyl-CoA + NADP(+) = cyclohex-1-ene-1-carbonyl-CoA + H(+) + NADPH.
(4R,5R)-4,5-dihydroxycyclohex-2-ene-1-carbonyl-CoA + NADP(+) = (3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carbonyl-CoA + H(+) + NADPH.
(3S)-3-hydroxycyclohexane-1-carbonyl-CoA + NADP(+) = (5S)-5-hydroxycyclohex-1-ene-1-carbonyl-CoA + H(+) + NADPH.
The enzyme, characterized from the bacteria Streptomyces venezuelae and Streptomyces pristinaespiralis, participates in the biosynthesis of the antibiotics chloramphenicol and pristinamycin IA, respectively.
4-amino-4-deoxyprephenate + NAD(+) = 3-(4-aminophenyl)pyruvate + CO2 + H(+) + NADH.
Isolated from the plants Catharanthus roseus, Olea europaea (common olive), and several Nepeta species.
The enzyme reduces 8-oxogeranial, generating an unstable product that is subsequently cyclized into several possible products, either non-enzymically or by dedicated cyclases.
The products, known as iridoids, are involved in the biosynthesis of many indole alkaloids.
(S)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial + H(+) + NADPH.
(S)-8-oxocitronellyl enol + NAD(+) = (6E)-8-oxogeranial + H(+) + NADH.
The enzyme, characterized from the plant Antirrhinum majus (snapdragon), is involved in biosynthesis of 7-epi-iridoids such as antirrhinoside.
The enzyme catalyzes the stereospecific reduction of 8-oxogeranial, forming an unstable product that in the absence of additional cylases undergoes spontaneous cyclization to (-)-cis,trans-nepetalactol.
(R)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial + H(+) + NADPH.
2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]
This enzyme, characterized from eukaryotic organisms, catalyzes the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (3E)-3-enoyl-CoA.
The best substrates for the enzyme from bovine liver have a chain-length of 8 or 10.
Mammals possess both mitochondrial and peroxisomal variants of this enzyme.
a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-enoyl-CoA + NADP(+).
a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-enoyl-CoA + NADP(+).
NADPH-dependent curcumin/dihydrocurcumin reductase
The enzyme, from the bacterium Escherichia coli is also active with 3-octene-2-one (59.7%), 3-hepten-2-one (28%), and resveratrol (14.8%).
2 NADP(+) + tetrahydrocurcumin = curcumin + 2 H(+) + 2 NADPH.
NADP(+) + tetrahydrocurcumin = dihydrocurcumin + H(+) + NADPH.
dihydrocurcumin + NADP(+) = curcumin + H(+) + NADPH.
Catalyzes the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds.
Very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma-lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates.
FAD, NAD(+), NADP(+) and O2 (cf. EC 1.3.3.12) cannot act as electron acceptor.
4 Fe(III)-[cytochrome c] + L-galactono-1,4-lactone = 4 Fe(II)-[cytochrome c] + 5 H(+) + L-dehydroascorbate.
coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX.
Also slowly oxidizes mesoporphyrinogen IX.
3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX.
2 bilirubin IXalpha + O2 = 2 biliverdin IXalpha + 2 H2O.
Acts on CoA derivatives of fatty acids with chain length from C8 to C18.
a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2.
Also oxidizes dihydrothymine to thymine.
(R)-tetrahydroberberines are not oxidized.
(S)-canadine + H(+) + 2 O2 = berberine + 2 H2O2.
The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring.
Also catalyzes the alpha,beta dehydrogenation of L-tryptophan side chains in peptides.
The product of the reaction can hydrolyze spontaneously to form indolepyruvate.
L-tryptophan + O2 = alpha,beta-didehydrotryptophan + H2O2.
So far only a single turnover of the enzyme has been observed, and the pyrroloquinoline quinone remains bound to it; it is not yet known what releases the product in the bacterium.
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = H(+) + 2 H2O + 2 H2O2 + pyrroloquinoline quinone.
Acts on the 1,4-lactones of L-galactonic, D-altronic, L-fuconic, D-arabinic and D-threonic acids.
Not identical with EC 1.1.3.8 (cf. EC 1.3.2.3).
L-galactono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate.
The enzyme can also oxidize several other cyclo dipeptides, the best being cyclo(L-tryptophyl-L-tryptophyl) and cyclo(L-phenylalanyl-L-phenylalanyl).
cyclo(L-phenylalanyl-L-leucyl) + 2 O2 = albonoursin + 2 H2O2.
The enzyme utilizes the same active site to catalyze the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y.
aclacinomycin A + O2 = aclacinomycin Y + H2O2.
coproporphyrinogen III oxidase (coproporphyrin-forming)
The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis.
It can also catalyze the reaction of EC 1.3.3.4 at a lower level.
coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2.
This enzyme oxidizes 2-oxazoline, 5-methyl-2-oxazoline, and 2-thiazoline within peptides, which were formed by EC 6.2.2.2 and EC 6.2.2.3 to the respective pyrrole-type rings.
The enzyme is found as either a stand-alone protein or as a domain within a multifunctional protein (the G protein) that also functions as a peptidase.
(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline-[protein] + O2 = (S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole-[protein] + H2O2.
(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline-[protein] + O2 = (S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole-[protein] + H2O2.
(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline-[protein] + O2 = (S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole-[protein] + H2O2.
The enzyme, isolated from the archaeon Methanobacterium thermoautotrophicum, is very oxygen sensitive.
It cannot use reduced flavins, reduced coenzyme F420, or NAD(P)H as an electron donor.
coenzyme B + coenzyme M + fumarate = coenzyme M-coenzyme B heterodisulfide + succinate.
With a quinone or related compound as acceptor
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones.
The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively.
Under aerobic conditions the enzyme catalyzes succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II).
Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor.
The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit.
These enzymes catalyze an electrogenic reaction and are thus classified as EC 7.1.1.12.
a quinone + succinate = a quinol + fumarate.
a ubiquinone + succinate = a ubiquinol + fumarate.
a menaquinone + succinate = a menaquinol + fumarate.
This Class 2 dihydroorotate dehydrogenase enzyme contains FMN.
The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane.
The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides.
The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates.
Methyl-, ethyl-, tert-butyl and benzyl-(S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not.
Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor.
(S)-dihydroorotate + a quinone = a quinol + orotate.
(S)-dihydroorotate + a ubiquinone = a ubiquinol + orotate.
(S)-dihydroorotate + ubiquinone-8 = orotate + ubiquinol-8.
protoporphyrinogen IX dehydrogenase (quinone)
protoporphyrinogen IX dehydrogenase (menaquinone)
The enzyme participates in heme b biosynthesis.
In the bacterium Escherichia coli it interacts with either ubiquinone or menaquinone, depending on whether the organism grows aerobically or anaerobically.
3 a quinone + protoporphyrinogen IX = 3 a quinol + protoporphyrin IX.
3 a menaquinone + protoporphyrinogen IX = 3 a menaquinol + protoporphyrin IX.
3 a ubiquinone + protoporphyrinogen IX = 3 a ubiquinol + protoporphyrin IX.
The enzyme, which is found in anaerobic and facultative organisms such as bacteria, parasitic helminthes, and lower marine organisms, utilizes low potential quinols, such as menaquinol and rhodoquinol, to reduce fumarate as the final step of an anaerobic respiratory chain.
The enzyme is known as complex II of the electron transfer chain, similarly to EC 1.3.5.1, to which it is closely related.
This enzyme is involved in carotenoid biosynthesis in plants and cyanobacteria.
The enzyme from Synechococcus can also use NAD(+) and NADP(+) as electron acceptor under anaerobic conditions.
The enzyme from Gentiana lutea shows no activity with NAD(+) or NADP(+).
15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-carotene + 2 a plastoquinol.
15-cis-phytoene + 2 plastoquinone-9 = 9,9',15-tri-cis-zeta-carotene + 2 plastoquinol-9.
9,9'-di-cis-zeta-carotene + 2 a quinone = 7,7',9,9'-tetra-cis-lycopene + 2 a quinol.
6-oxotetrahydro-nicotinate dehydrogenase
1,4,5,6-tetrahydro-6-oxonicotinate + oxidized 2[4Fe-4S]-[ferredoxin] = 6-hydroxynicotinate + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin].
15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Catalyzes the two-electron reduction of biliverdin IXalpha at the C15 methine bridge.
It has been proposed that this enzyme and EC 1.3.7.3 function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin.
15,16-dihydrobiliverdin + oxidized 2[4Fe-4S]-[ferredoxin] = biliverdin IXalpha + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin].
phycoerythrobilin:ferredoxin oxidoreductase
Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin.
It has been proposed that this enzyme and EC 1.3.7.2 function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin.
(3Z)-phycoerythrobilin + oxidized 2[4Fe-4S]-[ferredoxin] = 15,16-dihydrobiliverdin + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin].
phytochromobilin:ferredoxin oxidoreductase
Catalyzes the two-electron reduction of biliverdin IXalpha.
Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum.
The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm.
Flavodoxins can be used instead of ferredoxin.
(3Z)-phytochromobilin + 2 oxidized [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
phycocyanobilin:ferredoxin oxidoreductase
Catalyzes the four-electron reduction of biliverdin IXalpha (2-electron reduction at both the A and D rings).
Reaction proceeds via an isolatable 2-electron intermediate, 18(1),18(2)-dihydrobiliverdin.
The direct conversion of biliverdin IXalpha (BV) to (3Z)-phycocyanobilin (PCB) in the cyanobacteria Synechocystis sp. PCC 6803, Anabaena sp. PCC7120 and Nostoc punctiforme is in contrast to the proposed pathways of PCB biosynthesis in the red alga Cyanidium caldarium, which involves (3Z)-phycoerythrobilin (PEB) as an intermediate and in the green alga Mesotaenium caldariorum, in which PCB is an isolable intermediate.
(2R,3Z)-phycocyanobilin + 4 oxidized [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + 4 H(+) + 4 reduced [2Fe-2S]-[ferredoxin].
This enzyme, from a cyanophage infecting oceanic cyanobacteria of the Prochlorococcus genus, uses a four-electron reduction to carry out the reactions catalyzed by EC 1.3.7.2 and EC 1.3.7.3.
15,16-Dihydrobiliverdin is formed as a bound intermediate.
Free 15,16-dihydrobiliverdin can also act as a substrate to form phycoerythrobilin.
(3Z)-phycoerythrobilin + 2 oxidized 2[4Fe-4S]-[ferredoxin] = biliverdin IXalpha + 4 H(+) + 2 reduced 2[4Fe-4S]-[ferredoxin].
ferredoxin:protochlorophyllide reductase (ATP-dependent)
light-independent protochlorophyllide reductase
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms.
The enzyme catalyzes trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
Unlike EC 1.3.1.33 light is not required.
The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of EC 1.18.6.1, which catalyzes an ATP-driven reduction.
2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin].
Inactive toward aromatic acids that are not CoA esters but will also catalyze the reaction: NH3 + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O.
In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyzes the hydrolysis of ATP to ADP plus phosphate.
2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 H2O + reduced 2[4Fe-4S]-[ferredoxin].
A + 2 ADP + H(+) + NH4(+) + 2 phosphate = AH2 + 2 ATP + H2O + hydroxylamine.
2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (donor)
The enzyme is involved in the biosynthesis of archaeal membrane lipids.
It catalyzes the reduction of all 8 double bonds in 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipids and all 4 double bonds in 3-O-geranylgeranyl-sn-glycerol phospholipids with comparable activity.
Unlike EC 1.3.1.101, this enzyme shows no activity with NADPH, and requires a dedicated ferredoxin.
a 2,3-bis-O-phytanyl-sn-glycerol 1-phospholipid + 8 oxidized 2[4Fe-4S]-[ferredoxin] = a 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phospholipid + 16 H(+) + 8 reduced 2[4Fe-4S]-[ferredoxin].
2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 oxidized 2[4Fe-4S]-[ferredoxin] = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + 16 H(+) + 8 reduced 2[4Fe-4S]-[ferredoxin].
The enzyme participates in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants.
The reaction requires reduced ferredoxin, which is generated from NADPH produced either through the pentose-phosphate pathway or by the action of photosystem I.
This reaction takes place while red chlorophyll catabolite is still bound to EC 1.14.15.17.
Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer.
After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colorless breakdown products called non-fluorescent chlorophyll catabolites (NCCs).
2 oxidized [2Fe-2S]-[ferredoxin] + primary fluorescent chlorophyll catabolite = 3 H(+) + red chlorophyll catabolite + 2 reduced [2Fe-2S]-[ferredoxin].
3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin)
cyano-type divinyl chlorophyllide a 8-vinyl-reductase
The enzyme, found in many phototrophic bacteria, land plants, and some green and red algae, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors.
It can also act on 3,8-divinyl chlorophyllide a, 3,8-divinyl chlorophyll a, and chlorophyll c2.
2 oxidized [2Fe-2S]-[ferredoxin] + protochlorophyllide a = 3,8-divinyl protochlorophyllide a + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
chlorophyllide a + 2 oxidized [2Fe-2S]-[ferredoxin] = 3,8-divinyl chlorophyllide a + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
The enzyme, found only in bacteriochlorophyll b-producing bacteria, catalyzes the introduction of a C-8 ethylidene group.
The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase.
It is very similar to EC 1.3.7.15 and is composed of three subunits.
Two of them form the catalytic component, while the third one functions as an ATP-dependent reductase component that catalyzes the electron transfer from ferredoxin to the catalytic component.
ADP + bacteriochlorophyllide g + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3,8-divinyl chlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin].
The enzyme, together with EC 1.1.1.396 and EC 4.2.1.165, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a.
These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a.
This enzyme catalyzes a trans-reduction of the B-ring; the product has the (7R,8R)-configuration.
In addition, the enzyme has a latent activity of EC 1.3.7.13.
3-deacetyl-3-vinylbacteriochlorophyllide a + ADP + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = ATP + chlorophyllide a + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin].
ADP + bacteriochlorophyllide a + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3-acetyl-3-devinylchlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin].
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + ADP + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin].
One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R hydrogen atoms.
The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms.
The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA.
The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA.
a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
butanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein].
4,4'-diapophytoene desaturase (4,4'-diapolycopene-forming)
The enzyme catalyzes four successive dehydrogenations, resulting in production of 4,4'-diapolycopene.
While the enzyme from Staphylococcus aureus was only shown to produce 4,4'-diaponeurosporene in vivo, it is able to catalyze the last reaction in vitro.
15-cis-4,4'-diapophytoene + 4 FAD + 4 H(+) = all-trans-4,4'-diapolycopene + 4 FADH2.
15-cis-4,4'-diapophytoene + 3 FAD + 3 H(+) = all-trans-4,4'-diaponeurosporene + 3 FADH2.
Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate- and enantiomer specificity it is highly specific for (R)-benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA.
Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica.
Ferricenium ion is an effective artificial electron acceptor.
(R)-2-benzylsuccinyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (E)-2-benzylidenesuccinyl-CoA + reduced [electron-transfer flavoprotein].
3-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein].
short-chain 2-methylacyl-CoA dehydrogenase
2-methyl branched chain acyl-CoA dehydrogenase
2-methyl-branched-chain-enoyl-CoA reductase
The mammalian enzyme catalyzes an oxidative reaction as a step in the mitochondrial beta-oxidation of short-chain 2-methyl fatty acids and participates in isoleucine degradation.
The enzyme from the parasitic helminth Ascaris suum catalyzes a reductive reaction as part of a fermentation pathway, shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA.
2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein].
2-methylpropanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein].
The enzyme catalyzes the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5).
FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle.
The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyzes the oxidation to glutaconyl-CoA (EC 1.3.99.32).
glutaryl-CoA + 2 H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer flavoprotein].
The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds.
The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds.
a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms.
The highest activity was found with C12, and the rates with C8 and C16 were 80% and 70%, respectively.
The enzyme from rat can accept substrates with C8-C22.
It is most active with C14 and C16, and has no activity with C4, C6 or C24.
a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons.
It shows no activity for substrates of less than 12 carbons.
It's specific activity toward palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase.
a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
cyclohex-1-ene-1-carbonyl-CoA dehydrogenase
The enzyme, characterized from the strict anaerobic bacterium Syntrophus aciditrophicus, is involved in production of cyclohexane-1-carboxylate, a by-product produced by that organism during fermentation of benzoate and crotonate to acetate.
cyclohex-1-ene-1-carbonyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = cyclohexa-1,5-diene-1-carbonyl-CoA + reduced [electron-transfer flavoprotein].
cyclohexane-1-carbonyl-CoA dehydrogenase (electron-transfer flavoprotein)
cyclohexane-1-carbonyl-CoA dehydrogenase
cyclohexane-1-carbonyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = cyclohex-1-ene-1-carbonyl-CoA + reduced [electron-transfer flavoprotein].
The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation.
(2S)-methylsuccinyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = 2-methylfumaryl-CoA + reduced [electron-transfer flavoprotein].
The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21.
The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes.
gamma-butyrobetainyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = crotonobetainyl-CoA + reduced [electron-transfer flavoprotein].
L-prolyl-[peptidyl-carrier protein] dehydrogenase
The enzyme participates in the biosynthesis of several pyrrole-containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1.
It is believed to catalyze the formation of a Delta(2)-pyrrolin-2-yl(carbonyl)-S-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].
H(+) + L-prolyl-[peptidyl-carrier protein] + 2 oxidized [electron-transfer flavoprotein] = (1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 2 reduced [electron-transfer flavoprotein].
The enzyme, found in some amino acid-fermenting anaerobic bacteria, participates in the fermentation pathways of L-phenylalanine, L-tyrosine, and L-tryptophan.
Unlike EC 1.3.1.31, this enzyme has minimal activity with crotonate.
H(+) + oxidized [electron-transfer flavoprotein] + phloretate = (E)-4-coumarate + reduced [electron-transfer flavoprotein].
3-phenylpropanoate + H(+) + oxidized [electron-transfer flavoprotein] = (E)-cinnamate + reduced [electron-transfer flavoprotein].
3-(1H-indol-3-yl)propanoate + H(+) + oxidized [electron-transfer flavoprotein] = (E)-3-(indol-3-yl)acrylate + reduced [electron-transfer flavoprotein].
2-amino-2-deoxyisochorismate dehydrogenase
The sequential action of EC 2.6.1.86 and this enzyme leads to the formation of the benzoxazolinate moiety of the enediyne antitumor antibiotic C-1027.
(2S)-2-amino-4-deoxychorismate + FMN = 3-(1-carboxyvinyloxy)anthranilate + FMNH2.
This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria.
In some eubacteria the enzyme is multifunctional, also catalyzing the activities of EC 6.3.2.31, and EC 6.3.2.34.
FMN + H(+) + oxidized coenzyme F420-0 = dehydro coenzyme F420-0 + FMNH2.
The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides.
Molecular oxygen can replace fumarate in vitro.
Other class 1 dihydroorotate dehydrogenases use either NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor.
(S)-dihydroorotate + fumarate = orotate + succinate.
oxygen-independent coproporphyrinogen-III oxidase
Differs from EC 1.3.3.3 by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant.
Occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase.
The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl; this radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups.
This conversion, -.CH-CH2-COO- -> -CH=CH2 + CO2 + e(-) replaces the electron initially used.
coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX.
The enzyme, characterized from the bacteria Streptomyces aureofaciens and Streptomyces rimosus, catalyzes the last step in the biosynthesis of the tetracycline antibiotics tetracycline and oxytetracycline.
H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) + tetracycline = 5a,11a-dehydrotetracycline + reduced coenzyme F420-(gamma-L-Glu)(n).
H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) + oxytetracycline = 5a,11a-dehydrooxytetracycline + reduced coenzyme F420-(gamma-L-Glu)(n).
hydrogen peroxide-dependent heme synthase
The enzyme participates in a heme biosynthesis pathway found in Gram-positive bacteria.
The initial decarboxylation step is fast and yields the three-propanoate harderoheme isomer III.
The second decarboxylation is much slower, cf. EC 1.3.98.6.
Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b.
This radical AdoMet enzyme participates in a heme biosynthesis pathway found in archaea and sulfur-reducing bacteria, cf. EC 1.3.98.5.
Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + heme b + 2 L-methionine.
[mycofactocin precursor peptide]-tyrosine decarboxylase
This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyzes the first two steps in the biosynthesis of the enzyme cofactor mycofactocin.
Activity requires the presence of the MftB chaperone.
The other activity of the enzyme is EC 4.1.99.26.
[mycofactocin precursor peptide]-C-terminal glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine = 5'-deoxyadenosine + [mycofactocin precursor peptide]-C-terminal glycyl-N-{[2-(4-hydroxyphenyl)ethenyl]-3-methylbutanamide} + CO2 + L-methionine.
A + a 3-oxosteroid = a 3-oxo-Delta(1)-steroid + AH2.
5alpha-androstan-3,17-dione + A = 5alpha-androst-1-ene-3,17-dione + AH2.
A + androst-4-ene-3,17-dione = AH2 + androsta-1,4-diene-3,17-dione.
3-oxo-5alpha-steroid 4-dehydrogenase (acceptor)
This bacterial enzyme, characterized from Comamonas testosteroni, is involved in androsterone degradation.
A + a 3-oxo-5alpha-steroid = a 3-oxo-Delta(4)-steroid + AH2.
5alpha-androstan-3,17-dione + A = AH2 + androst-4-ene-3,17-dione.
5alpha-androst-1-ene-3,17-dione + A = AH2 + androsta-1,4-diene-3,17-dione.
A + a 3-oxo-5beta-steroid = a 3-oxo-Delta(4)-steroid + AH2.
The oxygen atom of the -OH produced is derived from water, not O2.
The actual oxidative step is probably dehydrogenation of a hydrated form -CHOH-CH2- to -C(OH)=CH-, which tautomerizes non-enzymically to -CO-CH2-, giving (5-oxo-4,5-dihydro-2-furoyl)-CoA.
Methylene blue, nitro blue tetrazolium and a membrane fraction from Pseudomonas putida can act as acceptors.
2-furoyl-CoA + A + H2O = 5-hydroxy-2-furoyl-CoA + AH2 + H(+).
The corresponding ketones of cyclopentane and cycloheptane cannot act as donors.
A + cyclohexanone = AH2 + cyclohex-2-enone.
The enzyme from Pseudomonas diminuta is specific toward N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline.
Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonitrotetrazolium chloride (INT), nitroblue tetrazolium (NBT), Meldola blue and phenazine methosulfate.
A + H2O + isoquinoline = AH2 + isoquinolin-1(2H)-one.
In addition to quinoline, quinolin-2-ol, quinolin-7-ol, quinolin-8-ol, 3-, 4- and 8-methylquinolines and 8-chloroquinoline are substrates.
Iodonitrotetrazolium chloride (INT) can act as an electron acceptor.
A + H2O + quinoline = AH2 + quinolin-2(1H)-one.
8-chloroquinoline + A + H2O = 8-chloroquinolin-2(1H)-one + AH2.
8-methylquinoline + A + H2O = 8-methylquinolin-2(1H)-one + AH2.
4-methylquinoline + A + H2O = 4-methylquinolin-2(1H)-one + AH2.
3-methylquinoline + A + H2O = 3-methylquinolin-2(1H)-one + AH2.
A + H2O + quinolin-8-ol = 8-hydroxyquinolin-2(1H)-one + AH2.
A + H2O + quinolin-7-ol = 7-hydroxyquinolin-2(1H)-one + AH2.
A + H2O + quinolin-6-ol = 6-hydroxyquinolin-2(1H)-one + AH2.
A + H2O + quinolin-5-ol = 5-hydroxyquinolin-2(1H)-one + AH2.
The enzyme from Pseudomonas sp. AK2 also acts on quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize nicotinate; quinaldate is a substrate for both of these enzymes.
2,4,6-Trinitrobenzene sulfonate acid, 1,4-benzoquinone, 1,2-naphthoquinone, nitroblue tetrazolium (NBT), thionine and menadione will serve as an electron acceptor for the former enzyme and ferricyanide for the latter; Meldola blue, iodonitrotetrazolium chloride (INT), phenazine methosulfate (PMS), 2,6-dichlorophenolindophenol (DCPIP) and cytochrome c will act as electron acceptors for both.
A + H2O + quinaldate = AH2 + kynurenate.
quinoline-4-carboxylate 2-oxidoreductase
quinoline-4-carboxylic acid 2-oxidoreductase
Quinoline, 4-methylquinoline and 4-chloroquinoline can also serve as substrates for the enzyme from Agrobacterium sp. 1B.
Iodonitrotetrazolium chloride, thionine, menadione and 2,6-dichlorophenolindophenol can act as electron acceptors.
A + H2O + quinoline-4-carboxylate = 2-oxo-1,2-dihydroquinoline-4-carboxylate + AH2.
The reaction is only known to occur in the opposite direction to that given above, with the enzyme being specific for all-trans-retinol as substrate.
Neither all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers are substrates.
May play a role in the metabolism of vitamin A.
A + all-trans-13,14-dihydroretinol = AH2 + all-trans-retinol.
Participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14.
Has not been purified, and requires an unknown cofactor, which is different from NAD(+), NADP(+) or a flavin.
(1R,4R)-dihydrocarvone + A = (R)-carvone + AH2.
(1R,4S)-isodihydrocarvone + A = (S)-carvone + AH2.
This enzyme is involved in carotenoid biosynthesis.
2 A + all-trans-zeta-carotene = 2 AH2 + all-trans-lycopene.
The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides prefer the acyclic carotenoids (e.g. 1-hydroxy-1,2-dihydroneurosporene, 1-hydroxy-1,2-dihydrolycopene) as substrates.
The conversion rate for the 3,4-desaturation of the monocyclic 1'-hydroxy-1',2'-dihydro-gamma-carotene is lower.
The enzyme from the marine bacterium strain P99-3 shows high activity with the monocyclic carotenoid 1'-hydroxy-1',2'-dihydro-gamma-carotene.
The enzyme from Rhodobacter sphaeroides utilizes molecular oxygen as the electron acceptor in vitro.
However, oxygen is unlikely to be the natural electron acceptor under anaerobic conditions.
A + rhodopin = (3E)-3,4-didehydrorhodopin + AH2.
phytoene desaturase (neurosporene-forming)
This enzyme is involved in carotenoid biosynthesis and catalyzes up to three desaturation steps (cf. EC 1.3.99.29, EC 1.3.99.30, EC 1.3.99.31).
NAD(+), NADP(+) or ATP show no activating effect.
15-cis-phytoene + 3 A = 3 AH2 + all-trans-neurosporene.
phytoene desaturase (zeta-carotene-forming)
The enzyme is involved in carotenoid biosynthesis and catalyzes up to two desaturation steps (cf. EC 1.3.99.28, EC 1.3.99.30 and EC 1.3.99.31).
15-cis-phytoene + 2 A = 2 AH2 + all-trans-zeta-carotene.
phytoene desaturase (3,4-didehydrolycopene-forming)
This enzyme is involved in carotenoid biosynthesis and catalyzes up to five desaturation steps (cf. EC 1.3.99.28, EC 1.3.99.29 and EC 1.3.99.31).
15-cis-phytoene + 5 A = 5 AH2 + all-trans-3,4-didehydrolycopene.
The enzyme is involved in carotenoid biosynthesis and catalyzes up to four desaturation steps (cf. EC 1.3.99.28, EC 1.3.99.29 and EC 1.3.99.30).
15-cis-phytoene + 4 A = 4 AH2 + all-trans-lycopene.
The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry).
The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
A + glutaryl-CoA = (2E)-glutaconyl-CoA + AH2.
The enzyme functions as part of an anaerobic electron transfer chain that utilizes urocanate as the terminal electron acceptor.
The activity has been demonstrated with the artificial donor reduced methyl viologen.
cypemycin cysteine dehydrogenase (decarboxylating)
Cypemycin, isolated from the bacterium Streptomyces sp. OH-4156, is a peptide antibiotic, member of the linaridins, a class of post-translationally modified ribosomally synthesized peptides.
The enzyme decarboxylates and reduces the C-terminal L-cysteine residue, producing a reactive ethenethiol group that reacts with a dethiolated cysteine upstream to form an aminovinyl-methyl-cysteine loop that is important for the antibiotic activity of the mature peptide.
[cypemycin](1-18)-L-Cys-L-Leu-L-Val-L-Cys + A = AH2 + C(3,19),S(21)-[cypemycin](1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + hydrogen sulfide.
1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase
The enzyme, isolated from the archaeon Haloarcula japonica, is involved in the biosynthesis of the C50 carotenoid bacterioruberin.
In this pathway it catalyzes the desaturation of the C-3,4 double bond in dihydroisopentenyldehydrorhodopin and the desaturation of the C-3'-4' double bond in dihydrobisanhydrobacterioruberin.
A + dihydroisopentenyldehydrorhodopin = AH2 + isopentenyldehydrorhodopin.
A + dihydrobisanhydrobacterioruberin = AH2 + bisanhydrobacterioruberin.
The enzyme from the bacterium Mycobacterium tuberculosis reduces the beta-isoprene unit of menaquinone-9, forming the predominant form of menaquinone found in mycobacteria.
AH2 + menaquinone-9 = A + beta-dihydromenaquinone-9.
The enzyme, found in green sulfur bacteria, some cyanobacteria and some actinobacteria, introduces additional double bonds to the carotenoid beta-end group, leading to aromatization of the ionone ring.
As a result, one of the methyl groups at C-1 is transferred to position C-2.
It is involved in the biosynthesis of carotenoids with phi-type aromatic end groups such as chlorobactene, beta-isorenieratene, and isorenieratene.
2 A + a carotenoid beta-end derivative = a carotenoid phi-end derivative + 2 AH2.
The enzyme, found in purple sulfur bacteria (Chromatiaceae) and some cyanobacteria, is involved in the biosynthesis of carotenoids that contain chi-type end groups, such as okenone, renierapurpurin, and synechoxanthin.
2 A + a carotenoid beta-end derivative = a carotenoid chi-end derivative + 2 AH2.
3-hydroxybenzoyl-CoA reductase (dearomatising)
Reduced methyl viologen can act as electron donor.
The enzyme also catalyzes the reaction of EC 1.3.7.8.
The reaction is catalyzed by a heterotetramer.
3-hydroxybenzoyl-CoA + AH2 + 2 ATP + 2 H2O = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + A + 2 ADP + 2 H(+) + 2 phosphate.
H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate.
H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+).
H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+).
an L-alpha-amino acid + H2O + NAD(+) = a 2-oxocarboxylate + H(+) + NADH + NH4(+).
L-serine:NAD oxidoreductase (deaminating)
H2O + L-serine + NAD(+) = 3-hydroxypyruvate + H(+) + NADH + NH4(+).
H2O + L-valine + NADP(+) = 3-methyl-2-oxobutanoate + H(+) + NADPH + NH4(+).
Also acts on isoleucine, valine, norvaline and norleucine.
H2O + L-leucine + NAD(+) = 4-methyl-2-oxopentanoate + H(+) + NADH + NH4(+).
glycine + H2O + NAD(+) = glyoxylate + H(+) + NADH + NH4(+).
L-erythro-3,5-diaminohexanoate dehydrogenase
(3S,5S)-3,5-diaminohexanoate + H2O + NAD(+) = (5S)-5-amino-3-oxohexanoate + H(+) + NADH + NH4(+).
Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5-oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate.
It has equal activity with NAD(+) and NADP(+) (cf. EC 1.4.1.26).
(2R,4S)-2,4-diaminopentanoate + H2O + NADP(+) = (2R)-2-amino-4-oxopentanoate + H(+) + NADPH + NH4(+).
(2R,4S)-2,4-diaminopentanoate + H2O + NAD(+) = (2R)-2-amino-4-oxopentanoate + H(+) + NADH + NH4(+).
glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase
glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP)
The reaction takes place in the opposite direction.
The protein is composed of two subunits, alpha and beta.
The alpha subunit is composed of two domains, one hydrolyzing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4).
The beta subunit transfers electrons from the cosubstrate.
The NH3 is channeled through a 31 A channel in the active protein.
In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced.
In the intact alphabeta complex, ammonia production only takes place as part of the overall reaction.
2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine + NADPH.
The reaction takes place in the direction of L-glutamate production.
The protein is composed of two domains, one hydrolyzing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.2).
2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine + NADH.
L-lysine + NAD(+) = Delta(1)-piperideine-2-carboxylate + H(+) + NADH + NH4(+).
H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6-oxoheptanedioate + H(+) + NADPH + NH4(+).
H2O + N-methyl-L-alanine + NADP(+) = H(+) + methylamine + NADPH + pyruvate.
Highly specific for L-lysine as substrate, although (S)-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly.
While the enzyme from Agrobacterium tumefaciens can use only NAD(+), that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP(+), but more slowly.
L-lysine + NAD(+) = 2 H(+) + L-1-piperideine-6-carboxylate + NADH + NH4(+).
L-lysine + NADP(+) = 2 H(+) + L-1-piperideine-6-carboxylate + NADPH + NH4(+).
NAD(+) + S-(2-aminoethyl)-L-cysteine = (4S)-5,6-dihydro-4H-1,3-thiazine-4-carboxylate + 2 H(+) + NADH + NH4(+).
H2O + L-tryptophan + NAD(+) = H(+) + indole-3-pyruvate + NADH + NH4(+).
H2O + L-tryptophan + NADP(+) = H(+) + indole-3-pyruvate + NADPH + NH4(+).
The enzymes from Bacillus badius and Sporosarcina ureae are highly specific for L-phenylalanine; that from Bacillus sphaericus also acts on L-tyrosine.
H2O + L-phenylalanine + NAD(+) = 3-phenylpyruvate + H(+) + NADH + NH4(+).
NADP(+)-dependent aspartate dehydrogenase
The enzyme is strictly specific for L-aspartate as substrate.
It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyzes spontaneously to form oxaloacetate.
The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC 2.5.1.72 preventing its hydrolysis and enabling the de novo biosynthesis of NAD(+).
H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate.
H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate.
The enzyme from Streptomyces spp. has no activity with NADP(+) (cf. EC 1.4.1.8).
H2O + L-valine + NAD(+) = 3-methyl-2-oxobutanoate + H(+) + NADH + NH4(+).
The enzyme, which was isolated from the archaeon Methanocaldococcus jannaschii, plays a key role in an alternative pathway for the biosynthesis of 3-dehydroquinate (DHQ), an intermediate of the canonical pathway for the biosynthesis of aromatic amino acids.
The enzyme catalyzes a two-step reaction - an oxidative deamination, followed by cyclization.
2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+) = 3-dehydroquinate + H(+) + NADH + NH4(+).
The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.99.6 a two-enzyme complex involved in the racemization of D- and L-arginine.
H2O + L-arginine + NAD(+) = 5-guanidino-2-oxopentanoate + H(+) + NADH + NH4(+).
H2O + L-arginine + NADP(+) = 5-guanidino-2-oxopentanoate + H(+) + NADPH + NH4(+).
2,4-diaminopentanoate dehydrogenase (NAD(+))
The enzyme, characterized from an unknown bacterium in an environmental sample, has some activity with (2R,4R)-2,4-diaminopentanoate.
It has very low activity with NADP(+) (cf. EC 1.4.1.12).
The glycine cleavage (GCV) system is a large multienzyme complex that belongs to the 2-oxoacid dehydrogenase complex family, which also includes EC 1.2.1.25, EC 1.2.1.105, EC 1.2.1.104 and EC 2.3.1.190.
The GCV system catalyzes the reversible oxidation of glycine, yielding carbon dioxide, ammonia, 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide.
Tetrahydrofolate serves as a recipient for one-carbon units generated during glycine cleavage to form the methylene group.
The GCV system consists of four protein components, the P protein (EC 1.4.4.2), T protein (EC 2.1.2.10), L protein (EC 1.8.1.4), and the non-enzyme H protein (lipoyl-carrier protein).
The P protein catalyzes the pyridoxal phosphate-dependent liberation of CO2 from glycine, leaving a methylamine moiety.
The methylamine moiety is transferred to the lipoic acid group of the H protein, which is bound to the P protein prior to decarboxylation of glycine.
The T protein catalyzes the release of ammonia from the methylamine group and transfers the remaining C1 unit to tetrahydrofolate, forming 5,10-methylenetetrahydrofolate.
The L protein then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD(+), forming NADH.
(6S)-5,6,7,8-tetrahydrofolate + glycine + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + CO2 + NADH + NH4(+).
2 Fe(III)-[cytochrome c] + glycine + H2O = 2 Fe(II)-[cytochrome c] + glyoxylate + 2 H(+) + NH4(+).
D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate.
an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+).
a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+).
D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+).
Catalyzes the oxidative deamination of neurotransmitters and biogenic amines.
Acts on primary amines, and also on some secondary and tertiary amines.
It differs from EC 1.4.3.21, as it can oxidize secondary and tertiary amines but not methylamine.
Inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22, it is not inhibited by semicarbazide.
a secondary aliphatic amine + H2O + O2 = a primary amine + an aldehyde + H2O2.
pyridoxine (pyridoxamine) 5'-phosphate oxidase
pyridoxine (pyridoxamine)phosphate oxidase
In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5.
H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate.
O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate.
D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+).
ethanolamine + H2O + O2 = glycolaldehyde + H2O2 + NH4(+).
4-aminobutanal condenses non-enzymically to 1-pyrroline.
H2O + O2 + putrescine = 4-aminobutanal + H2O2 + NH4(+).
The enzyme from Azotobacter previously listed under this number, which did not produce H2O2, was a crude cell-free extract which probably contained catalase.
H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+).
Some other cyclic amines can act instead of cyclohexylamine, but not simple aliphatic and aromatic amides.
cyclohexylamine + H2O + O2 = cyclohexanone + H2O2 + NH4(+).
Catalyzes the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices.
These reactions play an important role for the development, elasticity and extensibility of connective tissue.
Also active on free amines, such as cadaverine or benzylamine.
H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+).
Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine.
H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+).
D-glutamate and D-aspartate are oxidized at the same rate.
Other D-monoaminodicarboxylates, and other D- and L-amino acids, are not oxidized.
L-Aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria.
O2 can be replaced by fumarate as electron acceptor, yielding succinate.
The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions.
Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH3 or can be used by EC 2.5.1.72 in the production of quinolinate.
L-aspartate + O2 = H2O2 + iminosuccinate.
The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-alpha-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine.
It differs from EC 1.4.3.3 due to its activity on sarcosine and D-pipecolate.
The intermediate 2-iminoacetate is used directly by EC 2.8.1.10.
glycine + H2O + O2 = glyoxylate + H2O2 + NH4(+).
D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate.
H2O + O2 + sarcosine = glyoxylate + H2O2 + methylamine.
H2O + N-ethylglycine + O2 = ethylamine + glyoxylate + H2O2.
Differs from EC 1.4.3.13 by using free L-lysine rather than the protein-bound form.
N(2)-acetyl-L-lysine is also a substrate, but N(6)-acetyl-L-lysine, which has an acetyl group at position 6, is not.
Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly.
The amines cadaverine and putrescine are not substrates.
H2O + L-lysine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + NH4(+).
A group of enzymes that oxidize primary monoamines but have little or no activity toward diamines, such as histamine, or toward secondary and tertiary amines.
They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+).
2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4(+).
3-nitrotyramine + H2O + O2 = 4-hydroxy-3-nitrophenylacetaldehyde + H2O2 + NH4(+).
A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity toward secondary and tertiary amines.
They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 but unlike EC 1.4.3.4, they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
H2O + histamine + O2 = H2O2 + imidazole-4-acetaldehyde + NH4(+).
This enzyme catalyzes a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes.
During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide.
The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan.
7-chloro-L-tryptophan + O2 = 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2.
L-tryptophan + O2 = 2-iminio-3-(indol-3-yl)propanoate + H2O2.
This enzyme, characterized from the soil bacterium Pseudomonas sp. HZN6, is involved the nicotine degradation.
H2O + O2 + pseudooxynicotine = 4-oxo-4-(pyridin-3-yl)butanal + H2O2 + methylamine.
The enzyme from cyanobacteria can also act on other basic amino acids with lower activity.
The enzyme from the bacterium Pseudomonas sp. TPU 7192 is highly specific.
H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+).
The enzyme participates in the biosynthesis of the enzyme cofactor mycofactocin.
The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an alpha-keto moiety on the resulting molecule.
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one + H2O + O2 = H2O2 + NH4(+) + pre-mycofactocin.
glycine dehydrogenase (aminomethyl-transferring)
A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein.
(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2.
The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine.
This enzyme may be the same as EC 1.4.99.6.
a D-alpha-amino acid + a quinone + H2O = a 2-oxocarboxylate + a quinol + NH4(+).
The protein is composed of two domains, one hydrolyzing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate.
The NH3 is channeled through a 24 A channel in the active protein.
No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein.
2 L-glutamate + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-oxoglutarate + 2 H(+) + L-glutamine + 2 reduced [2Fe-2S]-[ferredoxin].
The enzyme oxidizes aliphatic monoamines and diamines, histamine and ethanolamine, but not secondary and tertiary amines, quaternary ammonium salts or aromatic amines.
H2O + methylamine + 2 oxidized [amicyanin] = formaldehyde + 2 H(+) + NH4(+) + 2 reduced [amicyanin].
Phenazine methosulfate can act as acceptor.
Acts on aromatic amines and, more slowly, on some long-chain aliphatic amines, but not on methylamine or ethylamine.
an aralkylamine + H2O + 2 oxidized [azurin] = an aromatic aldehyde + 2 H(+) + NH4(+) + 2 reduced [azurin].
A + H2O + taurine = AH2 + NH4(+) + sulfoacetaldehyde.
The enzyme is membrane-bound, and the 2-electron acceptor is a component of the respiratory chain.
The enzyme can act with various artificial electron acceptors, including phenazine methosulfate.
2 A + glycine = 2 AH2 + CO2 + hydrogen cyanide.
The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25 a two-enzyme complex involved in the racemization of D- and L-arginine.
The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate.
However, activity is maximal with D-arginine and D-lysine.
A + D-arginine + H2O = 5-guanidino-2-oxopentanoate + AH2 + NH4(+).
1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]
The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism.
In contrast to EC 1.5.1.21, which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH.
L-pipecolate + NADP(+) = Delta(1)-piperideine-2-carboxylate + H(+) + NADPH.
L-pipecolate + NAD(+) = Delta(1)-piperideine-2-carboxylate + H(+) + NADH.
L-proline + NADP(+) = 1-pyrroline-2-carboxylate + H(+) + NADPH.
L-proline + NAD(+) = 1-pyrroline-2-carboxylate + H(+) + NADH.
Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH.
L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH.
The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH.
methylenetetrahydrofolate dehydrogenase (NADP(+))
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH.
(6S)-10-formyltetrahydrofolate + H2O + NADP(+) = (6S)-5,6,7,8-tetrahydrofolate + CO2 + H(+) + NADPH.
saccharopine dehydrogenase (NAD(+), L-lysine-forming)
H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH.
saccharopine dehydrogenase (NADP(+), L-lysine-forming)
H2O + L-saccharopine + NADP(+) = 2-oxoglutarate + H(+) + L-lysine + NADPH.
saccharopine dehydrogenase (NAD(+), L-glutamate-forming)
H2O + L-saccharopine + NAD(+) = (S)-2-amino-6-oxohexanoate + H(+) + L-glutamate + NADH.
saccharopine dehydrogenase (NADP(+), L-glutamate-forming)
aminoadipate semialdehyde-glutamate reductase
aminoadipic semialdehyde-glutamate reductase
aminoadipic semialdehyde-glutamic reductase
H2O + L-saccharopine + NADP(+) = (S)-2-amino-6-oxohexanoate + H(+) + L-glutamate + NADPH.
Also acts, in the reverse direction, on L-ornithine, L-lysine and L-histidine.
D-octopine + H2O + NAD(+) = H(+) + L-arginine + NADH + pyruvate.
methylenetetrahydrofolate dehydrogenase (NAD(+))
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH.
In the reverse reaction, a number of L-amino acids can act instead of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate can act instead of pyruvate.
D-lysopine + H2O + NADP(+) = H(+) + L-lysine + NADPH + pyruvate.
In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine, or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22).
2,2'-iminodipropanoate + H2O + NAD(+) = H(+) + L-alanine + NADH + pyruvate.
The product immediately hydrolyzes to methylamine and 1-hydroxy-1-phenylpropan-2-one.
Acts on a number of related compounds including (-)-sympatol, (+)-pseudoephedrine and (+)-norephedrine.
(1R,2S)-ephedrine + NAD(+) = (R)-2-methylimino-1-phenylpropan-1-ol + 2 H(+) + NADH.
In the reverse direction, forms D-nopaline from L-arginine and D-ornaline from L-ornithine.
D-nopaline + H2O + NADP(+) = 2-oxoglutarate + H(+) + L-arginine + NADPH.
methylenetetrahydrofolate reductase [NAD(P)H]
The enzyme catalyzes the reversible conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, playing an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis.
This enzyme, characterized from Protozoan parasites of the genus Leishmania, is unique among similar characterized eukaryotic enzymes in that it lacks the C-terminal allosteric regulatory domain (allowing it to catalyze a reversible reaction) and uses NADH and NADPH with equal efficiency under physiological conditions.
(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH.
(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH.
1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)
Delta(1)-piperideine-2-carboxylate reductase
The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus.
In contrast to EC 1.5.1.1, which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.
Catalyzes the reaction of EC 1.5.1.17, more slowly.
H2O + N-(carboxymethyl)-D-alanine + NAD(+) = glycine + H(+) + NADH + pyruvate.
In the reverse reaction, alanine can act instead of taurine, more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate.
H2O + NAD(+) + tauropine = H(+) + NADH + pyruvate + taurine.
In the reverse direction L-lysine can act instead of L-ornithine, more slowly.
Acts on the amino group (cf. EC 1.5.1.16).
H2O + N(5)-[1(S)-1-carboxyethyl]-L-ornithine + NADP(+) = H(+) + L-ornithine + NADPH + pyruvate.
thiomorpholine-carboxylate dehydrogenase
The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine.
In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, more slowly.
(3R)-1,4-thiomorpholine-3-carboxylate + NADP(+) = 3,4-dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADPH.
(3R)-1,4-thiomorpholine-3-carboxylate + NAD(+) = 3,4-dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADH.
(R)-beta-alanopine + H2O + NAD(+) = beta-alanine + H(+) + NADH + pyruvate.
1,2-dehydroreticulinium reductase (NADPH)
Reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is a direct precursor of morphinan alkaloids in the poppy plant.
The enzyme does not catalyze the reverse reaction to any significant extent under physiological conditions.
(R)-reticuline + NADP(+) = 1,2-dehydroreticuline + H(+) + NADPH.
in the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine.
Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate.
In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor.
They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine.
The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate.
(2S)-2-[(R)-1-carboxyethylamino]pentanoate + H2O + NAD(+) = H(+) + L-2-aminopentanoate + NADH + pyruvate.
riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase
The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD.
NADH is oxidized more slowly than NADPH.
NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin.
Involved in alkaloid biosynthesis in Corydalis cava to give (R)-canadine with the opposite configuration to the precursor of berberine (see EC 1.3.3.8).
(R)-canadine + 2 NADP(+) = berberine + H(+) + 2 NADPH.
1,2-dihydrovomilenine + NADP(+) = H(+) + NADPH + vomilenine.
The enzyme from Leishmania (both amastigote and promastigote forms) catalyzes the NADPH-dependent reduction of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms.
It also catalyzes the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms.
In contrast to EC 1.5.1.3 and EC 1.5.1.34, pteridine reductase will not catalyze the reduction of the quinonoid form of dihydrobiopterin.
The enzyme is specific for NADPH; no activity has been detected with NADH.
It also differs from EC 1.5.1.3 in being specific for the B side of NADPH.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 2 H(+) + L-erythro-biopterin + 2 NADPH.
6,7-dihydropteridine:NAD(P)H oxidoreductase
dihydropteridine (reduced nicotinamide adenine dinucleotide) reductase
NAD(P)H2:6,7-dihydropteridine oxidoreductase
NADPH-specific dihydropteridine reductase
The substrate is the quinonoid form of dihydropteridine.
5,6,7,8-tetrahydropteridine + NADP(+) = 6,7-dihydropteridine + H(+) + NADPH.
5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine + H(+) + NADH.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NADP(+) = (6R)-L-erythro-6,7-dihydrobiopterin + H(+) + NADPH.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD(+) = (6R)-L-erythro-6,7-dihydrobiopterin + H(+) + NADH.
The enzyme from Escherichia coli W catalyzes the reduction of free flavins by NADH.
The enzyme has similar affinity to FAD, FMN and riboflavin.
Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.
a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) + NADH.
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD.
Unlike EC 1.5.1.36, the enzyme can not reduce riboflavin.
The enzyme does not use NADPH as acceptor.
The enzymes from bioluminescent bacteria contain FMN, while the enzyme from Escherichia coli does not.
The enzyme often forms a two-component system with monooxygenases such as luciferase.
Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor.
While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity.
The enzyme can utilize NADH and NADPH with similar reaction rates.
Different from EC 1.5.1.42 and EC 1.5.1.38.
The luminescent bacterium Vibrio harveyi possesses all three enzymes, while the bacterium Aliivibrio fischeri contains only this non-specific type.
Also reduces riboflavin and FAD, but more slowly.
8-hydroxy-5-deazaflavin:NADPH oxidoreductase
The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate.
NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n).
Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides.
When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin.
When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD.
NAD(+) + reduced riboflavin = 2 H(+) + NADH + riboflavin.
The enzyme often forms a two-component system with monooxygenases.
Unlike EC 1.5.1.38 and EC 1.5.1.39, this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed.
While FMN is the preferred substrate, FAD can also be used with much lower activity.
Part of a bacterial polyamine biosynthesis pathway.
L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively.
The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation.
The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro.
carboxynorspermidine + H2O + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH + propane-1,3-diamine.
carboxyspermidine + H2O + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH + putrescine.
The reaction proceeds in vivo in the opposite direction to the one shown here.
festuclavine + NAD(+) = 6,8-dimethyl-6,7-didehydroergoline + H(+) + NADH.
This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation.
The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and EC 1.14.14.8.
It can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD.
The enzyme has a slight preference for NADPH as acceptor.
The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family.
The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione.
agroclavine + NADP(+) = didehydroagroclavine + H(+) + NADPH.
dihydromethanopterin reductase [NAD(P)(+)]
5,6,7,8-tetrahydromethanopterin 5,6-oxidoreductase
The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin.
The specific activity with NADH is 15% of that with NADPH at the same concentration.
It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3).
5,6,7,8-tetrahydromethanopterin + NADP(+) = 7,8-dihydromethanopterin + H(+) + NADPH.
5,6,7,8-tetrahydromethanopterin + NAD(+) = 7,8-dihydromethanopterin + H(+) + NADH.
The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.
(R)-2-methylpyrrolidine + NADP(+) = 2-methyl-1-pyrroline + H(+) + NADPH.
1-pyrroline-2-carboxylate reductase [NAD(P)H]
The enzyme from the bacterium Colwellia psychrerythraea is involved in trans-3-hydroxy-L-proline metabolism.
In contrast to EC 1.5.1.1 which shows similar activity with 1-piperideine-2-carboxylate and 1-pyrroline-2-carboxylate, this enzyme is specific for the latter.
While the enzyme is active with both NADH and NADPH, activity is higher with NADPH.
The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).
7,8-dihydromonapterin + H(+) + NADPH = 5,6,7,8-tetrahydromonapterin + NADP(+).
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
H2O + N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD(+) = (S)-2,3-diaminopropanoate + 2-oxoglutarate + H(+) + NADH.
The enzyme, characterized from the bacterium Staphylococcus aureus, catalyzes the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
H2O + NADP(+) + staphylopine = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + NADPH + pyruvate.
methylenetetrahydrofolate reductase (NADPH)
5,10-methylenetetrahydrofolate reductase (FADH2)
5,10-methylenetetrahydrofolate reductase (NADPH)
N(5),10-methylenetetrahydrofolate reductase
The enzyme from yeast and mammals catalyzes a physiologically irreversible reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using NADPH as the electron donor.
It plays an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis.
The enzyme contains an N-terminal catalytic domain and a C-terminal allosteric regulatory domain that binds S-adenosyl-L-methionine, which acts as an inhibitor. cf. EC 1.5.1.54, EC 1.5.1.20, and EC 1.5.7.1.
methylenetetrahydrofolate reductase (NADH)
5,10-methylenetetrahydrofolate reductase
The enzyme, found in plants and some bacteria, catalyzes the reversible conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using NADH as the electron donor.
It play an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis.
These proteins either contain a C-terminal domain that does not mediate allosteric regulation (as in plants) or lack this domain entirely (as in Escherichia coli).
As a result, the plant enzymes are not inhibited by S-adenosyl-L-methionine, unlike other eukaryotic enzymes, and catalyze a reversible reaction.
sarcosine oxidasee (formaldehyde-forming)
The enzyme, reported from bacteria and fungi, catalyzes the oxidative demethylation of sarcosine.
It contains a FAD cofactor bound to an L-cysteine residue. cf. EC 1.5.3.24.
H2O + O2 + sarcosine = formaldehyde + glycine + H2O2.
an N-methyl-L-amino acid + H2O + O2 = an L-alpha-amino acid + formaldehyde + H2O2.
H2O + N(6)-methyl-L-lysine + O2 = formaldehyde + H2O2 + L-lysine.
The enzyme, which participates in nicotine degradation, is specific for the (S) isomer of 6-hydroxynicotine.
The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyzes a similar reaction with the less common (R)-isomer (cf. EC 1.5.3.6).
(S)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2.
The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)-nicotine.
The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyzes a similar reaction with the (S)-isomer (cf. EC 1.5.3.5).
(R)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2.
The product reacts with water to form (S)-2-amino-6-oxohexanoate.
L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-carboxylate.
The enzyme, characterized from the bacterium Arthrobacter globiformis, contains two active sites connected by a large 'reaction chamber'.
An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde.
In the absence of folate the enzyme does form formaldehyde.
Does not oxidize sarcosine. cf. EC 1.5.8.4.
(6S)-5,6,7,8-tetrahydrofolate + N,N-dimethylglycine + O2 = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H2O2 + sarcosine.
H2O + N,N-dimethylglycine + O2 = formaldehyde + H2O2 + sarcosine.
Produces oxidized forms of the benzophenanthridine alkaloids.
dihydrosanguinarine + H(+) + O2 = H2O2 + sanguinarine.
dihydrochelirubine + H(+) + O2 = chelirubine + H2O2.
dihydromacarpine + H(+) + O2 = H2O2 + macarpine.
The enzyme also catalyzes the reaction: N(1),N(12)-diacetylspermine + O2 + H2O = N(1)-acetylspermidine + 3-acetamamidopropanal + H2O2.
No or very weak activity with spermine, or spermidine in absence of aldehydes.
In presence of aldehydes the enzyme catalyzes the reactions: 1.
spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2.
spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2.
Found in mammalian peroxisomes and oxidizes N(1)-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal.
Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion.
Differs in specificity from EC 1.5.3.14, EC 1.5.3.15, EC 1.5.3.16 and EC 1.5.3.17.
H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2 + putrescine.
H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 + spermidine.
H2O + N(1),N(12)-diacetylspermine + O2 = 3-acetamidopropanal + H2O2 + N(1)-acetylspermidine.
H2O + O2 + spermidine = 3-aminopropanal + H2O2 + putrescine.
H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine.
polyamine oxidase (propane-1,3-diamine-forming)
As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines.
Catalyzes less efficiently the oxidation of N(1)-acetylspermine and spermine.
Differs in specificity from EC 1.5.3.13, EC 1.5.3.15, EC 1.5.3.16 and EC 1.5.3.17.
H2O + O2 + spermidine = 4-aminobutanal + H2O2 + propane-1,3-diamine.
H2O + O2 + spermine = H2O2 + N-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine.
H2O + N(1)-acetylspermine + O2 = H2O2 + N-(3-acetamidopropyl)-4-aminobutanal + propane-1,3-diamine.
N(8)-acetylspermidine oxidase (propane-1,3-diamine-forming)
Also active with N(1)-acetylspermine, weak activity with N(1),N(12)-diacetylspermine.
No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine.
Absence of monoamine oxidase (EC 1.4.3.4) activity.
Differs in specificity from EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.16 and EC 1.5.3.17.
H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 + propane-1,3-diamine.
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency.
The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyzes the oxidation of spermine at the exo (three-carbon) side of the tertiary amine.
Differs in specificity from EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.15 and EC 1.5.3.17.
H2O + norspermine + O2 = 3-aminopropanal + H2O2 + norspermidine.
The non-specific polyamine oxidases may differ from each other considerably.
The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N(8)-acetylspermidine.
The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine.
The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines.
The specific polyamine oxidases are classified as EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.15 and EC 1.5.3.16.
The enzyme is involved in pipecolic acid biosynthesis.
H2O + L-saccharopine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + L-glutamate.
4-methylaminobutanoate oxidase (formaldehyde-forming)
In the enzyme from the soil bacterium Arthrobacter nicotinovorans the cofactor is covalently bound.
Participates in the nicotine degradation pathway of this organism.
4-(methylamino)butanoate + H2O + O2 = 4-aminobutanoate + formaldehyde + H2O2.
N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating)
Isolated from the mold Cladosporium sp. G-10.
Acts on N(6)-(carboxymethyl)lysine, 6-[(carboxymethy)amino]hexanoic acid, sarcosine and N-ethylglycine.
It has negligible action on glycine (cf. EC 1.4.3.19).
an N-alkylglycine + H2O + O2 = an alkylamine + glyoxylate + H2O2.
4-methylaminobutanoate oxidase (methylamine-forming)
The enzyme participates in the nicotine degradation pathway of the soil bacterium Arthrobacter nicotinovorans.
Has a very weak EC 1.4.3.4 activity with 4-aminobutanoate.
4-(methylamino)butanoate + H2O + O2 = H2O2 + methylamine + succinate semialdehyde.
The enzyme from the archaeon Methanothermobacter marburgensis is Si-face specific with respect to C5 of coenzyme F420.
O2 + 2 reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + 2 H2O + 2 oxidized coenzyme F420-(gamma-L-Glu)(n).
Characterized from the bacterium Ochrobactrum sp. G-1.
The catalytic cycle starts with a reduction of the FAD cofactor by one molecule of glyphosate, yielding reduced FAD and a Schiff base of aminomethylphosphonate with glyoxylate that is hydrolyzed to the single components.
The reduced FAD is reoxidized by oxygen, generating water and an oxygenated flavin intermediate, which catalyzes the oxygenation of a second molecule of glyphosate, forming the second pair of aminomethylphosphonate and glyoxylate.
2 glyphosate + O2 = 2 aminomethylphosphonate + 2 glyoxylate + 2 H(+).
sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)
The enzyme, found in some bacterial species, is composed of four different subunits and two active sites connected by a large 'reaction chamber'.
The enzyme contains three cofactors: non-covalently bound FAD and NAD(+), and FMN that is covalently bound to a histidine residue.
In the absence of folate the enzyme catalyzes the reaction of EC 1.5.3.1.
(6S)-5,6,7,8-tetrahydrofolate + O2 + sarcosine = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O2.
In the reverse direction of reaction, the reduction of 6-pyruvoyl-tetrahydropterin is accompanied by the opening of the 6-membered pyrazine ring and the formation of the 7-membered diazepine ring.
The pyrimidodiazepine involved is an acetyldihydro derivative.
Involved in the formation of the eye pigment drosopterin in Drosophila melanogaster.
2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one + glutathione disulfide + H2O = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 glutathione.
electron-transferring-flavoprotein dehydrogenase
electron transfer flavoprotein-ubiquinone oxidoreductase
Forms part of the mitochondrial electron-transfer system.
a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein].
The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor.
In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88.
Both activities are carried out by the same enzyme in enterobacteria.
a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+).
a ubiquinone + L-proline = (S)-1-pyrroline-5-carboxylate + a ubiquinol + H(+).
The enzyme from human also has low activity with L-proline (Cf. EC 1.5.5.2).
a quinone + trans-4-hydroxy-L-proline = (3R,5S)-1-pyrroline-3-hydroxy-5-carboxylate + a quinol + H(+).
methylenetetrahydrofolate reductase (ferredoxin)
The enzyme from Clostridium formicoaceticum catalyzes the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate.
However, unlike EC 1.5.1.20, EC 1.5.1.53, or EC 1.5.1.24, there is no activity with either NADH or NADP(+).
(6S)-5-methyl-5,6,7,8-tetrahydrofolate + 2 oxidized [2Fe-2S]-[ferredoxin] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
coenzyme F420 oxidoreductase (ferredoxin)
2 oxidized [2Fe-2S]-[ferredoxin] + reduced coenzyme F420-(gamma-L-Glu)(n) = 3 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) + 2 reduced [2Fe-2S]-[ferredoxin].
dimethylamine + H(+) + H2O + oxidized [electron-transfer flavoprotein] = formaldehyde + methylamine + reduced [electron-transfer flavoprotein].
A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors.
Phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors.
H(+) + H2O + oxidized [electron-transfer flavoprotein] + trimethylamine = dimethylamine + formaldehyde + reduced [electron-transfer flavoprotein].
A flavoprotein (FMN) found in eukaryotes.
In the absence of tetrahydrofolate the enzyme produces formaldehyde. cf. EC 1.5.3.1 and EC 1.5.3.24.
(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + H(+) + oxidized [electron-transfer flavoprotein] + sarcosine = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + glycine + reduced [electron-transfer flavoprotein].
An imine intermediate is channeled from the FAD binding site to the 5,6,7,8-tetrahydrofolate binding site through a 40 A tunnel.
In the absence of 5,6,7,8-tetrahydrofolate the enzyme forms formaldehyde.
(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + H(+) + N,N-dimethylglycine + oxidized [electron-transfer flavoprotein] = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + reduced [electron-transfer flavoprotein] + sarcosine.
methylenetetrahydromethanopterin dehydrogenase
5,10-methylenetetrahydromethanopterin dehydrogenase
N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase
Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analog.
The enzyme is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
5,10-methylenetetrahydromethanopterin + 2 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n).
5,10-methylenetetrahydromethanopterin reductase
5,10-methylenetetrahydromethanopterin cyclohydrolase
coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase
N(5),N(10)-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
N(5),N(10)-methylenetetrahydromethanopterin reductase
Catalyzes an intermediate step in methanogenesis from CO2 and H2 in archaea.
5-methyl-5,6,7,8-tetrahydromethanopterin + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n).
coenzyme F420:methanophenazine dehydrogenase
The enzyme, found in some methanogenic archaea, is responsible for the reoxidation of coenzyme F420, which is reduced during methanogenesis, and for the reduction of methanophenazine to dihydromethanophenazine, which is required by EC 1.8.98.1.
The enzyme is membrane-bound, and is coupled to proton translocation across the cytoplasmic membrane, generating a proton motive force that is used for ATP generation.
methanophenazine + reduced coenzyme F420-(gamma-L-Glu)(n) = dihydromethanophenazine + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n).
A + L-pipecolate = AH2 + H(+) + L-1-piperideine-6-carboxylate.
The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases.
(S)-nicotine + A + H2O = (S)-6-hydroxynicotine + AH2.
(R)-nicotine + A + H2O = (R)-6-hydroxynicotine + AH2.
A number of N-methyl-substituted amino acids can act as donors.
2,6-dichloroindophenol is the best acceptor.
A + H2O + N-methyl-L-glutamate = AH2 + formaldehyde + L-glutamate.
Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor.
A + H2O + spermidine = 4-aminobutanal + AH2 + propane-1,3-diamine.
Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is a prenyl group.
Although this activity was previously thought to be catalyzed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide.
2,6-dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and copper(II) in the presence of imidazole can act as acceptors.
This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production.
A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2.
The enzyme prefers D-proline and acts on other D-amino acid with lower efficiency.
A + D-proline = 1-pyrroline-2-carboxylate + AH2.
6-hydroxypseudooxynicotine dehydrogenase
Contains a cytidylyl molybdenum cofactor.
The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans.
6-hydroxypseudooxynicotine + A + H2O = 2,6-dihydroxypseudooxynicotine + AH2.
dihydromethanopterin reductase (acceptor)
This archaeal enzyme catalyzes the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis.
The enzyme is characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii.
5,6,7,8-tetrahydromethanopterin + A = 7,8-dihydromethanopterin + AH2.
NAD(P)(+) transhydrogenase (Si-specific)
nicotinamide nucleotide transhydrogenase
Si-specific with respect to both NAD(+) and NADP(+).
NAD(P)(+) transhydrogenase (Re/Si-specific)
NAD(P)(+) transhydrogenase (AB-specific)
The enzyme from heart mitochondria is Re-specific with respect to NAD(+) and Si-specific with respect to NADP(+) (cf. EC 1.6.1.1.).
The enzyme catalyzes the NADPH-driven reduction of NAD(+).
This entry stands for enzymes whose stereo-specificity with respect to NADPH is not known (cf. EC 1.6.1.1 and EC 1.6.1.2).
The iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP(+) with reduced ferredoxin and the endergonic reduction of NADP(+) with NADH.
H(+) + NADH + 2 NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NAD(+) + 2 NADPH + 2 oxidized [2Fe-2S]-[ferredoxin].
2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+).
cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent)
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase
reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
This enzyme catalyzes the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P450 monooxygenases (e.g. EC 1.14.14.1) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN.
It also reduces cytochrome b5 and cytochrome c.
The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450].
2 Fe(III)-[cytochrome c] + NADPH = 2 Fe(II)-[cytochrome c] + H(+) + NADP(+).
2 Fe(III)-[cytochrome c2] + NADPH = 2 Fe(II)-[cytochrome c2] + H(+) + NADP(+).
2 Fe(III)-[leghemoglobin] + NADPH = 2 Fe(II)-[leghemoglobin] + H(+) + NADP(+).
2 Fe(III)-[leghemoglobin] + NADH = 2 Fe(II)-[leghemoglobin] + H(+) + NAD(+).
When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen.
The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups.
This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalyzed biosynthesis of thyroid hormones.
By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4).
The enzymes from the anaerobic archaea Methanocaldococcus jannaschii and Pyrococcus furiosus also produce low amounts of H2O.
Unlike EC 1.6.3.1 it has no activity toward NADPH.
The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O-forming enzyme and a H2O2-forming enzyme (cf. EC 1.6.3.3).
Renalase, previously thought to be a hormone, is a flavoprotein secreted into the blood by the kidney that oxidizes the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P)H back to beta-NAD(P)(+).
These isomeric forms, generated by non-specific reduction of beta-NAD(P)(+) or by tautomerization of beta-NAD(P)H, are potent inhibitors of primary metabolism dehydrogenases and pose a threat to normal respiration.
1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+).
1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+).
1,6-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+).
1,6-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+).
dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone)
reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
viologen accepting pyridine nucleotide oxidoreductase
The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone.
The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.
a quinone + H(+) + NADH = a quinol + NAD(+).
a quinone + H(+) + NADPH = a quinol + NADP(+).
H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-ascorbate + NAD(+).
Catalyzes the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates.
Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhibitors with respect to the quinone substrate.
The semiquinone free-radical product may be non-enzymically reduced to the hydroquinone or oxidized back to quinone in the presence of O2.
Abundant in the lens of the eye of some mammalian species.
2 a quinone + H(+) + NADPH = 2 a 1,4-benzosemiquinone + NADP(+).
Involved in the 4-nitrophenol degradation pathway in bacteria.
1,4-benzoquinone + H(+) + NADPH = hydroquinone + NADP(+).
The enzyme differs in substrate speificity from other quinone reductases.
The enzyme in Burkholderia cepacia is inducible by 2,4,5-trichlorophenoxyacetate.
2-hydroxy-1,4-benzoquinone + 2 H(+) + NADH = benzene-1,2,4-triol + NAD(+).
NADH:ubiquinone reductase (non-electrogenic)
Occurs in mitochondria of yeast and plants, and in aerobic bacteria.
Unlike EC 7.1.1.2, this enzyme does not pump proteons of sodium ions across the membrane.
The enzyme from Escherichia coli is specific for NADPH and is most active with quinone derivatives and ferricyanide as electron acceptors.
The enzyme from hog liver is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
The enzyme, found in plants and cyanobacteria, is involved in the biosynthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I.
demethylphylloquinone + H(+) + NADPH = demethylphylloquinol + NADP(+).
Acting on other nitrogenous compounds as donors
H2O + NAD(+) + nitrite = H(+) + NADH + nitrate.
nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate))
H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate.
assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase
triphosphopyridine nucleotide-nitrate reductase
nitrite reductase (reduced nicotinamide adenine dinucleotide (phosphate))
The enzymes from the fungi Neurospora crassa, Emericella nidulans and Candida nitratophila can use either NADPH or NADH as electron donor.
2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite.
2 hydroxylamine + 2 NAD(+) = 2 H(+) + hyponitrous acid + 2 NADH.
dibromopropylaminophenylazobenzoic azoreductase
N,N-dimethyl-4-phenylazoaniline azoreductase
NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase
NADPH:4-(dimethylamino)azobenzene oxidoreductase
nicotinamide adenine dinucleotide (phosphate) azoreductase
The reaction occurs in the reverse direction to that shown above.
Other azo dyes, such as Methyl Red, Rocceline, Solar Orange and Sumifix Black B can also be reduced.
aniline + N,N-dimethyl-1,4-phenylenediamine + 2 NADP(+) = 4-(dimethylamino)azobenzene + 2 H(+) + 2 NADPH.
guanosine 5'-monophosphate oxidoreductase
NADPH:guanosine-5'-phosphate oxidoreductase (deaminating)
IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH.
NAD(P)H:4-nitroquinoline-N-oxide oxidoreductase
4-(hydroxyamino)quinoline N-oxide + H2O + 2 NADP(+) = 4-nitroquinoline N-oxide + 2 H(+) + 2 NADPH.
4-(hydroxyamino)quinoline N-oxide + H2O + 2 NAD(+) = 4-nitroquinoline N-oxide + 2 H(+) + 2 NADH.
H2O + NAD(+) + NH4(+) = 2 H(+) + hydroxylamine + NADH.
4-(dimethylamino)phenylazoxybenzene reductase
dimethylaminoazobenzene N-oxide reductase
N,N-dimethyl-p-aminoazobenzene oxide reductase
NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase
4-(dimethylamino)azobenzene + H2O + NADP(+) = 4-(dimethylamino)phenylazoxybenzene + H(+) + NADPH.
N-hydroxy-2-acetylaminofluorene reductase
Also acts, more slowly, on N-hydroxy-4-acetamidobiphenyl.
2-acetamidofluorene + H2O + NAD(+) = H(+) + N-hydroxy-2-acetamidofluorene + NADH.
2-acetamidofluorene + H2O + NADP(+) = H(+) + N-hydroxy-2-acetamidofluorene + NADPH.
The reaction occurs in the reverse direction.
This enzyme catalyzes one of the early steps in the synthesis of queosine (Q-tRNA), and is followed by the action of EC 2.4.2.29.
Queosine is found in the wobble position of tRNAGUN in eukaryotes and bacteria and is thought to be involved in translational modulation.
7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
nitric oxide reductase [NAD(P)(+), nitrous oxide-forming]
The enzyme from Fusarium oxysporum utilizes only NADH, but the isozyme from Trichosporon cutaneum utilizes both NADH and NADPH.
The electron transfer from NAD(P)H to heme occurs directly, not requiring flavin or other redox cofactors.
H2O + NAD(+) + nitrous oxide = H(+) + NADH + 2 nitric oxide.
H2O + NADP(+) + nitrous oxide = H(+) + NADPH + 2 nitric oxide.
nitrite reductase (reduced nicotinamide adenine dinucleotide)
This prokaryotic enzyme is specific for NADH.
In addition to catalyzing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyze the 2-electron reduction of hydroxylamine to ammonia.
The enzyme, characterized from Pseudomonas species, catalyzes two successive reductions of nitrobenzene, via a nitrosobenzene intermediate.
It is also active on 1-chloro-4-nitrobenzene.
H2O + N-phenylhydroxylamine + 2 NADP(+) = 2 H(+) + 2 NADPH + nitrobenzene.
The enzyme catalyzes the reductive cleavage of an azo bond in aromatic azo compounds to form the corresponding amines.
anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH.
cytochrome c-551:O2, NO2(+) oxidoreductase
nitrite reductase (cytochrome; NO-forming)
The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria.
One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1.
Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin.
Cytochrome cd1 also has oxidase and hydroxylamine reductase activities.
May also catalyze the reaction of EC 1.7.99.1 since this is a well-known activity of cytochrome cd1.
Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite.
nitrite reductase (cytochrome; ammonia-forming)
The enzyme also reduces nitric oxide and hydroxylamine to ammonia, and sulfite to sulfide.
6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-[cytochrome c] + 8 H(+) + nitrite.
trimethylamine-N-oxide reductase (cytochrome c)
Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor.
The reductant is a membrane-bound multiheme cytochrome c.
Also reduces dimethyl sulfoxide to dimethyl sulfide.
2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-[cytochrome c] + 3 H(+) + trimethylamine N-oxide.
H2O + NAD(+) + trimethylamine = 2 H(+) + NADH + trimethylamine N-oxide.
The reaction is observed only in the direction of nitrous oxide reduction.
Contains the mixed-valent dinuclear CuA species at the electron entry site of the enzyme, and the tetranuclear Cu-Z center in the active site.
In Paracoccus pantotrophus, the electron donor is cytochrome c552.
2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c] + 2 H(+) + nitrous oxide.
The enzyme from Pseudomonas aeruginosa contains a dinuclear center comprising a non-heme iron center and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551.
2 Fe(III)-[cytochrome c] + H2O + nitrous oxide = 2 Fe(II)-[cytochrome c] + 2 H(+) + 2 nitric oxide.
The enzymes from the nitrifying bacterium Nitrosomonas europaea and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins with seven c-type hemes and one specialized P460-type heme per subunit.
The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate.
While nitrite is the main product, the enzyme from Nitrosomonas europaea can also produce nitric oxide by catalyzing the activity of EC 1.7.2.9.
4 Fe(III)-[cytochrome c] + H2O + hydroxylamine = 4 Fe(II)-[cytochrome c] + 5 H(+) + nitrite.
The enzyme, characterized from anaerobic ammonia oxidizers (anammox bacteria), is one of only a few enzymes that are known to form an N-N bond (other examples include EC 1.7.1.14 and EC 4.8.1.1).
The enzyme from the bacterium Candidatus Kuenenia stuttgartiensis is heterotrimeric and contains multiple c-type cytochromes.
3 Fe(III)-[cytochrome c] + H2O + hydrazine = 3 Fe(II)-[cytochrome c] + 2 H(+) + NH4(+) + nitric oxide.
The enzyme, which is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria, has been purified from the bacterium Candidatus Kuenenia stuttgartiensis.
The electrons derived from hydrazine are eventually transferred to the quinone pool.
4 Fe(III)-[cytochrome c] + hydrazine = 4 Fe(II)-[cytochrome c] + 4 H(+) + N2.
The enzyme, characterized from the anaerobic ammonium-oxidizing (anammox) bacterium Kuenenia stuttgartiensis, is very similar to EC 1.7.2.6.
Both enzymes are homotrimeric enzymes in which each subunit contains seven c-type hemes and one specialized P460-type heme that is bound to a tyrosine residue in an adjacent subunit.
However, this enzyme catalyzes only the 3 electron oxidation of hydroxylamine, forming nitric oxide, and is not capable of performing further oxidation to form nitrite.
3 Fe(III)-[cytochrome c] + hydroxylamine = 3 Fe(II)-[cytochrome c] + 3 H(+) + nitric oxide.
While nitroethane may be the physiological substrate, the enzyme also acts on several other nitroalkanes, including 1-nitropropane, 2-nitropropane, 1-nitrobutane, 1-nitropentane, 1-nitrohexane, nitrocyclohexane and some nitroalkanols.
Differs from EC 1.13.12.16 in that the preferred substrates are neutral nitroalkanes rather than anionic nitronates.
a primary nitroalkane + H2O + O2 = an aldehyde + H(+) + H2O2 + nitrite.
a secondary nitroalkane + H2O + O2 = a ketone + H(+) + H2O2 + nitrite.
H2O + nitroethane + O2 = acetaldehyde + H(+) + H2O2 + nitrite.
N-acetylindoxyl + O2 = H2O + N-acetylisatin.
Was previously thought to be a copper protein, but it is now known that the enzymes from soybean (Glycine max), the mold Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion.
The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalyzed pathway in which EC 3.5.2.17 catalyzes the first step.
The enzyme is different from EC 1.14.13.113.
H2O + O2 + urate = 5-hydroxyisourate + H2O2.
The primary products of the enzymatic reaction are probably the nitropropanoate free radical and superoxide.
Also acts, more slowly, on 4-aci-nitrobutanoate.
H2O + O2 + propionate 3-nitronate = 3-oxopropanoate + H(+) + H2O2 + nitrite.
The enzyme from the heterotrophic nitrifying bacterium Paracoccus denitrificans contains three to five non-heme, non-iron-sulfur iron atoms and interacts with cytochrome c556 and pseudoazurin.
Under anaerobic conditions in vitro only nitrous oxide is formed.
Presumably nitroxyl is released and combines with a second nitroxyl to give nitrous oxide and water.
When oxygen is present, nitrite is formed.
hydroxylamine + O2 = H(+) + H2O + nitrite.
A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.
a quinol + nitrate = a quinone + H2O + nitrite.
a menaquinol + 2 nitric oxide = a menaquinone + H2O + nitrous oxide.
The enzyme is one of the nitrophorins from the salivary gland of the blood-feeding insect Rhodnius prolixus.
Nitric oxide produced induces vasodilation after injection.
Nitrophorins 2 and 4 can also catalyze this reaction.
2 H(+) + 3 nitrite = H2O + nitrate + 2 nitric oxide.
2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin].
H2O + nitrite + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + nitrate + 2 reduced [2Fe-2S]-[ferredoxin].
Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine.
A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine.
The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast.
Different from EC 1.8.99.5, which is involved in prokaryotic sulfur-based energy metabolism.
3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite.
H2O + hypotaurine + NAD(+) = H(+) + NADH + taurine.
E3 component of alpha-ketoacid dehydrogenase complexes
A component of the multienzyme 2-oxo-acid dehydrogenase complexes.
In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups.
It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes.
Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine.
It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate.
Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase.
The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein.
(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH.
(R)-dihydrolipoamide + NAD(+) = (R)-lipoamide + H(+) + NADH.
2-oxopropyl-CoM reductase (carboxylating)
NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase
NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase
Also acts on thioethers longer in chain length on the oxo side, e.g. 2-oxobutyl-CoM, but this portion must be attached to CoM (2-sulfanylethane-1-sulfonate); no CoM analogs will substitute.
Forms component II of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
acetoacetate + coenzyme M + NADP(+) = 2-oxopropyl-coenzyme M + CO2 + NADPH.
2 L-cysteine + NAD(+) = H(+) + L-cystine + NADH.
NADPH:oxidized-glutathione oxidoreductase
Activity is dependent on a redox-active disulfide in each of the active centers.
2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH.
[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH.
[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) + NADPH.
NADPH:oxidized thioredoxin oxidoreductase
[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH.
coenzyme A disulfide-glutathione reductase
coenzyme A glutathione disulfide reductase
NADPH-dependent coenzyme A-SS-glutathione reductase
CoA + glutathione + NADP(+) = CoA-glutathione + H(+) + NADPH.
3-sulfanyl-2-(sulfanylmethyl)propanoate + NAD(+) = asparagusate + H(+) + NADH.
N(1),N(8)-bis(glutathionyl)spermidine reductase
Trypanothione disulfide is the oxidized form of N(1),N(8)-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata.
The activity is dependent on a redox-active cystine at the active center (cf. EC 1.8.1.7).
NADP(+) + trypanothione = H(+) + NADPH + trypanothione disulfide.
bis-gamma-glutamylcystine reductase (NADPH)
NADPH:bis-gamma-glutamylcysteine oxidoreductase
The enzyme, which is found only in halobacteria, maintains the concentration of gamma-glutamylcysteine, the major low molecular weight thiol in halobacteria.
Not identical with EC 1.8.1.7 or EC 1.8.1.14.
2 gamma-L-glutamyl-L-cysteine + NADP(+) = bis-gamma-glutamylcystine + H(+) + NADPH.
Not identical with EC 1.8.1.6, EC 1.8.1.7 or EC 1.8.1.13.
The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH, while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes.
2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH.
No activity with glutathione, trypanothione or coenzyme A as substrate.
2 mycothiol + NADP(+) = H(+) + mycothione + NADPH.
2 mycothiol + NAD(+) = H(+) + mycothione + NADH.
The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 back to glutathione amide (it catalyzes the reaction in the opposite direction to that shown).
The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH.
2 glutathione amide + NAD(+) = glutathione amide disulfide + H(+) + NADH.
dimethyl sulfoxide + H2O + NAD(+) = dimethyl sulfone + H(+) + NADH.
NAD(P)H sulfur oxidoreductase (CoA-dependent)
coenzyme A-dependent NADPH sulfur oxidoreductase
This enzyme, characterized from the archaeon Pyrococcus furiosus, is responsible for NAD(P)H-linked sulfur reduction.
The activity with NADH is about half of that with NADPH.
The reaction is dependent on CoA, although the nature of this dependency is not well understood.
hydrogen sulfide + NADP(+) = NADPH + sulfur.
hydrogen sulfide + NAD(+) = NADH + sulfur.
In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation.
The enzyme also catalyzes the reduction of sulfur with lower activity.
hydrogen sulfide + NADP(+) + n sulfur = NADPH + (n+1) sulfur.
4,4'-dithiodibutanoate disulfide reductase
2 4-sulfanylbutanoate + NAD(+) = 4,4'-disulfanyldibutanoate + H(+) + NADH.
dissimilatory dimethyldisulfide reductase
The enzyme's activity has been demonstrated in the bacterium Thiobacillus thioparus E6.
The methanethiol formed is eventually oxidized to sulfate and carbon dioxide, and the latter assimilated for autotrophic growth.
2 methanethiol + NAD(+) = dimethyl disulfide + H(+) + NADH.
2 Fe(III)-[cytochrome c] + H2O + sulfite = 2 Fe(II)-[cytochrome c] + 2 H(+) + sulfate.
The enzyme catalyzes the reversible formation of a sulfur-sulfur bond between the sulfane atoms of two thiosulfate molecules, yielding tetrathionate and releasing two electrons.
In many bacterial species the enzyme is a diheme c-type cytochrome.
In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, a second diheme cytochrome (TsdB) acts as the electron acceptor.
However, some organisms, such as Allochromatium vinosum, lack TsdB.
The electron acceptor in these organisms may be the high-potential iron-sulfur protein (HiPIP).
2 Fe(III)-[cytochrome c] + 2 thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + tetrathionate.
sulfide-cytochrome-c reductase (flavocytochrome c)
2 Fe(III)-[cytochrome c] + hydrogen sulfide = 2 Fe(II)-[cytochrome c] + H(+) + sulfur.
dimethyl sulfide:cytochrome c2 reductase
The enzyme from Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters.
dimethyl sulfide + 2 Fe(III)-[cytochrome c2] + H2O = dimethyl sulfoxide + 2 Fe(II)-[cytochrome c2] + 2 H(+).
The enzyme is found in sulfate-reducing bacteria.
The source of the electrons is molecular hydrogen, via EC 1.12.2.1.
The organisms utilize the sulfite that is produced for energy generation by EC 1.8.99.5.
2 Fe(III)-[cytochrome c3] + hydrogen sulfide + sulfite = 2 Fe(II)-[cytochrome c3] + thiosulfate.
The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate.
The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component.
The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine.
During the process, six electrons are transferred to the electron chain via cytochrome c.
6 Fe(III)-[cytochrome c] + 3 H2O + S-disulfanyl-L-cysteinyl-[SoxY protein] = 6 Fe(II)-[cytochrome c] + 7 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein].
The enzyme, characterized from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio paradoxus, contains three copper ions in its active site.
It catalyzes the direct conversion of thiocyanate into cyanate and elemental sulfur without involvement of molecular oxygen.
2 Fe(III)-[cytochrome c] + H2O + thiocyanate = cyanate + 2 Fe(II)-[cytochrome c] + 2 H(+) + sulfur.
R may be =S or =O, or a variety of other groups.
Also acts, more slowly, on L-cysteine and several other thiols.
2 glutathione + O2 = glutathione disulfide + H2O2.
H2O + methanethiol + O2 = formaldehyde + H(+) + H2O2 + hydrogen sulfide.
Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine.
N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates.
May represent the final step in the degradation of prenylated proteins in mammalian tissues.
an S-prenyl-L-cysteine + H2O + O2 = a prenal + H2O2 + L-cysteine.
H2O + O2 + S-(2E,6E)-farnesyl-L-cysteine = (2E,6E)-farnesal + H2O2 + L-cysteine.
[(2E,6E,10E)-geranylgeranyl]-L-cysteine + H2O + O2 = (2E,6E,10E)-geranylgeranial + H2O2 + L-cysteine.
In contrast to mammalian EC 1.8.3.5 the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine.
Calpha-formylglycine-generating enzyme 1
The enzyme, which is found in both prokaryotes and eukaryotes, catalyzes a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity.
The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro.
Glutathione alo acts in vitro, but it is not known whether it is used in vivo.
2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl-[sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide.
glutathione--homocystine transhydrogenase
The reactions catalyzed by this enzyme and by others in this subclass may be similar to those catalyzed by EC 2.5.1.18.
2 glutathione + L,L-homocystine = glutathione disulfide + 2 L-homocysteine.
protein-disulfide reductase (glutathione)
Reduces insulin and some other proteins.
[protein]-disulfide + 2 glutathione = [protein]-dithiol + glutathione disulfide.
glutathione--CoA-glutathione transhydrogenase
CoA + glutathione disulfide = CoA-glutathione + glutathione.
2 glutathione + L-cystine = glutathione disulfide + 2 L-cysteine.
enzyme-thiol transhydrogenase (glutathione-disulfide)
[xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase
enzyme-thiol transhydrogenase (oxidized-glutathione)
glutathione-dependent thiol:disulfide oxidoreductase
Converts EC 1.17.1.4 into EC 1.17.3.2 in the presence of glutathione disulfide.
Also reduces the disulfide bond of ricin.
Not inhibited by Cu(2+) or thiol reagents.
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione.
phosphoadenylyl-sulfate reductase (thioredoxin)
phosphoadenosine-phosphosulfate reductase
thioredoxin:3'-phospho-adenylylsulfate reductase
thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase
The enzyme from Escherichia coli will use thioredoxins from other species.
[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol.
adenylyl-sulfate reductase (glutathione)
AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming)
Differs from EC 1.8.99.2, in using glutathione as the reductant.
Glutathione can be replaced by gamma-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or 2-sulfanylethan-1-ol (2-mercaptoethanol).
The enzyme from Arabidopsis thaliana contains a glutaredoxin-like domain.
Also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.
AMP + glutathione disulfide + 2 H(+) + sulfite = adenosine 5'-phosphosulfate + 2 glutathione.
adenylyl-sulfate reductase (thioredoxin)
thioredoxin-dependent 5'-adenylylsulfate reductase
Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8.
Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 and EC 1.8.99.2.
[thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate.
peptide-methionine (S)-S-oxide reductase
methionine S-oxide reductase (S-form oxidizing)
Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid.
On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly.
Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged.
The reaction proceeds via a sulfenic-acid intermediate.
[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein].
[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (S)-S-oxide.
peptide-methionine (R)-S-oxide reductase
methionine S-oxide reductase (R-form oxidizing)
Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide.
While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater.
For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well.
[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein].
The reaction occurs in the opposite direction to that given above.
Dithiothreitol can replace reduced thioredoxin.
L-Methionine (R)-S-oxide is not a substrate (see EC 1.8.4.14).
Unlike EC 1.8.4.12 this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate.
Differs from EC 1.8.4.13, in that L-methionine (S)-S-oxide is not a substrate.
[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (R)-S-oxide.
protein dithiol oxidoreductase (disulfide-forming)
DsbA is a periplasmic thiol:disulfide oxidoreductase found in Gram-negative bacteria that promotes protein disulfide bond formation.
DsbA contains a redox active disulfide bond that is catalytically transferred via disulfide exchange to a diverse range of newly translocated protein substrates.
The protein is restored to the oxidized state by EC 1.8.5.9.
[DsbA protein]-disulfide + [protein]-dithiol = [DsbA protein]-dithiol + [protein]-disulfide.
DsbD is an inner membrane protein found in Gram-negative bacteria that transfers electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG, reducing disulfide bonds in the target proteins to dithiols.
DsbD consists of three domains: a periplasmic N-terminal domain, a central transmembrane domain and a periplasmic C-terminal domain.
[protein]-dithiol + [thioredoxin]-disulfide = [protein]-disulfide + [thioredoxin]-dithiol.
2 glutathione + L-dehydroascorbate = glutathione disulfide + L-ascorbate.
thiosulfate oxidoreductase, tetrathionate-forming
The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly.
Unlike EC 1.8.2.2, this enzyme cannot utilize cytochrome c as an acceptor.
6-decylubiquinone + 2 thiosulfate = 6-decylubiquinol + tetrathionate.
The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor.
It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron-sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool.
The electrons are passed through DmsB to DmsA and on to DMSO.
The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
a menaquinone + dimethyl sulfide + H2O = a menaquinol + dimethyl sulfoxide.
Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species.
This enzyme catalyzes the formation of sulfur globules.
It repeats the catalytic cycle without releasing the product, producing a polysulfide of up to 10 sulfur atoms.
The reaction stops when the maximum length of the polysulfide that can be accommodated in the sulfide oxidation pocket is achieved.
The enzyme also plays an important role in anoxygenic bacterial photosynthesis.
n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur.
The enzyme, characterized from the bacterium Salmonella enterica, is similar to EC 1.17.5.3.
The reaction occurs in vivo in the direction of thiosulfate disproportionation, which is highly endergonic.
It is driven by the proton motive force that occurs across the cytoplasmic membrane.
a quinone + 2 H(+) + hydrogen sulfide + sulfite = a quinol + thiosulfate.
This membrane-bound bacterial enzyme catalyzes the direct oxidation of sulfite to sulfate in the cytoplasm.
Characterized from the bacteria Ruegeria pomeroyi and Allochromatium vinosum.
a quinone + H2O + sulfite = a quinol + sulfate.
This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyze the glutathione-dependent reduction of glutathionyl-hydroquinones.
The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)-hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone.
Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.
2-(glutathione-S-yl)-hydroquinone + glutathione = glutathione disulfide + hydroquinone.
eukaryotic sulfide quinone oxidoreductase
This eukaryotic enzyme, located at the inner mitochondrial membrane, catalyzes the first step in the metabolism of sulfide.
While both sulfite and glutathione have been shown to act as sulfane sulfur acceptors in vitro, it is thought that the latter acts as the main acceptor in vivo.
The electrons are transferred via FAD and quinones to the electron transfer chain.
Unlike the bacterial homolog (EC 1.8.5.4), which repeats the catalytic cycle without releasing the product, producing a polysulfide, the eukaryotic enzyme transfers the persulfide to an acceptor at the end of each catalytic cycle.
a quinone + glutathione + H(+) + hydrogen sulfide = a quinol + S-sulfanylglutathione.
protein dithiol:quinone oxidoreductase DsbB
DsbB is a protein found in Gram-negative bacteria that functions within a pathway for protein disulfide bond formation.
The enzyme catalyzes the oxidation of the DsbA protein by generating disulfide bonds de novo via the reduction of membrane quinones.
[DsbA protein]-dithiol + a quinone = [DsbA protein]-disulfide + a quinol.
assimilatory sulfite reductase (ferredoxin)
The enzyme participates in sulfate assimilation.
While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria (cf. EC 1.8.1.2).
3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] = 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite.
The enzyme contains a [4Fe-4S] cluster and internal disulfide.
It forms a mixed disulfide with thioredoxin on one side, and docks ferredoxin on the other side, enabling two one-electron transfers.
The reduced thioredoxins generated by the enzyme activate the Calvin cycle enzymes EC 3.1.3.11, EC 3.1.3.37 and EC 2.7.1.19 as well as other chloroplast enzymes by disulfide reduction.
[thioredoxin]-disulfide + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [2Fe-2S]-[ferredoxin].
ferredoxin:CoB-CoM heterodisulfide reductase
HdrABC is an enzyme complex that is found in most methanogens and catalyzes the reduction of the CoB-CoM heterodisulfide back to CoB and CoM.
HdrA contains a FAD cofactor that acts as the entry point for electrons, which are transferred via HdrC to the HdrB catalytic subunit.
One form of the enzyme from Methanosarcina acetivorans (HdrA2B2C2) can also catalyze EC 1.8.98.4.
coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-[ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
dihydromethanophenazine:CoB--CoM heterodisulfide reductase
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1.
It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters.
coenzyme B + coenzyme M + methanophenazine = coenzyme M-coenzyme B heterodisulfide + dihydromethanophenazine.
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
In the course of the reaction of EC 1.11.1.15, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine.
Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme.
The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form.
Apparently the reductase first catalyzes the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between the two enzymes.
Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol.
[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-[peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-L-cysteinyl-[peroxiredoxin].
coenzyme F420-dependent sulfite reductase
The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, is involved in sulfite detoxification and assimilation.
2 H(+) + 3 H2O + hydrogen sulfide + 3 oxidized coenzyme F420-(gamma-L-Glu)(n) = 3 reduced coenzyme F420-(gamma-L-Glu)(n) + sulfite.
coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase
The enzyme, characterized from the archaeon Methanosarcina acetivorans, catalyzes the reduction of CoB-CoM heterodisulfide back to CoB and CoM.
The enzyme consists of three components, HdrA, HdrB and HdrC, all of which contain [4Fe-4S] clusters.
Electrons enter at HdrA, which also contains FAD, and are transferred via HdrC to the catalytic component, HdrB.
During methanogenesis from acetate the enzyme catalyzes the activity of EC 1.8.7.3.
However, it can also use electron bifurcation to direct electron pairs from reduced coenzyme F420 toward the reduction of both ferredoxin and CoB-CoM heterodisulfide.
This activity is proposed to take place during Fe(III)-dependent anaerobic methane oxidation.
coenzyme B + coenzyme M + 4 H(+) + 2 oxidized coenzyme F420-(gamma-L-Glu)(n) + 2 reduced [2Fe-2S]-[ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 reduced coenzyme F420-(gamma-L-Glu)(n).
H2:CoB-CoM heterodisulfide,ferredoxin reductase
This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus.
It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase.
Electron pairs donated by the hydrogenase are transferred via its Delta subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide.
The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase.
coenzyme B + coenzyme M + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H2 + 2 oxidized [2Fe-2S]-[ferredoxin].
formate:CoB-CoM heterodisulfide,ferredoxin reductase
The enzyme is found in formate-oxidizing CO2-reducing methanogenic archaea such as Methanococcus maripaludis.
It consists of a cytoplasmic complex of HdrABC reductase and formate dehydrogenase.
Electron pairs donated by formate dehydrogenase are transferred to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide.
2 CO2 + coenzyme B + coenzyme M + 2 reduced [2Fe-2S]-[ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 formate + 2 oxidized [2Fe-2S]-[ferredoxin].
cysteine-type anaerobic sulfatase-maturating enzyme
Cys-type anaerobic sulfatase-maturating enzyme
A radical S-adenosylmethionine (AdoMet) enzyme that contains three [4Fe-4S] clusters.
The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-cysteine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity.
Some enzymes can also act on L-serine, see EC 1.1.98.7 and EC 1.8.3.7.
H2O + L-cysteinyl-[sulfatase] + S-adenosyl-L-methionine = 3-oxo-L-alanyl-[sulfatase] + 5'-deoxyadenosine + 2 H(+) + hydrogen sulfide + L-methionine.
A + AMP + 2 H(+) + sulfite = adenosine 5'-phosphosulfate + AH2.
The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers.
In sulfur reducers it catalyzes the reduction of sulfite to sulfide, while in sulfur oxidizers it catalyzes the opposite reaction.
The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase.
During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC.
This disulfide can be reduced by a number of proteins including DsrK and TcmB.
This enzyme is different from EC 1.8.1.2 and EC 1.8.7.1, which are involved in sulfate assimilation.
[DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide = [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite.
[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite.
2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-[cytochrome] + H2O + nitrite.
Fe(3+) + Fe(II)-[cytochrome c] = Fe(2+) + Fe(III)-[cytochrome c].
Acting on diphenols and related substances as donors
trans-acenaphthene-1,2-diol dehydrogenase
(+-)-trans-acenaphthene-1,2-diol + 2 NADP(+) = acenaphthene-1,2-dione + 2 H(+) + 2 NADPH.
A type 3 copper protein that catalyzes exclusively the oxidation of catechols (i.e., o-diphenols) to the corresponding o-quinones.
The enzyme also acts on a variety of substituted catechols.
It is different from tyrosinase, EC 1.14.18.1, which can catalyze both the monooxygenation of monophenols and the oxidation of catechols.
2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O.
A group of multi-copper proteins of low specificity.
Acts on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine.
The semiquinone may react further either enzymically or non-enzymically.
4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O.
4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical.
4 2-aminophenol + 3 O2 = 2 2-aminophenoxazin-3-one + 6 H2O.
3-hydroxyanthranilate + O2 = 6-imino-5-oxocyclohexa-1,3-dienecarboxylate + H2O2.
Also acts on benzene-1,4-diol and, more slowly, on some other p-quinols.
2 H(+) + O2 + rifamycin B = H2O2 + rifamycin O.
Contains chlorophyll a, beta-carotene, pheophytin, plastoquinone, a Mn4Ca cluster, heme and non-heme iron.
Four successive photoreactions, resulting in a storage of four positive charges, are required to oxidize two water molecules to one oxygen molecule.
2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2.
2 H2O + 4 hnu + 2 plastoquinone-9 = O2 + 2 plastoquinol-9.
The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force.
The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O.
The enzyme, isolated from the bacterium Streptomyces griseus, catalyzes an 8 electron oxidation.
Activation of the enzyme requires a copper chaperone (GriE).
It also acts on 3-amino-4-hydroxybenzaldehyde, giving grixazone A.
The second aldehyde group is presumably lost as formate.
The enzyme also catalyzes the reaction of EC 1.10.3.4.
2 3-amino-4-hydroxybenzoate + H(+) + N-acetyl-L-cysteine + 2 O2 = CO2 + grixazone B + 4 H2O.
2 3-amino-4-hydroxybenzaldehyde + N-acetyl-L-cysteine + 2 O2 = formate + grixazone A + H(+) + 3 H2O.
The enzyme, isolated from the bacteria Pseudomonas fluorescens 2-79 and Burkholderia lata 383, is involved in biosynthesis of the reduced forms of phenazine, phenazine-1-carboxylate, and phenazine-1,6-dicarboxylate, where it catalyzes multiple reactions.
(1R,6R)-1,4,5,5a,6,9-hexahydrophenazine-1,6-dicarboxylate + O2 = (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + H2O2.
(1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + O2 = (5aS)-5,5a-dihydrophenazine-1,6-dicarboxylate + H2O2.
(1R,10aS)-1,4,10,10a-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2.
(1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2.
This membrane-bound, di-heme containing enzyme, identified in the bacterium Escherichia coli, is responsible for the detoxification of superoxide in the periplasm.
In vivo the reaction proceeds in the opposite direction of that shown and produces oxygen.
Superoxide production was only observed when the enzyme was incubated in vitro with an excess of ubiquinol.
a ubiquinol + 2 O2 = a ubiquinone + 2 H(+) + 2 superoxide.
ribosyldihydronicotinamide dehydrogenase (quinone)
N-ribosyldihydronicotinamide dehydrogenase (quinone)
Unlike EC 1.6.5.2, this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides.
Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the estrogens 17beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor.
This enzyme can catalyze both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced.
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone + H(+) = a quinol + beta-nicotinamide D-riboside.
Ferricyanide, quinones, etc., can replace H2O2.
Acts on long-chain fatty acids from dodecanoic to octadecanoic acid.
H(+) + 2 H2O2 + hexadecanoate = CO2 + 3 H2O + pentadecanal.
2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O.
A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase.
The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor.
Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21.
Heme proteins with histidine as proximal ligand.
The iron in the resting enzyme is Fe(III).
They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS).
Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O.
Thyroid peroxidase catalyzes the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine.
It catalyzes both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.
2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O.
[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O.
[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O.
2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O.
[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine + [thyroglobulin]-dehydroalanine + 2 H2O.
Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12).
2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds.
Enzymes of this type are either heme-thiolate proteins, or contain vanadate.
A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type.
It catalyzes the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride.
At a separate site it catalyzes the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species.
In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities.
The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides.
Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes.
The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18).
It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids.
In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.
Oxidizes ascorbate and low molecular weight aromatic substrates.
The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 or undergoes non-enzymatic disproportionation to ascorbate and dehydroascorbate.
H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate.
phospholipid-hydroperoxide glutathione peroxidase
The products of action of EC 1.13.11.12 on phospholipids can act as acceptor; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9).
a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O.
The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin.
The enzyme oxidizes a bound Mn(2+) ion to Mn(3+) in the presence of hydrogen peroxide.
The product, Mn(3+), is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn(2+) and insoluble Mn(4+).
The complexed Mn(3+) ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates.
It is inactive with veratryl alcohol or nonphenolic substrates.
Involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi.
The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (Fe(IV)=O radical cation) at the active site.
A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (Fe(IV)=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state.
The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously.
The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic beta-O-4 linked arylglycerol beta-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site.
However larger lignin molecules can be degraded in the presence of veratryl alcohol.
It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates.
In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III).
This form can be rescued by interaction with two molecules of the free radical products.
In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O.
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O.
This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13 and EC 1.11.1.14.
Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates.
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin.
This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus.
The enzyme has peroxidase activity toward hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress.
The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16.
2 glutathione amide + H2O2 = glutathione amide disulfide + 2 H2O.
Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate.
They catalyze the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds.
Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria.
They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II).
The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid.
Bacterial TfuDyP catalyzes sulfoxidation.
2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate.
prostamide/prostaglandin F2alpha synthase
The enzyme contains a thioredoxin-type disulfide as a catalytic group.
Prostamide H2 and prostaglandin H2 are the best substrates; the latter is converted to prostaglandin F2alpha.
The enzyme also reduces tert-butyl hydroperoxide, cumene hydroperoxide and H2O2, but not prostaglandin D2 or prostaglandin E2.
[thioredoxin]-dithiol + prostaglandin H2 = [thioredoxin]-disulfide + prostaglandin F2alpha.
[thioredoxin]-disulfide + prostamide F2alpha = [thioredoxin]-dithiol + prostamide H2.
Differs from EC 1.11.1.7, peroxidase, in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site.
In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides.
The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
a hydroperoxy polyunsaturated fatty acid + H(+) + NADPH = a hydroxy polyunsaturated fatty acid + H2O + NADP(+).
(S)-2-hydroxypropylphosphonic acid epoxidase
(S)-2-hydroxypropylphosphonate epoxidase
2-hydroxypropylphosphonic acid epoxidase
This is the last enzyme in the biosynthetic pathway of fosfomycin, a broad-spectrum antibiotic produced by certain Streptomyces species.
Contains non heme iron that forms a iron(IV)-oxo (ferryl) complex with hydrogen peroxide, which functions as a proton abstractor from the substrate.
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-epoxypropylphosphonate + 2 H2O.
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins.
They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins.
The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine.
All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid).
The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes.
For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle.
In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond.
The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule.
Thioredoxin-dependent peroxiredoxins are the most common.
They have been reported from archaea, bacteria, fungi, plants, and animals.
[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O.
To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor.
Glutaredoxin-dependent peroxiredoxins have been reported from bacteria, fungi, plants, and animals.
These enzymes are often able to use an alternative reductant such as thioredoxin or glutathione.
[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-disulfide + an alcohol + H2O.
This bacterial peroxiredoxin differs from most other forms by comprising two types of subunits.
One subunit (AhpC) is a typical 2-Cys peroxiredoxin.
Following the reduction of the substrate, one AhpC subunit forms a disulfide bond with an identical unit.
The disulfide bond is reduced by the second type of subunit (AhpF).
This second subunit is a flavin-containing protein that uses electrons from NADH to reduce the cysteine residues on the AhpC subunits back to their active state.
a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+).
Glutathione-dependent peroxiredoxins have been reported from bacteria and animals, and appear to be 1-Cys enzymes.
The mechanism for the mammalian PRDX6 enzyme involves heterodimerization of the enzyme with pi-glutathione S-transferase, followed by glutathionylation of the oxidized cysteine residue.
Subsequent dissociation of the heterodimer yields glutathionylated peroxiredoxin, which is restored to the active form via spontaneous reduction by a second glutathione molecule.
a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O.
Two types of lipoyl-dependent peroxiredoxins have been reported from bacteria.
One type is the AhpC/AhpD system, originally described from Mycobacterium tuberculosis.
In that system, AhpC catalyzes reduction of the substrate, resulting in an intramolecular disulfide.
AhpD then forms an intermolecular disulfide cross-link with AhpC, reducing it back to active state.
AhpD is reduced in turn by lipoylated proteins.
The second type, which has been characterized in Xylella fastidiosa, consists of only one type of subunit, which interacts directly with lipoylated proteins.
(R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + an alcohol + H2O.
Mycoredoxin-dependent enzymes are found in Mycobacteria.
Following the reduction of the substrate, the sulfenic acid derivative of the peroxidatic cysteine forms a protein mixed disulfide with the N-terminal cysteine of mycoredoxin, which is then reduced by the C-terminal cysteine of mycoredoxin, restoring the peroxiredoxin to active state and resulting in an intra-protein disulfide in mycoredoxin.
The disulfide is eventually reduced by mycothiol.
[mycoredoxin]-L-dithiol + a hydroperoxide = [mycoredoxin]-L-disulfide + an alcohol + H2O.
With H2O2 as acceptor, one oxygen atom of which is incorporated into the product
Enzymes of this type include glycoproteins secreted by agaric basidiomycetes.
They catalyze the insertion of an oxygen atom from H2O2 into a wide variety of substrates, including aromatic rings such as naphthalene, toluene, phenanthrene, pyrene and p-nitrophenol, recalcitrant heterocycles such as pyridine, dibenzofuran, various ethers (resulting in O-dealkylation) and alkanes such as propane, hexane and cyclohexane.
Reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, O- and N-dealkylation, bromination and one-electron oxidations.
They have little or no activity toward chloride.
Mechanistically, the catalytic cycle of unspecific (mono)-peroxygenases combines elements of the 'shunt' pathway of cytochrome P450s (a side activity that utilizes a peroxide in place of dioxygen and NAD[P]H) and the classic heme peroxidase cycle.
Is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal.
It differs from EC 1.11.1.10 in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8).
Hypochlorite in turn forms a number of antimicrobial products (Cl2, chloramines, hydroxyl radical, singlet oxygen).
MPO also oxidizes bromide, iodide and thiocyanate.
In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
chloride + H(+) + H2O2 = H2O + hypochlorous acid.
A heme protein with calcium binding motif (caleosin-type).
Enzymes of this type include membrane-bound proteins found in seeds of different plants.
They catalyze the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized.
Reactions catalyzed include hydroxylation, epoxidation and sulfoxidation.
Preferred substrate and cosubstrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively.
Plant seed peroxygenase is involved in the synthesis of cutin.
A cytosolic heme-thiolate protein with sequence homology to P450 monooxygenases.
Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function.
Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis).
Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalyzed by the common P450s.
A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated.
Oxidizes the peroxidase substrate 3,3,5,5-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.
a 1,2-saturated fatty acid + H2O2 = a 2-hydroxy fatty acid + H2O.
a 2,3-saturated fatty acid + H2O2 = a 3-hydroxy fatty acid + H2O.
H2O2 + tetradecanoate = (2R)-hydroxytetradecanoate + H2O.
H2O2 + tetradecanoate = (2S)-hydroxytetradecanoate + H2O.
H2O2 + tetradecanoate = (3R)-hydroxytetradecanoate + H2O.
The heme-containing peroxygenase from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
3-methyl-L-tyrosine + H2O2 = 5-hydroxy-3-methyl-L-tyrosine + H2O.
The enzyme from the bacterium Streptomyces lincolnensis participates in the biosynthesis of the antibiotic lincomycin A, while that from Streptomyces refuineus is involved in anthramycin biosynthesis.
The enzyme, which contains a heme b cofactor, is rapidly inactivated in the presence of hydrogen peroxide, but the presence of L-tyrosine protects it.
The protein from the bacterium Desulfovibrio fructosovorans exclusively functions as a hydrogen dehydrogenase, while the enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 1.12.98.4).
The enzyme from Thermotoga maritima contains a [FeFe] cluster (H-cluster) and iron-sulfur clusters.
It works in the direction evolving hydrogen as a means of eliminating excess reducing equivalents.
2 H2 + NAD(+) + 2 oxidized [2Fe-2S]-[ferredoxin] = 3 H(+) + NADH + 2 reduced [2Fe-2S]-[ferredoxin].
The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 1.12.98.4).
Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases).
Methylene blue and other acceptors can also be reduced.
2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 H(+).
Also catalyzes the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzylviologen or methylviologen) by H2.
Can use molecular hydrogen for the reduction of a variety of substances.
H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
8-hydroxy-5-deazaflavin-reducing hydrogenase
The enzyme from some sources contains selenocysteine.
The enzyme also reduces the riboflavin analog of F420, flavins and methylviologen, but to a lesser extent.
The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n).
5,10-methenyltetrahydromethanopterin hydrogenase
H2-dependent methylene-H4MPT dehydrogenase
H2-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase
hydrogen:N(5),N(10)-methenyltetrahydromethanopterin oxidoreductase
N(5),N(10)-methenyltetrahydromethanopterin hydrogenase
Does not catalyze the reduction of artificial dyes.
Does not by itself catalyze a H2/H(+) exchange reaction.
Does not contain nickel or iron-sulfur clusters.
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2 = 5,10-methylenetetrahydromethanopterin + H(+).
H2 + methanophenazine = dihydromethanophenazine.
The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3 and EC 1.12.1.4).
Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate.
H2 + n sulfur = H(+) + hydrogen sulfide + (n-1) sulfur.
Uses molecular hydrogen for the reduction of a variety of substances.
Acting on single donors with incorporation of molecular oxygen (oxygenases). The oxygen incorporated need not be derived from O2
With incorporation of two atoms of oxygen
Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
catechol + O2 = cis,cis-muconate + 2 H(+).
The enzyme initiates the meta-cleavage pathway of catechol degradation.
catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H(+).
The enzyme, which participates in the degradation of aromatic compounds, catalyzes the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring.
The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.
3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2 H(+).
2,5-dihydroxybenzoate + O2 = 3-maleylpyruvate + H(+).
homogentisate + O2 = 4-maleylacetoacetate + H(+).
The product of the reaction spontaneously rearrange to quinolinic acid (quin).
3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde.
3,4-dihydroxybenzoate + O2 = 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+).
2,5-dihydroxypyridine + O2 = H(+) + N-formylmaleamate.
7,8-dihydroxykynurenate 8,8a-dioxygenase
7,8-dihydroxykynurenate + O2 = 5-(3-carboxy-3-oxoprop-1-en-1-yl)-4,6-dihydroxypyridine-2-carboxylate + H(+).
Catalyzes, together with EC 1.13.11.52, the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism.
Specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan.
L-tryptophan + O2 = N-formyl-L-kynurenine.
A common plant lipoxygenase that oxidizes linoleate and alpha-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C13 position with (S)-configuration.
This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid.
EC 1.13.11.58 catalyzes a similar reaction at the second available position of these fatty acids.
(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate.
(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate.
2,3-dihydroxybenzoate + O2 = 2-hydroxy-3-(3-oxoprop-1-enyl)but-2-enedioate + H(+).
3,4-dihydroxyphenylacetate 2,3-dioxygenase
3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde + H(+).
2,3-dihydroxy-beta-phenylpropionate oxygenase
3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+).
(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H(+).
Enzymes from the plants Tecoma stans, Jasminum grandiflorum and Zea mays are flavoproteins containing copper.
They are part of enzyme systems that form either anthranil (3,4-benzoisoxazole) (Tecoma stans), anthranilate (Jasminum grandiflorum) or both (Zea mays) as the final product.
A second enzyme from Tecoma stans is not a flavoprotein, does not require copper, and is part of a system that forms anthranilate as the final product.
Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme.
The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3(-)) non-enzymically.
H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) + sulfite.
Involved in the biosynthesis of taurine.
3-Aminopropanethiol (homocysteamine) and 2-sulfanylethan-1-ol (2-mercaptoethanol) can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates.
L-cysteine + O2 = 3-sulfino-L-alanine + H(+).
(E)-caffeate + O2 = 3-(2-carboxyethenyl)-cis,cis-muconate + 2 H(+).
2,3-dihydroxyindole + O2 = anthranilate + CO2 + H(+).
Quercetin is a flavonol (5,7,3',4'-tetrahydroxyflavonol).
O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO.
3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase
Also acts on 3-isopropylcatechol and 3-tert-butyl-5-methylcatechol.
[protein]-L-tryptophan + O2 = [protein]-N-formyl-L-kynurenine.
3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate.
Also acts, more slowly, with 2,3-dihydroxy-4-methylbenzoate and 2,3-dihydroxy-4-isopropylbenzoate.
2,3-dihydroxybenzoate + O2 = 2-carboxy-cis,cis-muconate + 2 H(+).
The intermediate product undergoes ring closure and oxidation, with NAD(P)(+) as acceptor, to stizolobic acid.
L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+).
The intermediate product undergoes ring closure and oxidation, with NAD(P)(+) as acceptor, to stizolobinic acid.
L-dopa + O2 = 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+).
The product is rapidly reduced to the corresponding 12S-hydroxy compound.
(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate.
The product is rapidly converted to the corresponding 15S-hydroxy compound.
(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate.
(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = H2O + leukotriene A4.
1,2,3-trihydroxybenzene + O2 = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + 2 H(+).
Involved in the breakdown of the herbicide chloridazon.
5-amino-4-chloro-2-(2,3-dihydroxyphenyl)pyridazin-3(2H)-one + O2 = 5-amino-4-chloro-2-(2-hydroxymuconoyl)pyridazin-3(2H)-one + 2 H(+).
Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.
benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate.
Involved, with EC 4.1.2.34, in the metabolism of phenanthrene in bacteria.
1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H(+).
This enzyme participates in the degradation pathway of biphenyl and PCB (poly chlorinated biphenyls), and catalyzes the first ring cleavage step by incorporating two oxygen atoms into the catechol ring formed by EC 1.3.1.56.
The enzyme from the bacterium Burkholderia xenovorans LB400 can also process catechol, 3-methylcatechol, and 4-methylcatechol, but less efficiently.
The enzyme from the carbazole-degrader Pseudomonas resinovorans strain CA10 also accepts 2'-aminobiphenyl-2,3-diol.
The enzyme from Ralstonia sp. SBUG 290 can also accept 1,2-dihydroxydibenzofuran and 1,2-dihydroxynaphthalene.
The enzyme is strongly inhibited by the substrate.
biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H(+).
An enzyme from the coral Pseudoplexaura porosa.
(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate.
2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate + 2 H(+).
The enzyme catalyzes oxidative cleavage of the interphenyl double bond in the synthetic substrate and lignin-derived stilbenes.
It is responsible for the degradation of a diarylpropane-type structure in lignin.
1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin.
The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate.
The enzyme from the fungus Gaeumannomyces graminis requires Mn(2+).
It also acts on alpha-linolenate, whereas gamma-linolenate is a poor substrate.
Oleate and arachidonate are not substrates.
(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-octadecadienoate.
Involved in the biosynthesis of the vancomycin group of glycopeptide antibiotics.
3-(4-hydroxyphenyl)pyruvate + O2 = (S)-4-hydroxymandelate + CO2.
3-hydroxy-4-oxoquinoline 2,4-dioxygenase
(1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase
3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase
Does not contain a metal center or organic cofactor.
Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide.
The enzyme from Pseudomonas putida is highly specific for this substrate.
3-hydroxy-1H-quinolin-4-one + O2 = CO + H(+) + N-formylanthranilate.
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
(1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47), but more slowly.
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = CO + H(+) + N-acetylanthranilate.
Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria.
There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite.
The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation.
Forms the first step in the acetylacetone degradation pathway of Acinetobacter johnsonii.
While acetylacetone is by far the best substrate, heptane-3,5-dione, octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can also act as substrates.
acetylacetone + O2 = acetate + H(+) + methylglyoxal.
Acts on 9-cis-violaxanthin and 9'-cis-neoxanthin but not on the all-trans isomers.
In vitro, it will cleave 9-cis-zeaxanthin.
Catalyzes the first step of abscisic-acid biosynthesis from carotenoids in chloroplasts, in response to water stress.
The other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288, EC 1.2.3.14 and EC 1.14.13.93.
a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal.
9-cis-violaxanthin + O2 = (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin.
9'-cis-neoxanthin + O2 = (3S,5R,6R)-3,5-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin.
Requires ascorbic acid and methylene blue for activity.
Has broader substrate specificity than EC 1.13.11.11.
Is induced in response to pathological conditions and host-defense mechanisms.
While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan.
Superoxide radicals can replace O2 as oxygen donor.
D-tryptophan + O2 = N-formyl-D-kynurenine.
acireductone dioxygenase (Ni(2+)-requiring)
2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase
If Fe(2+) is bound instead of Ni(2+), the reaction catalyzed by EC 1.13.11.54 occurs instead.
The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC 8724 is involved in the methionine salvage pathway.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+).
acireductone dioxygenase (Fe(2+)-requiring)
If Ni(2+) is bound instead of Fe(2+), the reaction catalyzed by EC 1.13.11.53 occurs instead.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+).
Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen.
Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between sulfite and sulfur.
This enzyme differs from EC 1.13.11.18 and EC 1.12.98.4 in that both activities occur simultaneously.
4 H2O + O2 + 4 sulfur = 6 H(+) + 2 hydrogen sulfide + 2 sulfite.
This enzyme is involved in naphthalene degradation.
naphthalene-1,2-diol + O2 = 2-hydroxychromene-2-carboxylate + H(+).
The enzyme is a ring-cleavage dioxygenase that acts specifically on gallate to produce the keto-tautomer of 4-oxalomesaconate.
3,4,5-trihydroxybenzoate + O2 = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + 2 H(+).
A common plant lipoxygenase that oxidizes linoleate and alpha-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C9 position with (S)-configuration.
The enzyme plays a physiological role during the early stages of seedling growth.
The enzyme from Arabidopsis thaliana shows comparable activity toward linoleate and linolenate.
EC 1.13.11.12 catalyzes a similar reaction at another position of these fatty acids.
(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate.
It is assumed that 3-methylbut-2-enal is formed.
The enzyme cannot cleave the saturated 3',4'-bond of gamma-carotene which implies that a 3',4'-double bond is neccessary for this reaction.
O2 + torulene = 3-methyl-2-butenal + 4'-apo-beta-carotenal.
5,8-linoleate diol synthase (bifunctional enzyme)
7,8-linoleate diol synthase (bifunctional enzyme)
The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions.
Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5).
The bifunctional enzyme from Gaeumannomyces graminis also catalyzes the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6).
(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate.
In cyanobacteria the enzyme is involved in oxylipin biosynthesis.
The enzyme also converts linoleate to (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate.
(9Z,12Z,15Z)-octadecatrienoate + O2 = (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate.
(9Z,12Z)-octadecadienoate + O2 = (9R)-hydroperoxy-(10E,12Z)-octadecadienoate.
The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergillus spp.
(9Z,12Z)-octadecadienoate + O2 = (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate.
The enzyme cleaves beta-carotene symmetrically, producing two molecules of all-trans-retinal.
Both atoms of the oxygen molecule are incorporated into the products.
The enzyme can also process beta-cryptoxanthin, 8'-apo-beta-carotenal, 4'-apo-beta-carotenal, alpha-carotene and gamma-carotene in decreasing order.
The presence of at least one unsubstituted beta-ionone ring in a substrate greater than C30 is mandatory.
A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore.
all-trans-beta-carotene + O2 = 2 all-trans-retinal.
The enzyme, characterized from the soil bacterium Bradyrhizobium sp. JS329, is involved in the pathway of 5-nitroanthranilate degradation.
It is unusual in being able to catalyze the ring fission without the requirement for prior removal of the nitro group.
The product undergoes spontaneous lactonization, with concurrent elimination of the nitro group.
5-nitrosalicylate + O2 = 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + H(+) + nitrite.
The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects.
The enzyme accepts different all-trans carotenoids, including beta-carotene, alpha-carotene and lutein, and catalyzes the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration.
When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
all-trans-zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal.
The enzyme is an extradiol-type dioxygenase, and is a member of the nonheme-iron(II)-dependent dioxygenase family.
It catalyzes the ring cleavage of a wide range of hydroquinone substrates to produce the corresponding 4-hydroxymuconic semialdehydes.
hydroquinone + O2 = (2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate + H(+).
8'-apo-beta-carotenoid 14',13'-cleaving dioxygenase
Unlike EC 1.13.11.63, it is not active toward beta-carotene.
The secondary product has not been characterized, but may be (3E,5E)-7-hydroxy-6-methylhepta-3,5-dien-2-one.
8'-apo-beta-carotenol + O2 = (3E,5E)-7-hydroxy-6-methylhepta-3,5-dienal + 14'-apo-beta-carotenal.
9-cis-beta-carotene 9',10'-cleaving dioxygenase
The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza.
9-cis-beta-carotene + O2 = 9-cis-10'-apo-beta-carotenal + beta-ionone.
Also catalyzes EC 1.13.11.70, but 10-fold slower.
9-cis-10'-apo-beta-carotenal + 2 O2 = (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal + carlactone.
all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase
The enzyme from the plant Arabidopsis thaliana also catalyzes EC 1.13.11.69, 10-fold faster.
all-trans-10'-apo-beta-carotenal + O2 = (2E,4E,6E)-4-methylocta-2,4,6-trienedial + 13-apo-beta-carotenone.
The enzyme catalyzes the asymmetric oxidative cleavage of carotenoids.
The mammalian enzyme can also cleave all-trans-lycopene.
all-trans-beta-carotene + O2 = all-trans-10'-apo-beta-carotenal + beta-ionone.
Isolated from some bacteria including Streptomyces hygroscopicus and Streptomyces viridochromogenes.
The pro-R hydrogen at C-2 of the ethyl group is retained by the formate ion.
Any stereochemistry at C-1 of the ethyl group is lost.
One atom from dioxygen is present in each product.
Involved in phosphinothricin biosynthesis.
2-hydroxyethylphosphonate + O2 = formate + H(+) + hydroxymethylphosphonate.
Isolated from the marine archaeon Nitrosopumilus maritimus.
2-hydroxyethylphosphonate + O2 = H(+) + hydrogencarbonate + methylphosphonate.
The enzyme, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent).
The enzyme also has some activity with 2-amino-5-methylphenol and 2-amino-4-methylphenol.
The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.76.
2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde.
all-trans-8'-apo-beta-carotenal 15,15'-oxygenase
The enzyme is involved in retinal biosynthesis in bacteria.
all-trans-8'-apo-beta-carotenal + O2 = (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial + all-trans-retinal.
The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent).
The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.3.1.74.
2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde.
The enzyme isolated from the bacterium Pseudomonas sp. 42A2 has similar activity with all the three Delta(9) fatty acids (cf. EC 1.13.11.62).
(9Z)-octadecenoate + O2 = (8E,10S)-10-hydroperoxy-octadeca-8-enoate.
(9Z,12Z)-octadecadienoate + O2 = (8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate.
(9Z,12Z,15Z)-octadecatrienoate + O2 = (8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate.
2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)
The enzyme, characterized from a marine bacterium, is involved in a 2-aminoethylphosphonate degradation pathway.
(1R)-(2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + 2 H(+) + phosphate.
aerobic 5,6-dimethylbenzimidazole synthase
The enzyme catalyzes a complex oxygen-dependent conversion of reduced flavin mononucleotide to form 5,6-dimethylbenzimidazole, the lower ligand of vitamin B12.
This conversion involves many sequential steps in two distinct stages, and an alloxan intermediate that acts as a proton donor, a proton acceptor, and a hydride acceptor.
The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen.
While D-erythrose 4-phosphate has been shown to be one of the by-products, the nature of the other product(s) has not been verified yet.
FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + dialurate + H(+).
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin.
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA + H(+).
The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyzes the epimerisation of the 2'-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8) and the reaction of EC 4.1.2.25.
7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde + H(+).
8'-apo-carotenoid 13,14-cleaving dioxygenase
Isolated from the bacterium Novosphingobium aromaticivorans.
It is less active with 4'-apo-beta-carotenal and gamma-carotene.
all-trans-8'-apo-beta-carotenal + O2 = 13-apo-beta-carotenone + 2,6-dimethyldeca-2,4,6,8-tetraenedial.
4-hydroxy-3-prenylphenylpyruvate oxygenase
Isolated from the bacterium Streptomyces roseochromogenes DS 12976.
A bifunctional enzyme involved in clorobiocin biosynthesis that also catalyzes the activity of EC 1.13.12.23.
3-dimethylallyl-4-hydroxyphenylpyruvate + O2 = 3-dimethylallyl-4-hydroxymandelate + CO2.
The enzyme, characterized from the plant Crocus sativus (saffron), acts twice, cleaving 3beta-hydroxy-beta-cyclocitral off each 3-hydroxy end group.
It is part of the zeaxanthin degradation pathway in that plant, leading to the different compounds that impart the color, flavor and aroma of the saffron spice.
The enzyme can similarly cleave the 7-8 double bond of other carotenoids with a 3-hydroxy-beta-carotenoid end group.
all-trans-zeaxanthin + 2 O2 = 2 3beta-hydroxy-beta-cyclocitral + crocetin dialdehyde.
The enzyme, studied mainly from the bacterium Xanthomonas sp. 35Y, catalyzes the cleavage of the double bonds in natural and synthetic rubber (cis-1,4-polyisoprene polymers), generating ends that contain ketone and aldehyde groups.
The enzyme from Xanthomonas sp. 35Y contains two c-type cytochromes.
It attacks the substrate from its end, producing a single product of 15 carbons.
[cis-1,4-isoprene](n) + O2 = (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal + cis-1,4-isoprene(n-3).
The enzyme, characterized from different bacteria, is a nonheme iron dioxygenase in the bicupin family.
5-amino-2-hydroxybenzoate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate + H(+).
The enzyme catalyzes the cleavage of the double bonds in natural and synthetic rubber, producing a mixture of C20, C25, C30, and higher oligo-isoprenoids with ketone and aldehyde groups at their ends.
Two unrelated bacterial enzymes are known to possess this activity - the enzyme from Streptomyces sp. K30 (Lcp) contains a b-type cytochrome, while the enzyme from Xanthomonas sp. 35Y, (RoxB) contains two c-type cytochromes.
Both enzymes attack the substrate at random locations, and are not able to cleave the C35 or smaller products into shorter fragments.
Cleavage of cis-1,4-polyisoprene polymers into a mixture of compounds, including a C20 compound ((4Z,8Z,12Z,16Z,20Z,24Z)-4,8,12,16,20,24-hexamethyl-28-oxononacosa-4,8,12,16,20,24-hexaenal), a C25 compound ((4Z,8Z,12Z,16Z,20Z)-4,8,12,16,20-pentamethyl-24-oxopentacosa-4,8,12,16,20-pentaenal), a C30 compound ((4Z,8Z,12Z,16Z)-4,8,12,16-tetramethyl-20-oxohenicosa-4,8,12,16-tetraenal), and higher molecular weight compounds.
The enzyme, charcterised from the bacteria Pseudomonas putida and Pseudomonas nitroreducens, catalyzes the epoxidation of the double bond in the side chain of isoeugenol, followed by a second oxygenation and cleavage of the side chain in the form of acetaldehyde.
O2 + trans-isoeugenol = acetaldehyde + vanillin.
The enzyme, characterized from the marine bacterium Gimesia maris, participates in a (methyl)phosphonate degradation pathway.
It also has the activity of EC 1.13.11.78.
hydroxymethylphosphonate + O2 = formate + 2 H(+) + phosphate.
[1-hydroxy-2-(trimethylamino)ethyl]phosphonate dioxygenase (glycine-betaine-forming)
This bacterial enzyme is involved in a degradation pathway for [(2-trimethylamino)ethyl]phosphonate.
[(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate + O2 = glycine betaine + 2 H(+) + phosphate.
This bacterial enzyme contains an iron(2+) atom coordinated by three protein-derived histidines and a Ser-His-Tyr motif.
It is similar to EC 1.13.11.20 and can act on L-cysteine, but has a much higher activity with its native substrate, 3-sulfanylpropanoate.
3-sulfanylpropanoate + O2 = 3-sulfinopropanoate + H(+).
This plant enzyme catalyzes the (2R)-hydroperoxidation of fatty acids.
It differs from lipoxygenases and cyclooxygenases in that the oxygen addition does not target an unsaturated region in the fatty acid.
In vitro the product undergoes spontaneous decarboxylation, resulting in formation of a chain-shortened aldehyde.
In vivo the product may be reduced to a (2R)-2-hydroxyfatty acid.
The enzyme, which is involved in responses to different abiotic and biotic stresses, has a wide substrate range that includes both saturated and unsaturated fatty acids.
a 1,2-saturated fatty acid + O2 = a (2R)-2-hydroperoxy fatty acid.
(9Z,12Z,15Z)-octadecatrienoate + O2 = (R)-2-hydroperoxy-(9Z,12Z,15Z)-octadecatrienoate.
hexadecanoate + O2 = (2R)-2-hydroperoxyhexadecanoate.
dodecanoate + O2 = (2R)-2-hydroperoxydodecanoate.
O2 + tetradecanoate = (2R)-2-hydroperoxytetradecanoate.
(9Z,12Z)-octadecadienoate + O2 = (2R,9Z,12Z)-2-hydroperoxyoctadecadienoate.
O2 + octadecanoate = (2R)-2-hydroperoxyoctadecanoate.
(9Z)-octadecenoate + O2 = (2R,9Z)-2-hydroperoxyoctadecenoate.
With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)
Also acts on canavanine and homoarginine.
L-arginine + O2 = 4-guanidinobutanamide + CO2 + H2O.
L-lysine + O2 = 5-aminopentanamide + CO2 + H2O.
L-tryptophan + O2 = CO2 + H2O + indole-3-acetamide.
This enzyme has been studied from the soft coral Renilla reniformis.
Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein.
Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase.
Upon binding the substrate, the enzyme catalyzes an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule.
The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion.
In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence.
In vitro, in the absence of GFP, the product emits blue light.
coelenterazine h + O2 = CO2 + excited coelenteramide h monoanion + H(+) + hnu.
Cypridina luciferin is a bioluminescent crustacea.
The enzyme may be assayed by measurement of light emission.
Cypridina luciferin + O2 = CO2 + hnu + oxidized Cypridina luciferin.
Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)
The enzyme, which is found in fireflies (Lampyridae), is responsible for their biolouminescence.
The reaction begins with the formation of an acid anhydride between the carboxylic group of D-firefly luciferin and AMP, with the release of diphosphate.
An oxygenation follows, with release of the AMP group and formation of a very short-lived peroxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule.
The spontaneous breakdown of the dioxetanone (rather than the hydrolysis of the adenylate) releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of oxyluciferin.
The excited luciferin then emits a photon, returning to its ground state.
The enzyme has a secondary acyl-CoA ligase activity when acting on L-firefly luciferin.
ATP + firefly D-luciferin + O2 = AMP + CO2 + diphosphate + firefly oxyluciferin + hnu.
O2 + Watasenia luciferin = CO2 + hnu + oxidized Watasenia luciferin.
L-phenylalanine oxidase (deaminating and decarboxylating)
phenylalanine (deaminating, decarboxylating) oxidase
The reaction shown above is about 80% of the reaction catalyzed; the remaining 20% is: L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid + NH3 + H2O2, a reaction similar to that of EC 1.4.3.2.
L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O.
The luciferase from the deep sea shrimp Oplophorus gracilirostris is a complex composed of more than one protein.
The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates.
coelenterazine + O2 = CO2 + coelenteramide + hnu.
3,4-dihydroxyphenylalanine oxidative deaminase
One of the three enzymes involved in L-dopa (3,4-dihydroxyphenylalanine) catabolism in the non-oxygenic phototrophic bacterium Rubrivivax benzoatilyticus OU5 (and not Rhodobacter sphaeroides OU5 as had been thought), the other two being EC 4.3.1.22 and EC 2.6.1.49.
In addition to DOPA, the enzyme can also use L-tyrosine, L-phenylalanine, L-tryptophan and glutamate as substrate, but more slowly.
2 L-dopa + O2 = 2 3-(3,4-dihydroxyphenyl)pyruvate + 2 NH4(+).
Previously classified as EC 1.13.11.32, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms.
The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor.
Neither hydrogen peroxide nor superoxide were detected during enzyme turnover.
Active toward linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, toward propyl-2-nitronate.
The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity.
ethylnitronate + O2 = acetaldehyde + chemical entity + H(+) + nitrite.
The conversion of dichlorochromopyrrolate to dichloroarcyriaflavin A is a complex process that involves two enzyme components.
RebP is an NAD-dependent cytochrome P450 oxygenase that performs an aryl-aryl bond formation yielding the six-ring indolocarbazole scaffold.
Along with RebC, a flavin-dependent hydroxylase, it also catalyzes the oxidative decarboxylation of both carboxyl groups.
The presence of RebC ensures that the only product is the rebeccamycin aglycone dichloroarcyriaflavin A.
The enzymes are similar, but not identical, to StaP and StaC, which are involved in the synthesis of staurosporine.
dichlorochromopyrrolate + 6 H(+) + 4 NADH + 4 O2 = 2 CO2 + dichloroarcyriaflavin A + 6 H2O + 4 NAD(+).
A luciferase from dinoflagelates such as Gonyaulax polyhedra, Lingulodinium polyedrum, Noctiluca scintillans, and Pyrocystis lunula.
It is a single protein with three luciferase domains.
The luciferin is strongly bound by a luciferin binding protein above a pH of 7.
dinoflagellate luciferin + O2 = H(+) + H2O + hnu + oxidized dinoflagellate luciferin.
2-oxoglutarate dioxygenase (ethylene-forming)
This is one of two simultaneous reactions catalyzed by the enzyme, which is responsible for ethylene production in bacteria of the Pseudomonas syringae group.
In the other reaction (EC 1.14.11.34) the enzyme catalyzes the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and L-hydroxyarginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate.
The enzymes catalyze two cycles of the ethylene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethylene and succinate is 2:1.
2-oxoglutarate + 2 H(+) + O2 = 3 CO2 + ethene + H2O.
noranthrone + O2 = H2O + norsolorinic acid.
The enzyme is involved in biosynthesis of the anthracycline antibiotic tetracenomycin C by the bacterium Streptomyces glaucescens.
O2 + tetracenomycin F1 = H(+) + H2O + tetracenomycin D3.
The enzyme, characterized from the bacterium Streptomyces nogalater, is involved in the biosynthesis of the aromatic polyketide nogalamycin.
deoxynogalonate + O2 = H(+) + H2O + nogalonate.
A bifunctional enzyme involved in clorobiocin biosynthesis that also catalyzes the activity of EC 1.13.11.83.
3-dimethylallyl-4-hydroxymandelate + O2 = 3-dimethylallyl-4-hydroxybenzoate + CO2 + H2O.
Ca(2+)-regulated photoproteins are found in a variety of bioluminescent marine organisms, mostly coelenterates, and are responsible for their light emission.
The best studied enzyme is from the jellyfish Aequorea victoria.
The enzyme tightly binds the imidazolopyrazinone derivative coelenterazine, which is then peroxidized by oxygen.
The hydroperoxide is stably bound until three Ca(2+) ions bind to the protein, inducing a structural change that results in the formation of a 1,2-dioxetan-3-one ring, followed by decarboxylation and generation of a protein-bound coelenteramide in an excited state.
The calcium-bound protein-product complex is known as a blue fluorescent protein.
In vivo the energy is transferred to a green fluorescent protein (GFP) by Foerster resonance energy transfer.
In vitro, in the absence of GFP, coelenteramide emits a photon of blue light while returning to its ground state.
apo-[aequorin] + 3 Ca(2+) + coelenterazine + O2 = [excited state blue fluorescent protein] + CO2.
myo-inositol + O2 = D-glucuronate + H(+) + H2O.
tryptophan side-chain alpha,beta-oxidase
Acts on a number of indole-3-alkane derivatives, oxidizing the 3-side-chain in the 2'-position.
Best substrates are L-tryptophan and 5-hydroxy-L-tryptophan.
H(+) + L-tryptophan + O2 = 3-indoleglycolaldehyde + CO2 + NH4(+).
Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
gamma-butyrobetaine,2-oxoglutarate dioxygenase
2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate.
The enzyme, which is located within the lumen of the endoplasmic reticulum, catalyzes the 4-hydroxylation of prolines in -X-Pro-Gly- sequences.
The 4-hydroxyproline residues are essential for the formation of the collagen triple helix.
The enzyme forms a complex with protein disulfide isomerase and acts not only on procollagen but also on more than 15 other proteins that have collagen-like domains.
2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen].
pyrimidine-deoxynucleoside 2'-dioxygenase
pyrimidine-deoxynucleoside,2-oxoglutarate 2'-dioxygenase
pyrimidine deoxyribonucleoside 2'-hydroxylase
Also acts on thymidine (cf. EC 1.14.11.10).
2'-deoxyuridine + 2-oxoglutarate + O2 = CO2 + succinate + uridine.
procollagen-lysine,2-oxoglutarate 5-dioxygenase
2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate.
Also acts on 5-hydroxymethyluracil to oxidize its -CH2-OH group first to -CHO and then to -COOH.
2-oxoglutarate + O2 + thymine = 5-hydroxymethyluracil + CO2 + succinate.
procollagen-proline,2-oxoglutarate 3-dioxygenase
The enzyme forms a complex with protein disulfide isomerase, and is located in the endoplasmic reticulum.
It modifies proline residues within the procollagen peptide of certain collagen types.
The modification is essential for proper collagen triple helix formation.
2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-3-hydroxy-L-prolyl-[collagen].
epsilon-trimethyllysine 2-oxoglutarate dioxygenase
trimethyllysine,2-oxoglutarate dioxygenase
trimethyllysine alpha-ketoglutarate dioxygenase
2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate.
This plant enzyme catalyzes an early step in the flavonoid biosynthesis pathway, leading to the production of flavanols and anthocyanins.
Substrates include (2S)-naringenin, (2S)-eriodictyol, (2S)-dihydrotricetin and (2S)-pinocembrin.
Some enzymes are bifuctional and also catalyze EC 1.14.20.6.
2-oxoglutarate + a (2S)-flavan-4-one + O2 = a (2R,3R)-dihydroflavonol + CO2 + succinate.
pyrimidine-deoxynucleoside 1'-dioxygenase
pyrimidine-deoxynucleoside,2-oxoglutarate 1'-dioxygenase
2'-deoxyuridine + 2-oxoglutarate + O2 = 2-deoxy-D-ribono-1,4-lactone + CO2 + succinate + uracil.
2-oxoglutarate + L-hyoscyamine + O2 = (6S)-6-hydroxyhyoscyamine + CO2 + succinate.
2-oxoglutarate + gibberellin A44 + O2 = CO2 + gibberellin A19 + H2O + succinate.
Also acts on a number of other gibberellins.
2-oxoglutarate + gibberellin A1 + O2 = CO2 + gibberellin A8 + succinate.
2-oxoglutarate + gibberellin A20 + O2 = CO2 + gibberellin A1 + succinate.
Some vitamin K-dependent coagulation factors, as well as synthetic peptides based on the structure of the first epidermal growth factor domain of human coagulation factor IX or X, can act as acceptors.
2-oxoglutarate + L-aspartyl-[protein] + O2 = 3-hydroxy-L-aspartyl-[protein] + CO2 + succinate.
alpha-ketoglutarate-dependent taurine dioxygenase
The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.
2-oxoglutarate + O2 + taurine = aminoacetaldehyde + CO2 + H(+) + succinate + sulfite.
phytanoyl-CoA 2 oxoglutarate dioxygenase
Part of the peroxisomal phytanic acid alpha-oxidation pathway.
2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate.
desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4beta-hydroxylating)
Also acts, to a lesser extent, on 16-methoxy-2,3-dihydrotabersonine.
2-oxoglutarate + deacetoxyvindoline + O2 = 4-O-deacetylvindoline + CO2 + succinate.
(3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + 2-oxoglutarate + O2 = 4-O-deacetyl-16-O-demethylvindoline + CO2 + succinate.
Catalyzes three separate oxidative reactions in the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus.
The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC 3.5.3.22.
The three reactions are all catalyzed at the same nonheme iron site.
2-oxoglutarate + deoxyamidinoproclavaminate + O2 = amidinoproclavaminate + CO2 + succinate.
2-oxoglutarate + O2 + proclavaminate = CO2 + dihydroclavaminate + H2O + succinate.
2-oxoglutarate + dihydroclavaminate + O2 = clavaminate + CO2 + H2O + succinate.
It is also likely that this enzyme can catalyze the hydroxylation of 3-epihydroxy-2'-deoxymugineic acid to form 3-epihydroxymugineic acid.
2'-deoxymugineate + 2-oxoglutarate + O2 = CO2 + mugineate + succinate.
2-oxoglutarate + mugineate + O2 = 3-epihydroxymugineate + CO2 + H(+) + succinate.
2'-deoxymugineate + 2-oxoglutarate + O2 = 3-epihydroxy-2'-deoxymugineate + CO2 + H(+) + succinate.
The enzyme can also use 3-exomethylenecephalosporin C as a substrate to form deacetoxycephalosporin C, although more slowly.
In Acremonium chrysogenum, the enzyme forms part of a bifunctional protein along with EC 1.14.20.1.
It is a separate enzyme in Streptomyces clavuligerus.
2-oxoglutarate + deacetoxycephalosporin C + O2 = CO2 + deacetylcephalosporin C + succinate.
[histone H3]-dimethyl-L-lysine(36) demethylase
JmjC domain-containing histone demethylase 1A
Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys(36).
Lysine residues exist in three methylation states (mono-, di- and trimethylated).
The enzyme preferentially demethylates the dimethyl form of Lys(36) (K36me2), which is its natural substrate, to form the monomethylated and unmethylated forms of Lys(36).
It can also demethylate monomethylated (but not the trimethylated) Lys(36), cf. EC 1.14.11.69.
2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate.
Unlike the proline hydroxylases involved in collagen biosynthesis (EC 1.14.11.2 and EC 1.14.11.7), this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme.
The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates.
2-oxoglutarate + L-proline + O2 = cis-3-hydroxy-L-proline + CO2 + succinate.
hypoxia-inducible factor-proline dioxygenase
Specifically hydroxylates a proline residue in HIF-alpha, the alpha subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which targets HIF for proteasomal destruction.
The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.
2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-inducible factor alpha subunit].
hypoxia-inducible factor-asparagine dioxygenase
Catalyzes hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-alpha, the alpha subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which reduces its interaction with the transcriptional coactivator protein p300.
2-oxoglutarate + L-asparaginyl-[hypoxia-inducible factor alpha subunit] + O2 = (3S)-3-hydroxy-L-asparaginyl-[hypoxia-inducible factor alpha subunit] + CO2 + succinate.
Catalyzes a step in morphine biosynthesis.
The product neopinione spontaneously rearranges to the more stable codeinone.
The enzyme also catalyzes the 6-O-demethylation of oripavine to morphinone, with lower efficiency.
2-oxoglutarate + O2 + thebaine = CO2 + formaldehyde + neopinone + succinate.
The enzyme also catalyzes the 3-O-demethylation of thebaine to oripavine, with lower efficiency.
2-oxoglutarate + codeine + O2 = CO2 + formaldehyde + morphine + succinate.
Activity is slightly stimulated by ascorbate.
Catalyzes oxidative demethylation of the DNA base lesions N(1)-methyladenine, N(3)-methylcytosine, N(1)-methylguanine, and N(3)-methylthymine.
It works better on single-stranded DNA (ssDNA) and is capable of repairing damaged bases in RNA.
2-oxoglutarate + a methylated nucleobase within DNA + O2 = a nucleobase within DNA + CO2 + formaldehyde + succinate.
1-deoxypentalenic acid 11beta-hydroxylase
Isolated from the bacterium Streptomyces avermitilis.
1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + CO2 + succinate.
Isolated from the bacteria Streptomyces exfoliatus, Streptomyces arenae and Streptomyces avermitilis.
Part of the pentalenolactone biosynthesis pathway.
2 2-oxoglutarate + 2 O2 + pentalenolactone D = 2 CO2 + H2O + pentalenolactone F + 2 succinate.
Found in the bacterium Streptomyces kanamyceticus where it is involved in the conversion of the aminoglycoside antibiotic kanamycin B to kanamycin A.
2-oxoglutarate + kanamycin B + O2 = 2'-dehydrokanamycin A + CO2 + NH4(+) + succinate.
Found in the fungus Aspergillus fumigatus.
Both atoms of a dioxygen molecule are incorporated into verruculogen.
Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgin A.
2-oxoglutarate + AH2 + fumitremorgin B + 2 O2 = A + CO2 + H2O + succinate + verruculogen.
The enzyme is only able to hydroxylate free L-asparagine.
The beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone.
2-oxoglutarate + L-asparagine + O2 = (2S,3S)-3-hydroxyasparagine + CO2 + succinate.
The enzyme is involved in biosynthesis of the nonproteinogenic amino acid beta-hydroxyenduracididine, a component of the mannopeptimycins (cyclic glycopeptide antibiotic), produced by Streptomyces hygroscopicus NRRL 30439.
2-oxoglutarate + L-enduracididine + O2 = (3S)-3-hydroxy-L-enduracididine + CO2 + succinate.
The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin.
It differs from EC 1.14.20.7, because it does not form guanidine and (S)-1-pyrroline-5-carboxylate from 3-hydroxy-L-arginine.
2-oxoglutarate + L-arginine + O2 = (2S,3S)-hydroxyarginine + CO2 + succinate.
tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase
The enzyme is not active with wybutosine.
2-oxoglutarate + 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37) in tRNA(Phe) + CO2 + succinate.
(S)-dichlorprop dioxygenase (2-oxoglutarate)
2-oxoglutarate-dependent (S)-dichlorprop dioxygenase
2-oxoglutarate-dependent (S)-mecoprop dioxygenase
alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase
The enzymes from the Gram-negative bacteria Delftia acidovorans MC1 and Sphingomonas herbicidovorans MH are involved in the degradation of the (S)-enantiomer of the phenoxyalkanoic acid herbicides mecoprop and dichlorprop.
(S)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 2-methyl-4-chlorophenol + CO2 + pyruvate + succinate.
(S)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + CO2 + pyruvate + succinate.
(R)-dichlorprop dioxygenase (2-oxoglutarate)
2-oxoglutarate-dependent (R)-dichlorprop dioxygenase
2-oxoglutarate-dependent (R)-mecoprop dioxygenase
alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase
The enzymes from the Gram-negative bacteria Delftia acidovorans MC1 and Sphingomonas herbicidovorans MH are involved in the degradation of the (R)-enantiomer of the phenoxyalkanoic acid herbicides mecoprop and dichlorprop.
(R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O2 = 2-methyl-4-chlorophenol + CO2 + pyruvate + succinate.
(R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + CO2 + pyruvate + succinate.
The enzyme, characterized from the bacterium Bacillus thuringiensis, can also catalyze the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine.
2-oxoglutarate + L-isoleucine + O2 = (4S)-4-hydroxy-L-isoleucine + CO2 + succinate.
The enzyme, characterized from an uncultured marine bacterium, is involved in a (2-aminoethyl)phosphonate degradation pathway.
(2-aminoethyl)phosphonate + 2-oxoglutarate + O2 = (1R)-(2-amino-1-hydroxyethyl)phosphonate + CO2 + succinate.
[50S ribosomal protein L16]-arginine 3-hydroxylase
The enzyme, characterized from the bacterium Escherichia coli, hydroxylates an arginine residue on the 50S ribosomal protein L16, and is involved in regulation of bacterial ribosome assembly.
2-oxoglutarate + L-arginyl-[ribosomal protein uL16] + O2 = (3R)-3-hydroxy-L-arginyl-[ribosomal protein uL16] + CO2 + succinate.
alpha-ketoglutarate-dependent xanthine hydroxylase
The enzyme, which was characterized from fungi, is specific for xanthine.
2-oxoglutarate + O2 + xanthine = CO2 + succinate + urate.
The enzyme catalyzes a net dephosphorylation and oxidation of UMP to generate 5'-dehydrouridine, the first intermediate in the biosynthesis of the unusual aminoribosyl moiety found in several C(7)-furanosyl nucleosides such as A-90289s, caprazamycins, liposidomycins, muraymycins and FR-900453.
2-oxoglutarate + O2 + UMP = CO2 + phosphate + succinate + uridine-5'-aldehyde.
Catalyzes oxidative demethylation of DNA N(6)-methyladenine, a prevalent modification in LINE-1 transposons, which are specifically enriched on the human X chromosome.
2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2 = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate.
The enzyme was characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus.
2-oxoglutarate + O2 + validamycin A = CO2 + H(+) + succinate + validamycin B.
Catalyzes oxidative demethylation of mRNA N(6)-methyladenine.
The FTO enzyme from human can also demethylate N(3)-methylthymine from single stranded DNA and N(3)-methyluridine from single stranded RNA with low activity.
2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate.
Catalyzes oxidative demethylation of mRNA N(1)-methyladenine.
The enzyme is also involved in alkylation repair in DNA.
2-oxoglutarate + an N(1)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate.
The enzyme, found in bacteria, is specific for ectoine.
2-oxoglutarate + L-ectoine + O2 = 5-hydroxyectoine + CO2 + succinate.
The enzyme, isolated from Rhizobium species, only produces cis-4-hydroxy-L-proline (cf. EC 1.14.11.57).
2-oxoglutarate + L-proline + O2 = cis-4-hydroxy-L-proline + CO2 + succinate.
The enzyme, isolated from multiple bacterial species, only produces trans-4-hydroxy-L-proline (cf. EC 1.14.11.56).
2-oxoglutarate + L-proline + O2 = CO2 + succinate + trans-4-hydroxy-L-proline.
ornithine lipid ester-linked acyl 2-hydroxylase
The enzyme, characterized from the bacterium Rhizobium tropici, catalyzes the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid.
2-oxoglutarate + an N(2)-[(3R)-3-(2-saturated-acyloxy)acyl]-L-ornithine lipid + O2 = a 2-hydroxyornithine lipid + CO2 + succinate.
2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poacea (grasses).
2-oxoglutarate + DIBOA beta-D-glucoside + O2 = CO2 + succinate + TRIBOA beta-D-glucoside.
A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
2-oxoglutarate + O2 + scopoletin = CO2 + fraxetin + succinate.
The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process.
The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA.
(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-hydroxyferuloyl-CoA + CO2 + succinate.
The product spontaneously undergoes trans-cis isomerization followed by lactonization and cyclization, liberating CoA and forming umbelliferone.
The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-feruloyl-CoA (cf. EC 1.14.11.61).
(E)-4-coumaroyl-CoA + 2-oxoglutarate + O2 = (E)-2,4-dihydroxycinnamoyl-CoA + CO2 + succinate.
The enzyme acts on specific lysine residues in its substrates, and is stereo-specific.
The enzyme encoded by the human JMJD7 gene acts specifically on two related members of the translation factor family of GTPases, DRG1 and DRG2.
2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-lysyl-[protein] + CO2 + succinate.
The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, participates in L-lysine degradation in many bacteria.
It provides an alternative route for L-glutarate degradation that does not proceed via CoA-activated intermediates.
2-oxoglutarate + glutarate + O2 = (S)-2-hydroxyglutarate + CO2 + succinate.
[histone H3]-dimethyl-L-lysine(9) demethylase
This entry describes a group of enzymes that demethylate N-methylated Lys-9 residues in the tail of the histone protein H3 (H3K9).
This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the di- and mono-methylated forms.
The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde, cf. EC 1.14.11.66.
2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2 succinate.
[histone H3]-trimethyl-L-lysine(9) demethylase
This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the tri- and di-methylated forms.
The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde, cf. EC 1.14.11.65.
2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate.
[histone H3]-trimethyl-L-lysine(4) demethylase
This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4).
The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde.
They can act on tri-, di-, and mono-methylated forms.
3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone H3] + 3 succinate.
[histone H3]-trimethyl-L-lysine(27) demethylase
This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 27 of histone H3 (H3K27).
They can act on tri- and di-methylated forms, but have no activity with the mono-methylated form.
2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate.
[histone H3]-trimethyl-L-lysine(36) demethylase
This entry describes a group of enzymes that demethylate N-methylated Lys(36) residues in the tail of the histone protein H3 (H3K36).
Since trimethylation of H3K36 enhances transcription, this enzyme acts as a transcription repressor.
The enzymes that possess this activity often also catalyze the activity of EC 1.14.11.66, cf. EC 1.14.11.27.
2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(36)-[histone H3] + 2 succinate.
The enzyme, found in some cyanobacterial species, catalyzes the last step in the biosynthesis of the toxins cylindrospermopsin and 7-epi-cylindrospermopsin.
The ratio of the two products differs among different strains.
2-oxoglutarate + 7-deoxycylindrospermopsin + O2 = CO2 + cylindrospermopsin + succinate.
2-oxoglutarate + 7-deoxycylindrospermopsin + O2 = 7-epi-cylindrospermopsin + CO2 + succinate.
The enzyme, characterized from the marine bacterium Gimesia maris, participates in a methylphosphonate degradation pathway.
2-oxoglutarate + methylphosphonate + O2 = CO2 + hydroxymethylphosphonate + succinate.
[2-(trimethylamino)ethyl]phosphonate dioxygenase
The enzyme, found in bacteria, participates in a degradation pathway for [2-(trimethylamino)ethyl]phosphonate.
2-oxoglutarate + [2-(trimethylamino)ethyl]phosphonate + O2 = [(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate + CO2 + succinate.
The enzyme, characterized from humans, catalyzes the stereoselective formation of the (2S,3R)-hydroxy-L-arginine stereoisomer.
So far the enzyme has been shown to act on two substrates - the 40S ribosomal protein S6 (RPS6), which is hydroxylated at R137, and, at a lower activity, RCCD1, a protein involved in chromatin stability, which is hydroxylated at R141.
Even though the same stereoisomer is produced by the bacterial EC 1.14.11.47, the two enzymes do not exhibit any cross-reactivity on their respective ribosomal protein substrates.
2-oxoglutarate + L-arginyl-[protein] + O2 = (3R)-3-hydroxy-L-arginyl-[protein] + CO2 + succinate.
The enzyme has been characterized from the bacterium Pantoea ananatis.
2-oxoglutarate + L-isoleucine + O2 = 3(1)-hydroxy-L-isoleucine + CO2 + succinate.
2-oxoglutarate + 3(1)-hydroxy-L-isoleucine + O2 = (4S)-3(1),4-dihydroxy-L-isoleucine + CO2 + succinate.
The enzyme, characterized from the basidiomycete mushroom Amanita muscaria, participates in the biosynthesis of the psychoactive compounds ibotenate and muscimol.
2-oxoglutarate + L-glutamate + O2 = (3R)-3-hydroxy-L-glutamate + CO2 + succinate.
2-oxoglutarate-dependent sulfate ester dioxygenase
alpha-ketoglutarate-dependent sulfate ester dioxygenase
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors.
The type II sulfatases oxidize the C-H bond of the carbon next to the sulfate ester, using 2-oxoglutarate and oxygen as substrates.
The resulting hemiacetal sulfate ester collapses, liberating inorganic sulfate and an alkyl aldehyde along with carbon dioxide and succinate.
The enzymes often desulfate a broad spectrum of linear and branched-chain sulfate esters.
The enzyme from Pseudomonas putida acts on a range of medium-chain alkyl sulfate esters, with chain lengths ranging from C4 to C12.
cf. EC 3.1.6.1, EC 3.1.6.21, EC 3.1.6.22, and linear primary-alkylsulfatase.
2-oxoglutarate + a primary linear alkyl sulfate ester + O2 = an aldehyde + CO2 + H(+) + succinate + sulfate.
2-oxoglutarate + butyl sulfate + O2 = butanal + CO2 + H(+) + succinate + sulfate.
2-oxoglutarate + O2 + pentyl sulfate = CO2 + H(+) + pentanal + succinate + sulfate.
2-oxoglutarate + hexyl sulfate + O2 = CO2 + H(+) + hexanal + succinate + sulfate.
2-oxoglutarate + heptyl sulfate + O2 = CO2 + H(+) + heptanal + succinate + sulfate.
2-oxoglutarate + O2 + octyl sulfate = CO2 + H(+) + octanal + succinate + sulfate.
2-oxoglutarate + nonyl sufate + O2 = CO2 + H(+) + nonanal + succinate + sulfate.
2-oxoglutarate + decyl sulfate + O2 = CO2 + decanal + H(+) + succinate + sulfate.
2-oxoglutarate + dodecyl sulfate + O2 = CO2 + dodecanal + H(+) + succinate + sulfate.
2-ethylhexyl sulfate + 2-oxoglutarate + O2 = 2-ethylhexanal + CO2 + H(+) + succinate + sulfate.
Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC).
Might initiate a process leading to cytosine demethylation through deamination into 5-hydroxymethyluracil (5hmU) and subsequent replacement by unmethylated cytosine by the base excision repair system.
Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation.
2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate.
2-oxoglutarate + L-histidyl-[ankyrin-repeat domain protein] + O2 = (3S)-3-hydroxy-L-histidyl-[ankyrin-repeat domain protein] + CO2 + succinate.
2-oxoglutarate + L-asparaginyl-[ankyrin-repeat domain protein] + O2 = (3S)-3-hydroxy-L-asparaginyl-[ankyrin-repeat domain protein] + CO2 + succinate.
2-oxoglutarate + L-aspartyl-[ankyrin-repeat domain protein] + O2 = (3S)-3-hydroxy-L-aspartyl-[ankyrin-repeat domain protein] + CO2 + succinate.
With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor
anthranilate 1,2-dioxygenase (deaminating, decarboxylating)
anthranilate + 3 H(+) + NADPH + O2 = catechol + CO2 + NADP(+) + NH4(+).
anthranilate + 3 H(+) + NADH + O2 = catechol + CO2 + NAD(+) + NH4(+).
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin.
benzene + H(+) + NADH + O2 = cis-1,2-dihydrobenzene-1,2-diol + NAD(+).
A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin.
H(+) + NADH + O2 + phthalate = cis-4,5-dihydroxycyclohexa-2,6-diene-1,2-dicarboxylate + NAD(+).
4-sulfobenzoate + NADH + O2 = 3,4-dihydroxybenzoate + NAD(+) + sulfite.
A system, containing a reductase and an iron-sulfur oxygenase, and no independent ferredoxin.
4-chlorophenylacetate + NADH + O2 = 3,4-dihydroxyphenylacetate + chloride + NAD(+).
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), and an iron-sulfur oxygenase.
benzoate + H(+) + NADH + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+).
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin.
Some other aromatic compounds, including ethylbenzene, 4-xylene and some halogenated toluenes, are converted into the corresponding cis-dihydrodiols.
H(+) + NADH + O2 + toluene = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD(+).
Comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.3), an iron-sulfur oxygenase, and ferredoxin.
H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+).
A multicomponent enzyme system composed of a dioxygenase component and an electron transfer component.
The enzyme, characterized from the bacterium Burkholderia cepacia 2CBS, has a broad substrate specificity.
Substrates include 2-fluorobenzoate, 2-chlorobenzoate, 2-bromobenzoate, and 2-iodobenzoate, which are processed in this order of preference.
a 2-halobenzoate + H(+) + NADH + O2 = a halide anion + catechol + CO2 + NAD(+).
2-chlorobenzoate + H(+) + NADH + O2 = catechol + chloride + CO2 + NAD(+).
2-aminobenzenesulfonate + 2 H(+) + NADH + O2 = 2,3-dihydroxybenzenesulfonate + NAD(+) + NH4(+).
benzene-1,4-dicarboxylate 1,2-dioxygenase
In Comamonas testoteroni, contains a Rieske [2Fe-2S] center.
H(+) + NADH + O2 + terephthalate = (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD(+).
2-oxo-1,2-dihydroquinoline 5,6-dioxygenase
3-Methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also substrates.
Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers.
H(+) + NADH + O2 + quinolin-2-ol = 5,6-dihydroquinoline-2,5,6-triol + NAD(+).
It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group.
NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate.
NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate.
The enzyme from Burkholderia fungorum strain LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron center.
Chlorine-substituted biphenyls can also act as substrates.
Similar to the three-component enzyme systems EC 1.14.12.3 and EC 1.14.12.11.
biphenyl + H(+) + NADH + O2 = (2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+).
It catalyzes the insertion of both atoms of molecular oxygen into positions 2 and 3 of the phenyl ring of 3-phenylpropanoate or (2E)-3-phenylprop-2-enoate.
3-phenylpropanoate + H(+) + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+).
(E)-cinnamate + H(+) + NADH + O2 = (2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD(+).
This enzyme catalyzes the first reaction in the pathway of carbazole degradation.
The enzyme attacks at the 1 and 9a positions of carbazole, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2'-aminobiphenyl-2,3-diol.
In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase.
The terminal oxygenase component contains a nonheme iron center and a Rieske [2Fe-2S] iron-sulfur cluster.
9H-carbazole + H(+) + NADH + O2 = 2'-aminobiphenyl-2,3-diol + NAD(+).
9H-carbazole + H(+) + NADPH + O2 = 2'-aminobiphenyl-2,3-diol + NADP(+).
This enzyme is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases.
It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3), and an alpha3beta3 oxygenase.
The enzyme forms of a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite.
It can typically act on many different nitroaromatic compounds, including chlorinated species.
Enzymes found in different strains may have different substrate preferences.
NADH + nitrobenzene + O2 = catechol + NAD(+) + nitrite.
2,6-dinitrotoluene + NADH + O2 = 3-methyl-4-nitrocatechol + NAD(+) + nitrite.
2-nitrotoluene + NADH + O2 = 3-methylcatechol + NAD(+) + nitrite.
3-nitrotoluene + NADH + O2 = 4-methylcatechol + NAD(+) + nitrite.
2-chloro-6-nitrotoluene + NADH + O2 = 4-chloro-3-methylcatechol + NAD(+) + nitrite.
2-chloro-4-nitrotoluene + NADH + O2 = 3-chloro-4-methylcatechol + NAD(+) + nitrite.
1,4-dinitrobenzene + NADH + O2 = 4-nitrocatechol + H(+) + NAD(+) + nitrite.
1,3-dinitrobenzene + NADH + O2 = 4-nitrocatechol + H(+) + NAD(+) + nitrite.
3,4-dinitrotoluene + NADH + O2 = 4-methyl-6-nitrocatechol + NAD(+) + nitrite.
4-nitrotoluene + NADH + O2 = 4-methylcatechol + NAD(+) + nitrite.
2,3-dinitrotoluene + NADH + O2 = 4-methyl-3-nitrocatechol + H(+) + NAD(+) + nitrite.
1-chloro-3-nitrobenzene + NADH + O2 = 4-chlorocatechol + NAD(+) + nitrite.
This enzyme, characterized from the bacterium Burkholderia sp. strain DNT, is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases.
The enzyme forms a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite.
2,4-dinitrotoluene + NADH + O2 = 4-methyl-5-nitrocatechol + NAD(+) + nitrite.
The enzyme, characterized from several Pseudomonas strains, is involved in the degradation of p-cymene and p-cumate.
It comprises four components: a ferredoxin, a ferredoxin reductase, and two subunits of a catalytic component.
The enzyme can also act on indole, transforming it to the water-insoluble blue dye indigo.
H(+) + NADH + O2 + p-cumate = (2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD(+).
This bacterial enzyme is a class IIB dioxygenase, comprising three components - a heterodimeric terminal dioxygenase, a ferredoxin protein, and a ferredoxin reductase.
The enzyme acts on a range of aromatic compounds, including mono-, di-, tri-, and tetra-chlorinated benzenes and toluenes.
chlorobenzene + H(+) + NADH + O2 = (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD(+).
With NADH or NADPH as one donor, and incorporation of one atom of oxygen
2 H(+) + NADH + O2 + salicylate = catechol + CO2 + H2O + NAD(+).
Most enzymes from Pseudomonas are highly specific for NAD(P)H (cf. EC 1.14.13.33).
4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP(+).
3-(2-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD(+).
H(+) + imidazole-4-acetate + NADH + O2 = 5-hydroxyimidazole-4-acetate + H2O + NAD(+).
H(+) + NADH + O2 + orcinol = 2,3,5-trihydroxytoluene + H2O + NAD(+).
The enzyme from the fungus Trichosporon cutaneum has a broad substrate specificity, and has been reported to catalyze the hydroxylation of a variety of substituted phenols, such as fluoro-, chloro-, amino- and methyl-phenols and also dihydroxybenzenes.
H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+).
dimethylaniline monooxygenase (N-oxide-forming)
methylphenyltetrahydropyridine N-monooxygenase
A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines.
Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate.
Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites.
For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP).
H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+).
H(+) + hypotaurine + NADPH + O2 = H2O + NADP(+) + taurine.
H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP(+).
2,6-dihydroxypyridine + H(+) + NADH + O2 = 2,3,6-trihydroxypyridine + H2O + NAD(+).
(E)-cinnamate + H(+) + NADPH + O2 = H2O + NADP(+) + trans-2-coumarate.
cyclopentanone + H(+) + NADPH + O2 = 5-valerolactone + H2O + NADP(+).
Also acts on 4-hydroxyhydratropate forming 2-methylhomogentisate and on 4-hydroxyphenoxyacetate forming hydroquinone and glycolate.
4-hydroxyphenylacetate + H(+) + NADPH + O2 = H2O + homogentisate + NADP(+).
4-hydroxyphenylacetate + H(+) + NADH + O2 = H2O + homogentisate + NAD(+).
Also acts on fustin, but not on catechin, quercetin or mollisacacidin.
(2R,3R)-dihydroquercetin + H(+) + NADH + O2 = (2R,3R)-2,3-dihydrogossypetin + H2O + NAD(+).
(2R,3R)-dihydroquercetin + H(+) + NADPH + O2 = (2R,3R)-2,3-dihydrogossypetin + H2O + NADP(+).
Also acts, more slowly, on 4-chlorophenol and 4-chloro-2-methylphenol.
NADH can act instead of NADPH, but more slowly.
2,4-dichlorophenol + H(+) + NADPH + O2 = 3,5-dichlorocatechol + H2O + NADP(+).
cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing)
In the catalytic mechanism of this enzyme, the nucleophilic species that attacks the carbonyl group is a peroxyflavin intermediate that is generated by reaction of the enzyme-bound flavin cofactor with NAD(P)H and oxygen.
This enzyme is able to catalyze a wide range of oxidative reactions, including enantioselective Baeyer-Villiger reactions, sulfoxidations, amine oxidations and epoxidations.
cyclohexanone + H(+) + NADPH + O2 = H2O + hexano-6-lactone + NADP(+).
Also acts on a number of analogs of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
3-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP(+).
NADPH can act instead of NADH, more slowly.
3-hydroxybenzoate + H(+) + NADH + O2 = 2,5-dihydroxybenzoate + H2O + NAD(+).
The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3.
Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO2, ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly.
H(+) + methane + NADH + O2 = H2O + methanol + NAD(+).
H(+) + methane + NADPH + O2 = H2O + methanol + NADP(+).
Acts on anthranilate and 4-aminosalicylate but not on salicylate (cf. EC 1.14.13.1).
4-aminobenzoate + 2 H(+) + NADH + O2 = 4-aminophenol + CO2 + H2O + NAD(+).
4-aminobenzoate + 2 H(+) + NADPH + O2 = 4-aminophenol + CO2 + H2O + NADP(+).
4-nitrophenol + H(+) + NADH + O2 = 4-nitrocatechol + H2O + NAD(+).
2-nitrophenol + 2 H(+) + 2 NADPH + O2 = catechol + H2O + 2 NADP(+) + nitrite.
albendazole monooxygenase (flavin-containing)
A microsomal flavin-containing monooxygenase.
A similar conversion is also carried out by some microsomal cytochrome P450 enzymes (EC 1.14.14.73).
It is estimated that cytochrome P450s are responsible for 70% of the activity.
albendazole + H(+) + NADPH + O2 = albendazole S-oxide + H2O + NADP(+).
4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
The enzyme from Corynebacterium cyclohexanicum is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at approximately equal rates (cf. EC 1.14.13.2).
It is less specific for NADPH than EC 1.14.13.2.
4-hydroxybenzoate + H(+) + NADH + O2 = 3,4-dihydroxybenzoate + H2O + NAD(+).
Also acts on N-acetyl-leukotriene E4, more slowly.
H(+) + leukotriene E4 + NADPH + O2 = 20-hydroxy-leukotriene E4 + H2O + NADP(+).
anthranilate 3-monooxygenase (deaminating)
anthranilate 2,3-hydroxylase (deaminating)
The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD).
anthranilate + 2 H(+) + NADPH + O2 = 2,3-dihydroxybenzoate + NADP(+) + NH4(+).
The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics.
anhydrotetracycline + H(+) + NADPH + O2 = 5a,11a-dehydrotetracycline + H2O + NADP(+).
endothelium-derived relaxation factor-forming enzyme
endothelium-derived relaxing factor synthase
The enzyme consists of linked oxygenase and reductase domains.
The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain.
Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center.
The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center.
H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide.
2-aminobenzoyl-CoA monooxygenase/reductase
The non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexanedione.
anthraniloyl-CoA + 2 H(+) + 2 NADPH + O2 = 2-amino-5-oxocyclohex-1-enecarbonyl-CoA + H2O + 2 NADP(+).
anthraniloyl-CoA + 2 H(+) + 2 NADH + O2 = 2-amino-5-oxocyclohex-1-enecarbonyl-CoA + H2O + 2 NAD(+).
The enzyme cleaves the anthraquinone ring of questin to form a benzophenone.
Involved in the biosynthesis of the seco-anthraquinone (+)-geodin.
NADPH + O2 + questin = demethylsulochrin + NADP(+).
Also converts 2,2'-dihydroxybiphenyl into 2,2',3-trihydroxy-biphenyl.
biphenyl-2-ol + H(+) + NADH + O2 = biphenyl-2,3-diol + H2O + NAD(+).
biphenyl-2,2'-diol + H(+) + NADH + O2 = biphenyl-2,2',3-triol + H2O + NAD(+).
(-)-menthol + H(+) + NADPH + O2 = 1,4-menthane-3,8-diol + H2O + NADP(+).
The enzyme displaces a diverse range of substituents from the 4-position of polyhalogenated phenols but requires that a halogen substituent be present at the 2-position.
If C-4 carries a halogen substituent, reaction 1 is catalyzed; if C-4 is unsubstituted, reaction 2 is catalyzed.
H(+) + NADPH + O2 + pentachlorophenol = 2,3,5,6-tetrachloro-1,4-benzoquinone + chloride + H2O + NADP(+).
2,3,5,6-tetrachlorophenol + NADPH + O2 = 2,3,5,6-tetrachlorohydroquinone + H2O + NADP(+).
The product undergoes non-enzymic cleavage and subsequent ring closure to form the lactone 4,5-dihydro-5,5-dimethyl-4-(3-oxobutyl)furan-2(3H)-one.
6-oxocineole + H(+) + NADPH + O2 = 1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one + H2O + NADP(+).
A single enzyme catalyzing three types of monooxygenase (Baeyer-Villiger oxidation) reactions.
H(+) + NADPH + O2 + progesterone = H2O + NADP(+) + testosterone acetate.
androst-4-ene-3,17-dione + H(+) + NADPH + O2 = H2O + NADP(+) + testololactone.
17alpha-hydroxyprogesterone + NADPH + O2 = acetate + androst-4-ene-3,17-dione + H2O + NADP(+).
benzoyl-CoA + H(+) + NADPH + O2 = 3-hydroxybenzoyl-CoA + H2O + NADP(+).
The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates.
L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+).
2-oxo-1,2-dihydroquinoline 8-monooxygenase
Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.
H(+) + NADH + O2 + quinolin-2-ol = H2O + NAD(+) + quinoline-2,8-diol.
quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer.
H(+) + NADH + O2 + quinolin-4-ol = H2O + NAD(+) + quinoline-3,4-diol.
3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency.
3-hydroxyphenylacetate + H(+) + NADPH + O2 = H2O + homogentisate + NADP(+).
3-hydroxyphenylacetate + H(+) + NADH + O2 = H2O + homogentisate + NAD(+).
The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron donor.
4-hydroxybenzoate + 2 H(+) + NADPH + O2 = CO2 + H2O + hydroquinone + NADP(+).
4-hydroxybenzoate + 2 H(+) + NADH + O2 = CO2 + H2O + hydroquinone + NAD(+).
2-hydroxycyclohexan-1-one + NADPH + O2 = 6-oxohexanoate + H2O + NADP(+).
The enzyme from Xanthobacter sp. strain Py2 is a multicomponent enzyme comprising: (1) an NADH reductase, which provides the reductant for O2 activation. (2) a Rieske-type ferredoxin, which is an electron-transfer protein. (3) an oxygenase, which contains the catalytic center for alkene epoxidation. (4) a small protein of unknown function that is essential for activity.
The enzyme oxygenates C2 to C6 aliphatic alkenes.
With propene as substrate, the stereospecificity of the epoxypropane formed is 95% (R) and 5% (S).
H(+) + NADH + O2 + propene = 1,2-epoxypropane + H2O + NAD(+).
magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase
Mg-protoporphyrin IX monomethyl ester oxidative cyclase
The enzyme participates in the biosynthesis of chlorophyllide a in aerobic organisms.
The same transformation is achieved in anaerobic organisms by EC 1.21.98.3.
Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.
2 H(+) + Mg-protoporphyrin IX 13-monomethyl ester + 3 NADPH + 3 O2 = 3,8-divinyl protochlorophyllide a + 5 H2O + 3 NADP(+).
Forms part of the vanillin degradation pathway in Arthrobacter sp.
H(+) + NADH + O2 + vanillate = 3,4-dihydroxybenzoate + formaldehyde + H2O + NAD(+).
An oxygen atom from dioxygen is incorporated into the macrocycle at C-20.
In the aerobic cobalamin biosynthesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A.
This enzyme carries out the first of the four steps, yielding precorrin-3B as the product.
This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively.
2 H(+) + NADH + O2 + precorrin-3A = H2O + NAD(+) + precorrin-3B.
The enzyme from Pseudomonas fluorescens ACB catalyzes the conversion of a wide range of acetophenone derivatives.
Highest activity occurs with compounds bearing an electron-donating substituent at the para position of the aromatic ring.
In the absence of substrate, the enzyme can act as an NADPH oxidase (EC 1.6.3.1).
4'-hydroxyacetophenone + H(+) + NADPH + O2 = 4-acetoxyphenol + H2O + NADP(+).
In addition to phenylacetone, which is the best substrate found to date, this Baeyer-Villiger monooxygenase can oxidize other aromatic ketones [1-(4-hydroxyphenyl)propan-2-one, 1-(4-hydroxyphenyl)propan-2-one and 3-phenylbutan-2-one], some alipatic ketones (e.g. dodecan-2-one) and sulfides (e.g. 1-methyl-4-(methylsulfanyl)benzene).
H(+) + NADPH + O2 + phenylacetone = benzyl acetate + H2O + NADP(+).
senecionine monooxygenase (N-oxide-forming)
While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates.
Senecionine N-oxide is used by insects as a chemical defense: it is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P450 oxidase when absorbed by insectivores.
NADPH + O2 + senecionine = H2O + NADP(+) + senecionine N-oxide.
monocyclic monoterpene ketone monooxygenase
1-hydroxy-2-oxolimonene 1,2-monooxygenase
This Baeyer-Villiger monooxygenase enzyme from the Gram-positive bacterium Rhodococcus erythropolis DCL14 has wide substrate specificity, catalyzing the lactonization of a large number of monocyclic monoterpene ketones and substituted cyclohexanones.
Both (1R,4S)- and (1S,4R)-1-hydroxymenth-8-en-2-one are metabolized, with the lactone product spontaneously rearranging to form 3-isopropenyl-6-oxoheptanoate.
(1R,4S)-menthone + H(+) + NADPH + O2 = (4R,7S)-7-isopropyl-4-methyloxepan-2-one + H2O + NADP(+).
dihydrocarvone + H(+) + NADPH + O2 = 4-isopropenyl-7-methyloxepan-2-one + H2O + NADP(+).
dihydrocarvone + H(+) + NADPH + O2 = 6-isopropenyl-3-methyloxepan-2-one + H2O + NADP(+).
1-hydroxylimonen-2-one + NADPH + O2 = 3-isopropenyl-6-oxoheptanoate + H2O + NADP(+).
(1S,4R)-1-hydroxylimonen-2-one + H(+) + NADPH + O2 = (4R,7R)-7-hydroxy-4-isopropenyl-7-methyloxepan-2-one + H2O + NADP(+).
(1R,4S)-1-hydroxylimonen-2-one + H(+) + NADPH + O2 = (4S,7S)-7-hydroxy-4-isopropenyl-7-methyloxepan-2-one + H2O + NADP(+).
(1R,4S)-1-hydroxylimonen-2-one + NADPH + O2 = (3S)-3-isopropenyl-6-oxoheptanoate + H2O + NADP(+).
(1S,4R)-1-hydroxylimonen-2-one + NADPH + O2 = (3R)-3-isopropenyl-6-oxoheptanoate + H2O + NADP(+).
(4S,7S)-7-hydroxy-4-isopropenyl-7-methyloxepan-2-one = (3S)-3-isopropenyl-6-oxoheptanoate + H(+).
(4R,7R)-7-hydroxy-4-isopropenyl-7-methyloxepan-2-one = (3R)-3-isopropenyl-6-oxoheptanoate + H(+).
(1R,4R)-dihydrocarvone + H(+) + NADPH + O2 = (3R,6R)-6-isopropenyl-3-methyloxepan-2-one + H2O + NADP(+).
(1R,4R)-dihydrocarvone + H(+) + NADPH + O2 = (4R,7R)-4-isopropenyl-7-methyloxepan-2-one + H2O + NADP(+).
(1S,4R)-isodihydrocarvone + H(+) + NADPH + O2 = (3S,6R)-6-isopropenyl-3-methyloxepan-2-one + H2O + NADP(+).
Limonene is the most widespread terpene and is formed by more than 300 plants.
Rhodococcus erythropolis DCL14, a Gram-positive bacterium, is able to grow on both (S)-limonene and (R)-limonene as the sole source of carbon and energy.
NADPH can act instead of NADH, although more slowly.
It has not been established if the product formed is optically pure or a mixture of two enantiomers.
(4S)-limonene + H(+) + NADPH + O2 = H2O + limonene 1,2-epoxide + NADP(+).
(4S)-limonene + H(+) + NADH + O2 = H2O + limonene 1,2-epoxide + NAD(+).
(4R)-limonene + H(+) + NADH + O2 = H2O + limonene 1,2-epoxide + NAD(+).
(4R)-limonene + H(+) + NADPH + O2 = H2O + limonene 1,2-epoxide + NADP(+).
Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms.
Compared with EC 1.14.14.5, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates.
The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising an hydroxylase, a reductase (MsmD) and a ferredoxin (MsmC).
The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] cluster.
methanesulfonate + NADH + O2 = formaldehyde + H2O + NAD(+) + sulfite.
The reaction is part of the purine catabolic pathway in the bacterium Klebsiella pneumoniae.
The enzyme is different from EC 1.7.3.3, found in most plants, which produces hydrogen peroxide.
The product of the enzyme is a substrate for EC 3.5.2.17.
H(+) + NADH + O2 + urate = 5-hydroxyisourate + H2O + NAD(+).
The reaction is involved in the aerobic catabolism of nicotinic acid.
6-hydroxynicotinate + 2 H(+) + NADH + O2 = 2,5-dihydroxypyridine + CO2 + H2O + NAD(+).
Catalyzes two successive hydroxylations at the 7-methyl group of chlorophyllide a.
The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b.
Chlorophyll a and protochlorophyllide a are not substrates.
chlorophyllide a + 2 H(+) + 2 NADPH + 2 O2 = chlorophyllide b + 3 H2O + 2 NADP(+).
3-(3-hydroxy-phenyl)propanoic acid hydroxylase
This enzyme participates in a meta-cleavage pathway employed by the bacterium Escherichia coli for the degradation of various phenylpropanoid compounds.
3-(3-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD(+).
(2E)-3-(3-hydroxyphenyl)prop-2-enoate + H(+) + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H2O + NAD(+).
Part of the caffeine degradation pathway in Pseudomonas putida.
7-methylxanthine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+) + xanthine.
7-methylxanthine + H(+) + NADH + O2 = formaldehyde + H2O + NAD(+) + xanthine.
The enzyme initiates the degradation of pyrrole-2-carboxylate.
H(+) + NADH + O2 + pyrrole-2-carboxylate = 5-hydroxypyrrole-2-carboxylate + H2O + NAD(+).
dissimilatory dimethyl-sulfide monooxygenase
The enzyme participates exclusively in sulfur dissimilation.
It has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides.
Its activity is stimulated by combined addition of FMN, and, after depletion of cations, of Mg(2+) and Fe(2+).
The enzymes from bacteria of the Hyphomicrobium genus are a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit.
dimethyl sulfide + H(+) + NADH + O2 = formaldehyde + H2O + methanethiol + NAD(+).
The enzyme is involved in the catabolic pathway for the degradation of chrysene in some bacteria.
1-hydroxy-2-naphthoate + 2 H(+) + NADH + O2 = CO2 + H2O + NAD(+) + naphthalene-1,2-diol.
1-hydroxy-2-naphthoate + 2 H(+) + NADPH + O2 = CO2 + H2O + NADP(+) + naphthalene-1,2-diol.
Also acts on taxa-4(20),11-dien-5alpha-yl acetate.
10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate + H(+) + NADPH + O2 = 10beta,14beta-dihydroxytaxa-4(20),11-dien-5alpha-yl acetate + H2O + NADP(+).
A cytochrome P-450 (heme-thiolate) protein from the yew tree Taxus cuspidata.
Does not act on earlier intermediates in taxol biosynthesis.
O2 + reduced [NADPH--hemoprotein reductase] + taxusin = 7beta-hydroxytaxusin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
2alpha-hydroxytaxusin + O2 + reduced [NADPH--hemoprotein reductase] = 2alpha,7beta-dihydroxytaxusin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy.
The mammalian enzyme is involved in detoxification of trimethylamine.
Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome).
NADPH + O2 + trimethylamine = H2O + NADP(+) + trimethylamine N-oxide.
Part of the aerobic pathway of phenylacetate catabolism in Escherichia coli and Pseudomonas putida.
H(+) + NADPH + O2 + phenylacetyl-CoA = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP(+).
The enzyme has been characterized from Salvia officinalis (sage).
(1R,5R)-sabinene + H(+) + NADPH + O2 = (1S,3R,5S)-sabinol + H2O + NADP(+).
The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis.
It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B.
erythromycin D + H(+) + NADPH + O2 = erythromycin C + H2O + NADP(+).
Involved in the catabolism of alpha-pinene.
(1S,5S)-alpha-pinene + H(+) + NADH + O2 = alpha-pinene oxide + H2O + NAD(+).
(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase
2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase
2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase
Forms part of the catabolism of camphor.
It acts on the CoA ester in preference to the free acid.
[(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + H(+) + NADPH + O2 = [(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA + H2O + NADP(+).
A cytochrome P450 monooxygenase isolated from Salvia officinalis (sage).
Involved in the catabolism of camphor in senescent tissue.
(1R,4R)-camphor + H(+) + NADPH + O2 = (+)-6-exo-hydroxycamphor + H2O + NADP(+).
6-hydroxy-3-succinoylpyridine 3-monooxygenase
6-hydroxy-3-succinoylpyridine hydroxylase
The enzyme catalyzes a reaction in the nicotine degradation pathway of Pseudomonas species.
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 H(+) + 2 NADH + O2 = 2,5-dihydroxypyridine + H2O + 2 NAD(+) + succinate semialdehyde.
The enzyme catalyzes the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite.
Forms a two-component system with a flavoprotein reductase.
The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyze EC 1.14.13.29, while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyze EC 1.14.13.167.
4-nitrocatechol + NADPH + O2 = 2-hydroxy-1,4-benzoquinone + H2O + NADP(+) + nitrite.
4-nitrocatechol + NADH + O2 = 2-hydroxy-1,4-benzoquinone + H2O + NAD(+) + nitrite.
The enzyme catalyzes the first step in a degradation pathway for 4-nitrophenol, the oxidation of 4-nitrophenol at position 4 with the concomitant removal of the nitro group as nitrite.
The enzyme from the bacterium Pseudomonas sp. WBC-3 also catalyzes EC 1.14.13.166.
4-nitrophenol + H(+) + NADPH + O2 = 1,4-benzoquinone + H2O + NADP(+) + nitrite.
This plant enzyme, along with EC 2.6.1.99, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.
H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate + CO2 + H2O + NADP(+).
Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae.
The ketone undergoes a biological Baeyer-Villiger reaction.
Part of the pathway of pentalenolactone biosynthesis.
1-deoxy-11-oxopentalenate + H(+) + NADPH + O2 = H2O + NADP(+) + pentalenolactone D.
1-deoxy-11-oxopentalenate + H(+) + NADPH + O2 = H2O + NADP(+) + neopentalenolactone D.
This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7), an iron-sulfur oxygenase, and ferredoxin.
H(+) + NADH + O2 + salicylate = 2,5-dihydroxybenzoate + H2O + NAD(+).
The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, and has a 5-fold higher activity with NADH than with NADPH.
Also demethylates 1-methylxantine with lower efficiency.
Forms part of the degradation pathway of methylxanthines.
caffeine + H(+) + NADH + O2 = formaldehyde + H2O + NAD(+) + theobromine.
caffeine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+) + theobromine.
H(+) + NADPH + O2 + theophylline = 3-methylxanthine + formaldehyde + H2O + NADP(+).
H(+) + NADH + O2 + theophylline = 3-methylxanthine + formaldehyde + H2O + NAD(+).
1,7-dimethylxanthine + H(+) + NADH + O2 = 7-methylxanthine + formaldehyde + H2O + NAD(+).
1,7-dimethylxanthine + H(+) + NADPH + O2 = 7-methylxanthine + formaldehyde + H2O + NADP(+).
The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, and has higher activity with NADH than with NADPH.
Also demethylates caffeine and theophylline with lower efficiency.
H(+) + NADH + O2 + theobromine = 7-methylxanthine + formaldehyde + H2O + NAD(+).
H(+) + NADPH + O2 + theobromine = 7-methylxanthine + formaldehyde + H2O + NADP(+).
3-methylxanthine + H(+) + NADH + O2 = formaldehyde + H2O + NAD(+) + xanthine.
3-methylxanthine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+) + xanthine.
The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins.
aklavinone + H(+) + NADPH + O2 = epsilon-rhodomycinone + H2O + NADP(+).
The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogs (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.
13-deoxydaunorubicin + H(+) + NADPH + O2 = 13-dihydrodaunorubicin + H2O + NADP(+).
13-dihydrodaunorubicin + H(+) + NADPH + O2 = daunorubicin + 2 H2O + NADP(+).
daunorubicin + H(+) + NADPH + O2 = doxorubicin + H2O + NADP(+).
2-heptyl-3-hydroxy-4(1H)-quinolone synthase
2-heptyl-3,4-dihydroxyquinoline synthase
The enzyme from the bacterium Pseudomonas aeruginosa catalyzes the terminal step in biosynthesis of the signal molecule 2-heptyl-3,4-dihydroxyquinoline that plays a role in regulation of virulence genes.
2-heptyl-4(1H)-quinolone + H(+) + NADH + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + H2O + NAD(+).
Isolated from the bacterium Micromonospora carbonacea var. africana.
The nitroso group is probably spontaneously oxidized to a nitro group giving dTDP-beta-L-evernitrose, which is involved in the biosynthesis of the antibiotic everninomycin.
The reaction was studied using dTDP-beta-L-4-epi-vancosamine (dTDP-4-O-desmethyl-beta-L-evernitrosamine).
dTDP-beta-L-evernosamine + H(+) + 2 NADPH + 2 O2 = dTDP-2,3,6-trideoxy-3-C-methyl-4-O-methyl-3-nitroso-beta-L-arabino-hexopyranose + 3 H2O + 2 NADP(+).
The enzyme from the bacterium Streptomyces sahachiroi is involved in the biosynthesis of 3-methoxy-5-methyl-1-naphthoate, a component of of the the antitumor antibiotic azinomycin B.
5-methyl-1-naphthoate + H(+) + NADPH + O2 = 3-hydroxy-5-methyl-1-naphthoate + H2O + NADP(+).
The enzyme is involved in biosynthesis of N(5)-hydroxy-L-ornithine, N(5)-formyl-N(5)-hydroxy-L-ornithine or N(5)-acetyl-N(5)-hydroxy-L-ornithine.
These nonproteinogenic amino acids are building blocks of siderophores produced by some bacteria (e.g. Streptomyces coelicolor, Saccharopolyspora erythraea and Pseudomonas aeruginosa).
L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+).
L-ornithine N(5)-monooxygenase [NAD(P)H]
The enzyme from the pathogenic fungus Aspergillus fumigatus catalyzes a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria sp. 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics.
Activity of the fungal enzyme is higher with NADPH, due to the fact that following the reduction of the flavin, NADP(+) (but not NAD(+)) stabilizes the C4a-hydroperoxyflavin intermediate that oxidizes the substrate.
L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+).
tetracenomycin A2 monooxygenase-diooxygenase
Isolated from the bacterium Streptomyces glaucescens.
The enzyme was also isolated from the bacterium Streptomyces olivaceus, where it acts on 8-demethyltetracenomycin A2 (tetracenomycin B2) as part of elloramycin biosynthesis.
The reaction involves a monooxygenase reaction which is followed by a dioxygenase reaction giving a gem-diol and an epoxide.
Water opens the epoxide giving two hydroxy groups.
The gem-diol eliminates water to give a ketone which is then reduced to a hydroxy group.
2 H(+) + 2 NADPH + 2 O2 + tetracenomycin A2 = H2O + 2 NADP(+) + tetracenomycin C.
2 H(+) + 2 NADH + 2 O2 + tetracenomycin A2 = H2O + 2 NAD(+) + tetracenomycin C.
The enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii.
BoxB functions as the oxygenase part of benzoyl-CoA oxygenase in conjunction with BoxA, the reductase component, which upon binding of benzoyl-CoA, transfers two electrons to the ring in the course of dioxygenation.
benzoyl-CoA + H(+) + NADPH + O2 = 2,3-epoxy-2,3-dihydrobenzoyl-CoA + H2O + NADP(+).
The enzyme, characterized from the bacterium Streptomyces sp. WA46, participates in a pathway for salicylate degradation.
2-hydroxybenzoyl-CoA + H(+) + NADH + O2 = 2,5-dihydroxybenzoyl-CoA + H2O + NAD(+).
4-methyl-5-nitrocatechol 5-monooxygenase
The enzyme, isolated from the bacterium Burkholderia sp. DNT, can use both NADH and NADPH, but prefers NADPH.
It has a narrow substrate range, but can also act on 4-nitrocatechol.
4-methyl-5-nitrocatechol + NADPH + O2 = 2-hydroxy-5-methylquinone + H(+) + H2O + NADP(+) + nitrite.
4-methyl-5-nitrocatechol + NADH + O2 = 2-hydroxy-5-methylquinone + H(+) + H2O + NAD(+) + nitrite.
The enzyme has been found in the Corynebacteria Rhodococcus equi and Nocardia farcinica.
It confers increased resistance to the antibiotic rifampicin by initiating its degradation.
NADPH + O2 + rifampicin = 2'-N-hydroxyrifampicin + H2O + NADP(+).
NADH + O2 + rifampicin = 2'-N-hydroxyrifampicin + H2O + NAD(+).
1,3,7-trimethyluric acid 5-monooxygenase
The enzyme, characterized from the bacterium Pseudomonas sp. CBB1, is part of the bacterial C-8 oxidation-based caffeine degradation pathway.
The product decomposes spontaneously to a racemic mixture of 3,6,8-trimethylallantoin.
The enzyme shows no acitivity with urate.
1,3,7-trimethylurate + H(+) + NADH + O2 = 1,3,7-trimethyl-5-hydroxyisourate + H2O + NAD(+).
The enzyme, characterized from the bacterium Streptomyces nodosus subsp. asukaensis, is involved in the biosynthesis of the antibiotic asukamycin.
H(+) + NADH + O2 + protoasukamycin = 4-hydroxyprotoasukamycin + H2O + NAD(+).
The enzyme, characterized from the fungus Aspergillus alliaceus, contains an FAD cofactor.
The enzyme inserts a hydroxyl group, leading to formation of a N-C bond that creates an additional cycle between the bicyclic indole and the tetracyclic core moieties, resulting in the heptacyclic asperlicin E.
asperlicin C + H(+) + NADH + O2 = asperlicin E + H2O + NAD(+).
asperlicin C + H(+) + NADPH + O2 = asperlicin E + H2O + NADP(+).
The enzyme, characterized from the bacterium Chromobacterium violaceum, participates in the biosynthesis of the violet pigment violacein.
The immediate product, protoviolaceinate, can be acted upon by EC 1.14.13.224, leading to violacein production.
However, it is very labile, and in the presence of oxygen can be converted to the shunt product proviolacein.
H(+) + NADPH + O2 + protodeoxyviolaceinate = H2O + NADP(+) + protoviolaceinate.
H(+) + NADH + O2 + protodeoxyviolaceinate = H2O + NAD(+) + protoviolaceinate.
2 H(+) + NADPH + 2 O2 + protodeoxyviolaceinate = CO2 + 2 H2O + NADP(+) + proviolacein.
2 H(+) + NADH + 2 O2 + protodeoxyviolaceinate = CO2 + 2 H2O + NAD(+) + proviolacein.
H(+) + O2 + protoviolaceinate = CO2 + H2O + proviolacein.
5-methylphenazine-1-carboxylate 1-monooxygenase
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanine, a toxin produced and secreted by the organism.
It can also act on phenazine-1-carboxylate, converting it into 1-hydroxyphenazine.
5-methyl-phenazine-1-carboxylate + 2 H(+) + NADH + O2 = CO2 + H2O + NAD(+) + pyocyanin.
2 H(+) + NADH + O2 + phenazine-1-carboxylate = 1-hydroxyphenazine + CO2 + H2O + NAD(+).
The enzyme, characterized from the bacterium Corynebacterium glutamicum, is a single-component hydroxylase.
H(+) + NADPH + O2 + resorcinol = benzene-1,2,4-triol + H2O + NADP(+).
The enzyme, characterized from the bacterium Rhodococcus jostii RHA1, is a single-component hydroxylase.
H(+) + NADH + O2 + resorcinol = benzene-1,2,4-triol + H2O + NAD(+).
The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH.
It catalyzes the initial steps in the conversion of aurachin C to aurachin B.
The FAD-dependent monooxygenase catalyzes the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4.
aurachin C + H(+) + NADH + O2 = 4-hydroxy-2-methyl-3-oxo-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + H2O + NAD(+).
aurachin C + H(+) + NADPH + O2 = 4-hydroxy-2-methyl-3-oxo-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + H2O + NADP(+).
3-hydroxy-4-methyl-anthranilyl-[aryl-carrier protein] 5-monooxygenase
The enzyme, characterized from the bacterium Streptosporangium sibiricum, is involved in the biosynthesis of the antitumor antibiotic sibiromycin.
The enzyme is not active with free 3-hydroxy-4-methylanthranilate.
3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] + H(+) + NADH + O2 = 3,5-dihydroxy-4-methylanthranilyl-[aryl-carrier protein] + H2O + NAD(+).
The immediate products, violaceinate and deoxyviolaceinate, undergo non-enzymic autooxidation into violacein and deoxyviolacein, respectively.
H(+) + NADH + O2 + protoviolaceinate = H2O + NAD(+) + violaceinate.
H(+) + NADPH + O2 + protoviolaceinate = H2O + NADP(+) + violaceinate.
H(+) + NADPH + O2 + protodeoxyviolaceinate = deoxyviolaceinate + H2O + NADP(+).
H(+) + NADH + O2 + protodeoxyviolaceinate = deoxyviolaceinate + H2O + NAD(+).
2 H(+) + NADH + 2 O2 + protoviolaceinate = CO2 + 2 H2O + NAD(+) + violacein.
H(+) + O2 + violaceinate = CO2 + H2O + violacein.
2 H(+) + NADPH + 2 O2 + protoviolaceinate = CO2 + 2 H2O + NADP(+) + violacein.
2 H(+) + NADPH + 2 O2 + protodeoxyviolaceinate = CO2 + deoxyviolacein + 2 H2O + NADP(+).
2 H(+) + NADH + 2 O2 + protodeoxyviolaceinate = CO2 + deoxyviolacein + 2 H2O + NAD(+).
deoxyviolaceinate + H(+) + O2 = CO2 + deoxyviolacein + H2O.
The enzyme, characterized from the fruit fly Drosophila melanogaster, is a multi-domain oxidoreductase that acts as an F-actin disassembly factor.
The enzyme selectively reduces two L-Met residues of F-actin, causing fragmentation of the filaments and preventing repolymerization.
The reaction is stereospecific and generates the (R)-sulfoxide.
H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-(R)-S-oxide-[F-actin] + NADP(+).
H(+) + L-methionyl(44)-[F-actin] + NADPH + O2 = H2O + L-methionyl(44)-(R)-S-oxide-[F-actin] + NADP(+).
H(+) + L-methionyl(47)-[F-actin] + NADPH + O2 = H2O + L-methionyl(47)-(R)-S-oxide-[F-actin] + NADP(+).
acetone monooxygenase (methyl acetate-forming)
The enzyme, characterized from the bacterium Gordonia sp. TY-5, is a Baeyer-Villiger type monooxygenase and participates in a propane utilization pathway.
acetone + H(+) + NADPH + O2 = H2O + methyl acetate + NADP(+).
The enzyme, characterized from several bacterial strains, is a multicomponent dinuclear iron monooxygenase that includes a hydroxylase, an NADH-dependent reductase, and a coupling protein.
The enzyme has several additional activities, including acetone monooxygenase (acetol-forming) and phenol 4-monooxygenase.
H(+) + NADH + O2 + propane = H2O + NAD(+) + propan-2-ol.
Although believed to occur in plants, the enzyme has so far been characterized only from the rice blast fungus, Magnaporthe oryzae.
The fungus strategically deploys the enzyme to hydroxylate and inactivate endogenous jasmonate to evade the jasmonate-based innate immunity in rice plants.
H(+) + jasmonate + NADPH + O2 = (1R,2R)-12-hydroxyjasmonate + H2O + NADP(+).
Characterized from the bacterium Aquincola tertiaricarbonis.
It can also act, with lower efficiency, on propan-2-ol, converting it to propane-1,2-diol.
Depending on the substrate, the enzyme also catalyzes EC 1.14.19.48.
H(+) + NADPH + O2 + tert-butanol = 2-methylpropane-1,2-diol + H2O + NADP(+).
The enzyme, characterized from the bacterium Thauera butanivorans, is similar to EC 1.14.13.25, but has a very low activity with methane.
The enzyme can also act on other C3-C6 linear and branched aliphatic alkanes with lower activity.
butane + H(+) + NADH + O2 = butan-1-ol + H2O + NAD(+).
This bacterial enzyme confers resistance to all clinically relevant tetracyclines when expressed under aerobic conditions.
The hydroxylated products are very unstable and lead to intramolecular cyclization and non-enzymic breakdown to undefined products.
H(+) + NADPH + O2 + tetracycline = 11a-hydroxytetracycline + H2O + NADP(+).
That bacterium possesses two enzymes that can catalyze the reaction - OxyE is the main isozyme, while OxyL has a lower activity.
OxyL is bifunctional, and its main function is EC 1.14.13.233.
6-methylpretetramide + 2 H(+) + NADPH + O2 = 4-hydroxy-6-methylpretetramide + H2O + NADP(+).
4-hydroxy-6-methylpretetramide 12a-monooxygenase
The enzyme is bifunctional, and can also catalyze EC 1.14.13.232.
4-hydroxy-6-methylpretetramide + NADPH + O2 = 4-dedimethylamino-4-oxo-anhydrotetracycline + H2O + NADP(+).
The enzyme, characterized from the bacterium Streptomyces rimosus, is bifunctional, catalyzing two successive monooxygenation reactions.
It starts by catalyzing the stereospecific hydroxylation of anhydrotetracycline at C(6) (EC 1.14.13.38).
If the released product is captured by EC 1.3.98.4 it is reduced to tetracycline.
However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C(5), producing 5a,11a-dehydrooxytetracycline, which, following the action of EC 1.3.98.4, becomes oxytetracycline.
5a,11a-dehydrotetracycline + H(+) + NADPH + O2 = 5a,11a-dehydrooxytetracycline + H2O + NADP(+).
The enzyme, characterized from Pseudomonas putida strains, catalyzes the first step in a pathway for degradation of the plant hormone indole-3-acetate.
When acting on indole, the enzyme forms indoxyl, which reacts spontaneously with oxygen to form the blue dye indigo.
(indol-3-yl)acetate + H(+) + NADH + O2 = 2-hydroxy-(1H-indol-3-yl)acetate + H2O + NAD(+).
This bacterial enzyme belongs to a family of soluble diiron hydroxylases that includes toluene-, benzene-, xylene- and methane monooxygenases, phenol hydroxylases, and alkene epoxidases.
The enzyme comprises a four-component complex that includes a hydroxylase, NADH-ferredoxin oxidoreductase, a Rieske-type [2Fe-2S] ferredoxin, and an effector protein.
H(+) + NADH + O2 + toluene = 4-methylphenol + H2O + NAD(+).
omega-(methylthio)alkylglucosinolate S-oxygenase
The enzyme is a member of the flavin-dependent monooxygenase (FMO) family (cf. EC 1.14.13.8).
The plant Arabidopsis thaliana contains five isoforms.
GS-OX1 through GS-OX4 are able to catalyze the S-oxygenation independent of chain length, while GS-OX5 is specific for 8-(methylsulfanyl)octyl glucosinolate.
a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate S-glucoside + H(+) + NADPH + O2 = a (Z)-omega-(methylsulfinyl)-alkyl-glucosinolate + H2O + NADP(+).
The enzyme, characterized from several bacterial species, is involved in a pathway for the degradation of methylated amines.
It is composed of three subunits, one of which is a ferredoxin, and contains heme iron and an FMN cofactor.
dimethylamine + H(+) + NADPH + O2 = formaldehyde + H2O + methylamine + NADP(+).
The bacterial enzyme is a complex consisting of a reductase and an oxygenase components.
The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues.
(R)-carnitine + H(+) + NADH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NAD(+) + trimethylamine.
(R)-carnitine + H(+) + NADPH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NADP(+) + trimethylamine.
The enzyme from the bacterium Escherichia coli (UbiI) catalyzes the first hydroxylation during the aerobic biosynthesis of ubiquinone.
The enzyme from the bacterium Neisseria meningitidis (UbiM) can also catalyze the two additional hydroxylations that occur in the pathway (cf. EC 1.14.99.60).
a 2-all-trans-polyprenylphenol + H(+) + NADPH + O2 = a 3-(all-trans-polyprenyl)benzene-1,2-diol + H2O + NADP(+).
2-all-trans-octaprenylphenol + H(+) + NADPH + O2 = 3-(all-trans-octaprenyl)benzene-1,2-diol + H2O + NADP(+).
The enzyme, characterized from the bacterium Arthrobacter sp Cr-7, participates in the degradation of pyridoxine (vitamin B6).
Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have suggested that it is a monooxygnase, incorporating only one oxygen atom from molecular oxygen into the product.
The second oxygen atom originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
5-pyridoxate + NADPH + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP(+).
3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
3-hydroxy-2-methylpyridinecarboxylate dioxygenase
methylhydroxypyridine carboxylate dioxygenase
methylhydroxypyridinecarboxylate oxidase
Although the enzyme was initially thought to be a dioxygenase, oxygen-tracer experiments have shown that it is a monooxygnase, incorporating only one oxygen atom from molecular oxygen.
The second oxygen atom that is incorporated into the product originates from a water molecule, which is regenerated during the reaction and thus does not show up in the reaction equation.
3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2 = 2-(acetamidomethylene)succinate + NAD(+).
3-hydroxy-2-methylpyridine-5-carboxylate + NADPH + O2 = 2-(acetamidomethylene)succinate + NADP(+).
The enzyme, characterized from the bacterium Burkholderia cepacia, belongs to a class of nonheme, oxygen-dependent diiron enzymes.
It contains a hydroxylase component with two binuclear iron centers, an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-sulfur cluster, and a third component involved in electron transfer between the hydroxylase and the reductase.
The enzyme dihydroxylates its substrate in two sequential hydroxylations, initially forming 2-methylphenol, which is hydroxylated to 3-methylcatechol.
H(+) + NADH + O2 + toluene = 2-hydroxytoluene + H2O + NAD(+).
2-hydroxytoluene + H(+) + NADH + O2 = 3-methylcatechol + H2O + NAD(+).
The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component.
The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.
H(+) + NADH + O2 + phenol = catechol + H2O + NAD(+).
assimilatory dimethylsulfide S-monooxygenase
The enzyme, studied from the bacterium Acinetobacter sp. strain 20B, is very similar to EC 1.14.13.244.
It consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component.
The three components comprise five different polypeptides.
The enzyme catalyzes the first two steps of a dimethyl sulfide oxidation pathway in this organism.
dimethyl sulfide + H(+) + NADH + O2 = dimethyl sulfoxide + H2O + NAD(+).
dimethyl sulfoxide + H(+) + NADH + O2 = dimethyl sulfone + H2O + NAD(+).
Contains a Rieske [2Fe-2S] iron-sulfur cluster.
This bacterial enzyme (SdmA) participates in the biosynthesis of bacterial sterols.
Together with SdmB it forms an enzyme system that removes one methyl group from the C-4 position of 4,4-dimethylated steroid molecules.
SdmA catalyzes three successive oxidations of the C-4beta methyl group, turning it into a carboxylate group; the second enzyme, SdmB, is a bifunctional enzyme that catalyzes two different activities.
As EC 1.1.1.270 it reduces the 3-oxo group back to a 3beta-hydroxyl.
Unlike the animal/fungal enzyme EC 1.14.18.9 and the plant enzymes EC 1.14.18.10 and EC 1.14.18.11, this enzyme acts preferentially on the 4beta-methyl group.
Since no epimerization of the remaining C-4alpha methyl group occurs, the enzyme can only remove one methyl group, leaving a 4alpha-monomethylated product.
a 3beta-hydroxy-4,4-dimethylsteroid + 2 H(+) + 3 NADH + 3 O2 = a 3beta-hydroxy-4alpha-methylsteroid-4beta-carboxylate + 4 H2O + 3 NAD(+).
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + 2 H(+) + 3 NADH + 3 O2 = 4beta-carboxy-4alpha-methyl-5alpha-cholesta-8,24-dien-3beta-ol + 4 H2O + 3 NAD(+).
The enzyme, characterized from the bacterium Sinorhizobium meliloti 1021, consists of three different types of subunits.
The catalytic unit contains a Rieske [2Fe-2S] iron-sulfur cluster, and catalyzes the monooxygenation of a methyl group.
The resulting N-methoxyl group is unstable and decomposes spontaneously to form formaldehyde.
The other subunits are involved in the transfer of electrons from NAD(P)H to the catalytic subunit.
H(+) + L-proline betaine + NADPH + O2 = formaldehyde + H2O + N-methyl-L-proline + NADP(+).
H(+) + L-proline betaine + NADH + O2 = formaldehyde + H2O + N-methyl-L-proline + NAD(+).
L-aspartate N-monooxygenase (nitrosuccinate-forming)
The enzyme, found in some Actinobacteria, is involved in a pathway that forms nitrite, which is subsequently used to generate a diazo group in some secondary metabolites.
2 H(+) + L-aspartate + 3 NADPH + 3 O2 = 2-nitrobutanedioate + 4 H2O + 3 NADP(+).
3-amino-4-hydroxybenzoate 2-monooxygenase
The CreL enzyme from the bacterium Streptomyces cremeus participates in the biosynthesis of cremeomycin.
The PrmB3 and PtnB3 enzymes from Streptomyces platensis are involved in the biosynthesis of platensimycin and platencin, respectively.
3-amino-4-hydroxybenzoate + H(+) + NADPH + O2 = 3-amino-2,4-dihydroxybenzoate + H2O + NADP(+).
The enzyme, characterized from the bacterium Streptomyces achromogenes subsp. streptozoticus, catalyzes a complex multi-step reaction during the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin.
The overall reaction is an oxidative rearrangement of the guanidine group of N(omega)-methyl-L-arginine, generating an N-nitrosourea product.
The enzyme hydroxylates its substrate at the N(delta) position, followed by a second hydroxylation at the N(omega)' position. It then catalyzes an oxidative rearrangement to form N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline.
This product is unstable, and degrades non-enzymically into nitric oxide and the denitrosated product N(delta)-hydroxy-N(omega)-methyl-L-citrulline.
The enzyme contains two active sites, each of which utilizes a different iron-containing cofactor.
H(+) + N(omega)-methyl-L-arginine + 2 NADH + 3 O2 = 3 H2O + N(delta)-hydroxy-N(omega)-methyl-N(omega)-nitroso-L-citrulline + 2 NAD(+).
hexahomomethionine + 2 O2 + 2 NADPH + 2 H(+) = 9-methylthiononanaldoxime + 3 H2O + CO2 + NADP(+).
pentahomomethionine + 2 O2 + 2 NADPH + 2 H(+) = 8-methylthiooctanaldoxime + 3 H2O + CO2 + NADP(+).
4-nitrophenol + H(+) + NADPH + O2 = 4-nitrocatechol + H2O + NADP(+).
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups.
Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH.
Some of the reactions attributed to EC 1.14.15.3 belong here.
an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The reaction sequence starts with the incorporation of a molecule of oxygen into reduced FMN bound to the enzyme, forming luciferase peroxyflavin.
The peroxyflavin interacts with an aliphatic long-chain aldehyde, producing a highly fluorescent species believed to be luciferase hydroxyflavin.
The enzyme is highly specific for reduced FMN and for long-chain aliphatic aldehydes with eight carbons or more.
The highest efficiency is achieved with tetradecanal.
a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu.
FMNH2-dependent aliphatic sulfonate monooxygenase
The enzyme from Escherichia coli catalyzes the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates).
Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates.
Instead, it uses reduced FMN (i.e., FMNH2) as a substrate.
FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.38).
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H(+) + H2O + sulfite.
The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which ensures ample supply of FAD to the monooxygenase.
anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H(+) + H2O.
4-hydroxyphenylacetic acid-3-hydroxylase
The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds.
The enzyme uses FADH2 as a substrate rather than a cofactor.
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H(+) + H2O.
The enzyme from Aminobacter aminovorans (previously Chelatobacter heintzii) is part of a two component system that also includes EC 1.5.1.42 (FMN reductase), which provides reduced flavin mononucleotide for this enzyme.
FMNH2 + nitrilotriacetate + O2 = ammoniodiacetate + FMN + glyoxylate + H2O.
The enzyme catalyzes the first step in the aerobic styrene degradation pathway.
It forms a two-component system with a reductase (StyB) that utilizes NADH to reduce FAD, which is then transferred to the oxygenase.
FADH2 + O2 + styrene = (2S)-2-phenyloxirane + FAD + H(+) + H2O.
3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase
This bacterial enzyme participates in the degradation of several steroids, including cholesterol and testosterone.
It can use either FADH or FMNH2 as flavin cofactor.
The enzyme forms a two-component system with a reductase (HsaB) that utilizes NADH to reduce the flavin, which is then transferred to the oxygenase subunit.
3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMNH2 + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMN + H(+) + H2O.
4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase
Catalyzes a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family.
Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase.
The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory.
Octanoyl-S-[BtrI acyl-carrier protein] is also accepted.
4-(gamma-L-glutamylamino)butanoy-[BtrI ACP] + FMNH2 + O2 = 4-(gamma-L-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI ACP] + FMN + H(+) + H2O.
The enzyme catalyzes three sequential hydroxylations of the androgens androst-4-ene-3,17-dione and testosterone, resulting in their aromatization and forming the estrogens estrone and 17beta-estradiol, respectively.
3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
androst-4-ene-3,17-dione + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = estrone + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] monooxygenase
The enzyme from the bacterium Streptomyces globisporus is involved in the biosynthesis of the (S)-3-chloro-5-hydroxy-beta-tyrosine moiety prior to incorporation into the chromoprotein antitumor antibiotic C-1027.
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[SgcC2 peptidyl-carrier protein] + FADH2 + O2 = (3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[SgcC2 peptidyl-carrier protein] + FAD + H(+) + H2O.
for the conversion of progesterone and 17alpha-hydroxyprogesterone to their respective 21-hydroxylated derivatives, 11-deoxycorticosterone and 11-deoxycortisol.
Involved in the biosynthesis of the hormones aldosterone and cortisol.
O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 21-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein reductase] = 11-deoxycortisol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This enzyme, together with EC 5.4.99.7, was formerly known as squalene oxidocyclase.
The electron donor, NADPH, is coupled via EC 1.6.2.4.
O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This mammalian enzyme participates in the degradation of heme.
The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules.
The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO.
The enzyme requires NAD(P)H and EC 1.6.2.4.
heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase].
Catalyzes two independent reactions at the same active site - the 17alpha-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis, and the conversion of the 17alpha-hydroxylated products via a 17,20-lyase reaction to form androstenedione and dehydroepiandrosterone, leading to sex hormone biosynthesis (EC 1.14.14.32).
The ratio of the 17alpha-hydroxylase and 17,20-lyase activities is an important factor in determining the directions of steroid hormone biosynthesis toward biosynthesis of glucocorticoid or sex hormones.
a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 17alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] = 17alpha-hydroxypregnenolone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein reductase] = acetate + androst-4-ene-3,17-dione + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
17alpha-hydroxypregnenolone + O2 + reduced [NADPH--hemoprotein reductase] = 3beta-hydroxyandrost-5-en-17-one + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme catalyzes the ortho-hydroxylation of simple phenols into the corresponding catechols.
It accepts 4-methylphenol, 4-chlorophenol, and 4-fluorophenol as well as 4-nitrophenol, 3-nitrophenol, and resorcinol.
The enzyme is part of a two-component system that also includes an NADH-dependent flavin reductase.
It is strictly dependent on FADH2 and does not accept FMNH2.
FADH2 + O2 + phenol = catechol + FAD + H(+) + H2O.
This bacterial enzyme catalyzes the first two steps in the desulfurization pathway of dibenzothiophenes, the oxidation of dibenzothiophene into dibenzothiophene sulfone via dibenzothiophene-5-oxide.
The enzyme forms a two-component system with EC 1.5.1.42, which also interacts with EC 1.14.14.22.
dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene 5,5-dioxide + 2 FMN + 2 H(+) + 2 H2O.
This bacterial enzyme catalyzes a step in the desulfurization pathway of dibenzothiophenes.
The enzyme forms a two-component system with EC 1.5.1.42, which also interacts with EC 1.14.14.21.
The flavin-N(5)-oxide that is formed by the enzyme reacts spontaneously with NADH to give oxidized flavin, releasing a water molecule.
dibenzothiophene 5,5-dioxide + FMNH2 + NADH + O2 = 2'-hydroxybiphenyl-2-sulfinate + FMN + H(+) + H2O + NAD(+).
Catalyzes the first step in the biosynthesis of bile acids.
The direct electron donor to the enzyme is EC 1.6.2.4.
cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A microsomal enzyme isolated from human and mouse liver that bioactivates vitamin D3.
While multiple isoforms (CYP27A1, CYP2J2/3, CYP3A4, CYP2D25 and CYP2C11) are able to catalyze the reaction in vitro, only CYP2R1 is thought to catalyze the reaction in humans in vivo.
calciol + O2 + reduced [NADPH--hemoprotein reductase] = calcidiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme can also produce 25-hydroxycholesterol.
In addition, it can further hydroxylate the product to 24,25-dihydroxycholesterol and 24,27-dihydroxycholesterol.
This reaction is the first step in the enzymic degradation of cholesterol in the brain as hydroxycholesterol can pass the blood-brain barrier whereas cholesterol cannot.
cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
24-hydroxycholesterol 7alpha-hydroxylase
24-hydroxycholesterol 7alpha-monooxygenase
Found in liver microsomes and in ciliary non-pigmented epithelium.
Specific for (24S)-cholest-5-ene-3beta,24-diol, which is formed mostly in the brain by EC 1.14.14.25.
(24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme, characterized from the bacterium Rhizobium sp. strain MTP-10005, uses FADH2 as a substrate rather than a cofactor.
FADH2 is provided by a dedicated EC 1.5.1.36.
The enzyme participates in the degradation of alpha-resorcylate and resorcinol.
FADH2 + O2 + resorcinol = benzene-1,2,4-triol + FAD + H(+) + H2O.
The enzyme, characterized from the bacterium Geobacillus thermodenitrificans NG80-2, is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols.
The FMNH2 cofactor is provided by an FMN reductase.
a long-chain alkane + FMNH2 + O2 = a long chain fatty alcohol + FMN + H(+) + H2O.
25/26-hydroxycholesterol 7alpha-hydroxylase
25-hydroxycholesterol 7alpha-hydroxylase
25-hydroxycholesterol 7alpha-monooxygenase
27-hydroxycholesterol 7alpha-hydroxylase
Unlike EC 1.14.14.26, which is specific for its oxysterol substrate, this enzyme can also metabolize the oxysterols 24,25-epoxycholesterol, 22-hydroxycholesterol and 24-hydroxycholesterol, but to a lesser extent.
25-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,25-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(25R)-cholest-5-ene-3beta,26-diol + O2 + reduced [NADPH--hemoprotein reductase] = (25R)-cholest-5-en-3beta,7alpha,26-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme, characterized from the bacterium Streptomyces viridifaciens, is part of a two component system that also includes a flavin reductase, which provides reduced flavin mononucleotide for this enzyme.
The enzyme, which is involved in the biosynthesis of the azoxy antibiotic valanimycin, has a similar activity with either FMNH2 or FADH2.
It exhibits broad specificity, and also accepts propan-1-amine, butan-1-amine, butan-2-amine and benzylamine.
2-methylpropan-1-amine + FADH2 + O2 = FAD + 2 H(+) + H2O + N-(2-methylpropyl)hydroxylamine.
2-methylpropan-1-amine + FMNH2 + O2 = FMN + 2 H(+) + H2O + N-(2-methylpropyl)hydroxylamine.
Involved in the insect aggregation pheromone production.
Isolated from the pine engraver beetle, Ips pini.
A small amount of (S)-ipsdienol is also formed.
In vitro it also hydroxylates (+)- and (-)-alpha-pinene, 3-carene, and (+)-limonene, but not alpha-phellandrene, (-)-beta-pinene, gamma-terpinene, or terpinolene.
beta-myrcene + O2 + reduced [NADPH--hemoprotein reductase] = (4R)-ipsdienol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
17alpha-hydroxyprogesterone acetaldehyde-lyase
A microsomal protein that catalyzes two independent reactions at the same active site - the 17-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis (EC 1.14.14.19), and the conversion of the 17-hydroxylated products via a 17,20-lyase reaction to form androstenedione and 3beta-hydroxyandrost-5-en-17-one, leading to sex hormone biosynthesis.
The activity of this reaction is dependent on the allosteric interaction of the enzyme with cytochrome b5 without any transfer of electrons from the cytochrome.
The enzymes from different organisms differ in their substrate specificity; while the enzymes from pig, hamster, and rat accept both 17alpha-hydroxyprogesterone and 17alpha-hydroxypregnenolone, the enzymes from human, bovine, sheep, goat, and bison do not accept the former, and the enzyme from guinea pig does not accept the latter.
ethylenediaminetetraacetate monooxygenase
The enzyme is part of a two component system that also includes EC 1.5.1.42 which provides reduced flavin mononucleotide for this enzyme.
While the enzyme has a substrate overlap with EC 1.14.14.10, it has a much wider substrate range, which includes nitrilotriacetate (NTA) and diethylenetriaminepentaacetate (DTPA) in addition to EDTA.
EDTA + 2 FMNH2 + 2 O2 = ethylenediaminediacetate + 2 FMN + 2 glyoxylate + 3 H(+) + 2 H2O.
The enzyme, characterized from Pseudomonas strains, allows the organisms to utilize methanesulfonate as their sulfur source.
It acts in combination with a dedicated NADH-dependent FMN reductase (EC 1.5.1.42), which provides it with reduced FMN.
FMNH2 + methanesulfonate + O2 = FMN + formaldehyde + 2 H(+) + H2O + sulfite.
The enzyme, characterized from Pseudomonas spp., is involved in a dimethyl sulfide degradation pathway.
It is dependent on NAD(P)H-dependent FMN reductase (EC 1.5.1.38, 1.5.1.39, or 1.5.1.42), which provides it with reduced FMN.
The product, methanesulfinate, is oxidized spontaneously to methanesulfonate in the presence of dioxygen and FMNH2.
dimethyl sulfone + FMNH2 + O2 = FMN + formaldehyde + 2 H(+) + H2O + methanesulfinate.
FMNH2 + methanesulfinate + O2 = FMN + H(+) + H2O + methanesulfonate.
The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin.
In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
L-tyrosine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-4-hydroxyphenylacetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
4-hydroxyphenylacetaldehyde oxime monooxygenase
4-hydroxybenzeneacetaldehyde oxime monooxygenase
cytochrome P450II-dependent monooxygenase
Involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum.
It catalyzes three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
(E)-4-hydroxyphenylacetaldehyde oxime + O2 + reduced [NADPH--hemoprotein reductase] = (S)-4-hydroxymandelonitrile + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
This enzyme catalyzes two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava).
The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime.
It is still not known whether the decarboxylation is spontaneous or catalyzed by the enzyme.
The enzyme can also accept L-isoleucine as substrate, with a lower activity.
L-valine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-2-methylpropanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
This enzyme, found in plants, catalyzes two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin.
The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime.
The enzyme can also accept L-valine, but with a lower activity.
Cf. EC 1.14.14.38, valine N-monooxygenase.
L-isoleucine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (1E,2S)-2-methylbutanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
This enzyme, found in plants, catalyzes two successive N-hydroxylations of L-phenylalanine, a committed step in the biosynthesis of benzylglucosinolate and the cyanogenic glucosides (R)-prunasin and (R)-amygdalin.
The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is labile and undergoes dehydration followed by decarboxylation, producing an oxime.
L-phenylalanine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-phenylacetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
Involved in the biosynthesis of the cyanogenic glucosides lotaustralin and linamarin.
It catalyzes three different activities - isomerization of its substrate the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
(1E,2S)-2-methylbutanal oxime + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-2-methylbutanenitrile + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(E)-2-methylpropanal oxime + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-2-methylpropanenitrile + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Involved in methionine-derived aliphatic glucosinolates biosynthesis.
It catalyzes two successive N-hydroxylations, which are followed by dehydration and decarboxylation.
CYP79F1 from Arabidopsis thaliana can metabolize homo-, di-, tri-, tetra-, penta-, and hexahomomethionine to their corresponding aldoximes, while CYP79F2 from the same plant can only metabolize penta- and hexahomomethionine.
an L-polyhomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = an (E)-omega-(methylsulfanyl)-alkanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
L-dihomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-5-(methylsulfanyl)pentanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
L-trihomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-6-(methylsulfanyl)hexanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
L-tetrahomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-7-(methylsulfanyl)heptanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
L-pentahomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-8-(methylsulfanyl)octanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
L-hexahomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-9-(methylsulfanyl)nonanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
(methylsulfanyl)alkanaldoxime N-monooxygenase
(methylthio)alkanaldoxime N-monooxygenase
Involved in the biosynthesis of glucosinolates in plants.
Catalyzes an N-hydroxylation of the E isomer of n-(methylsulfanyl)aldoximes, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates.
In the absence of a thiol compound, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro intermediate with active site residues.
an (E)-omega-(methylsulfanyl)-alkanal oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-glutathione + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Involved in the biosynthesis of the cyanogenic glucosides (R)-prunasin and (R)-amygdalin.
(E)-phenylacetaldehyde oxime + O2 + reduced [NADPH--hemoprotein reductase] = (R)-mandelonitrile + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme catalyzes the N-hydroxylation of aromatic aldoximes derived from L-tryptophan and L-phenylalanine, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates.
In the absence of glutathione, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro compound with catalytic residues in the active site.
(E)-(indol-3-yl)acetaldehyde oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = (E)-1-(glutathione-S-yl)-2-(1H-indol-3-yl)acetohydroximate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(E)-phenylacetaldehyde oxime + glutathione + O2 + reduced [NADPH--hemoprotein reductase] = (Z)-1-(glutathione-S-yl)-2-phenylacetohydroximate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
pimeloyl-[acyl-carrier protein] synthase
Catalyzes an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin.
The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal.
The mechanism is similar to EC 1.14.15.6, followed by a hydroxylation step, which may occur spontaneously.
a C2-C8-saturated long-chain fatty acyl-[ACP] + 3 O2 + 2 reduced [flavodoxin] = 6-carboxyhexanoyl-[ACP] + a fatty aldehyde + 3 H(+) + 3 H2O + 2 oxidized [flavodoxin].
The enzyme, found in bacteria and archaea, consist of only an oxygenase domain and functions together with bacterial ferredoxins or flavodoxins.
The orthologous enzymes from plants and animals also contain a reductase domain and use only NADPH as the electron donor (cf. EC 1.14.13.39).
2 L-arginine + 4 O2 + 3 reduced [flavodoxin] = 5 H(+) + 4 H2O + 2 L-citrulline + 2 nitric oxide + 3 oxidized [flavodoxin].
The enzyme, found in plants, acts on jasmonoyl-L-amino conjugates, catalyzing the hydroxylation of the C-12 position of the jasmonic acid chain.
While the best studied substrate is (+)-7-epi-jasmonoyl-L-isoleucine, the enzyme was shown to be active with jasmonoyl-L-valine and jasmonoyl-L-phenylalanine, and is likely to be active with other jasmonoyl-amino acid conjugates.
a jasmonyl-L-amino acid + O2 + reduced [NADPH--hemoprotein reductase] = a 12-hydroxyjasmonyl-L-alpha-amino acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
12-hydroxyjasmonoyl-L-amino acid 12-hydroxylase
The enzyme, found in plants, acts on jasmonoyl-L-amino conjugates that have been hydroxylated at the C-12 position of the jasmonic acid chain by EC 1.14.14.48 further oxidizing that position to a carboxylate via an aldehyde intermediate.
While the best studied substrate is (+)-7-iso-jasmonoyl-L-isoleucine, the enzyme was shown to be active with jasmonoyl-L-phenylalanine, and is likely to be active with other jasmonoyl-amino acid conjugates.
a 12-hydroxyjasmonyl-L-alpha-amino acid + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = a 12-hydroxy-12-oxojasmonyl-L-alpha-amino acid + 3 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
This cytochrome P-450 enzyme acts on 16-methoxytabersonine, leading to biosynthesis of vindoline in the plant Catharanthus roseus (Madagascar periwinkle).
It can also act on tabersonine, resulting in the production of small amounts of vindorosine.
The products are unstable and, in the absence of EC 1.1.99.41 will convert into 3-epoxylated compounds.
16-methoxytabersonine + O2 + reduced [NADPH--hemoprotein reductase] = (3R)-1,2-didehydro-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase] = (3R)-1,2-didehydro-3-hydroxy-2,3-dihydrotabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme participates in the biosynthesis of (-)-carvone, which is responsible for the aroma of spearmint.
(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] = (1S,5R)-carveol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme, characterized from the plant Perilla frutescens, participates in the biosynthesis of perillyl aldehyde, the major constituent of the essential oil that accumulates in the glandular trichomes of this plant.
Some forms of the enzyme also catalyze the oxidation of (-)-perillyl alcohol to (-)-perillyl aldehyde.
(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] = (4S)-perillyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The reaction is stereospecific with over 95% yield of (+)-trans-carveol from (R)-limonene.
(S)-Limonene, the substrate for EC 1.14.14.51 is not a substrate.
Forms part of the carvone biosynthesis pathway in Carum carvi (caraway) seeds.
(4R)-limonene + O2 + reduced [NADPH--hemoprotein reductase] = (1R,5S)-carveol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This cytochrome P450 enzyme, found in Aspergillus nidulans, is involved in the degradation of phenylacetate.
2-phenylacetate + O2 + reduced [NADPH--hemoprotein reductase] = (2-hydroxyphenyl)acetate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + quinine + reduced [NADPH--hemoprotein reductase] = 3-hydroxyquinine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including stereoids, fatty acids, and xenobiotics.
1,8-cineole + O2 + reduced [NADPH--hemoprotein reductase] = 2-exo-hydroxy-1,8-cineole + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
taurochenodeoxycholate 6alpha-hydroxylase
taurochenodeoxycholate 6alpha-monooxygenase
Requires cytochrome b5 for maximal activity.
Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate.
In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid.
O2 + reduced [NADPH--hemoprotein reductase] + taurochenodeoxycholate = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + taurohyocholate.
lithocholate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + hyodeoxycholate + oxidized [NADPH--hemoprotein reductase].
Isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize).
It forms this C16 homoterpene in response to herbivore attack.
In vitro some variants of the enzyme also convert (3S,6E)-nerolidol to (3E)-4,8-dimethylnona-1,3,7-triene (see EC 1.14.14.59).
(6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
It forms this C11 homoterpene in response to herbivore attack.
In vitro the enzyme also converts (6E,10E)-geranyllinalool to (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (see EC 1.14.14.58).
(3S,6E)-nerolidol + O2 + reduced [NADPH--hemoprotein reductase] = (3E)-4,8-dimethylnona-1,3,7-triene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Isolated from the plants Salvia pomifera (apple sage) and Salvia miltiorrhiza (danshen).
11-hydroxyferruginol is a precursor of carnosic acid, a potent antioxidant.
ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Isolated from the plants Salvia pomifera (apple sage), S. miltiorrhiza (red sage), S. fruticosa (Greek sage) and Rosmarinus officinalis (Rosemary).
11-hydroxyferruginol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = carnosate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
Isolated from the plant Salvia pomifera (apple sage).
ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + salviol.
A cytochrome P450 (heme-thiolate) protein isolated from the plant Platycodon grandiflorus (baloon flower).
The enzyme is also able to oxidize oleanolic acid to cochalic acid.
beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + maniladiol + oxidized [NADPH--hemoprotein reductase].
O2 + oleanolate + reduced [NADPH--hemoprotein reductase] = cochalate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the plant Solanum lycopersicum (tomato).
beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = daturadiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Isolated from the plant Salvia miltiorrhiza (danshen).
The enzyme also oxidizes 11-hydroxyferruginol to 11-hydroxysugiol.
It also oxidizes at C-12 of ferruginol (EC 1.14.14.60).
ferruginol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] + sugiol.
11-hydroxyferruginol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-hydroxysugiol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
Involved in psoralen biosynthesis, see EC 1.14.13.102.
demethylsuberosin + O2 + reduced [NADPH--hemoprotein reductase] = (7S)-marmesin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the plant Salvia miltiorrhiza (danshen).
The enzyme also oxidizes 11-hydroxyferruginol to 11,20-dihydroxyferruginol.
11-hydroxysugiol + O2 + reduced [NADPH--hemoprotein reductase] = 11,20-dihydroxysugiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
11-hydroxyferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11,20-dihydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from rice, Oryza sativa.
9beta-pimara-7,15-diene + O2 + reduced [NADPH--hemoprotein reductase] = 9beta-pimara-7,15-diene-3beta-ol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the plant Oryza sativa (rice) that is involved in phytocassanes biosynthesis.
Depending on the order of activities, the enzyme may form either ent-cassa-12,15-dien-2-one or ent-cassa-12,15-diene-2beta,3beta-diol as an intermediate.
ent-cassa-12,15-diene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = ent-3beta-hydroxycassa-12,15-dien-2-one + 3 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from Oryza sativa (rice).
Participates in the pathway for the biosynthesis of oryzalexins, a group of related phytoalexins produced by rice.
Can also use 9beta-pimara-7,15-diene as substrate (cf. EC 1.14.14.68, syn-pimaradiene 3-monooxygenase).
ent-sandaracopimara-8(14),15-diene + O2 + reduced [NADPH--hemoprotein reductase] = ent-sandaracopimaradien-3beta-ol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Isolated from the plant Siraitia grosvenorii (monk fruit).
cucurbitadienol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxocucurbitadienol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the plant Persicaria hydropiper (water pepper).
(5S,9S,10S)-drim-7-en-11-ol + O2 + reduced [NADPH--hemoprotein reductase] = (5S,10S)-(9R)-7-drimene-11,12-diol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
albendazole monooxygenase (sufoxide-forming)
This is one of the activities carried out by some microsomal cytochrome P450 monooxygenases.
A similar conversion is also carried out by a different microsomal enzyme (EC 1.14.13.32), but it is estimated that cytochrome P450s are responsible for 70% of the activity.
albendazole + O2 + reduced [NADPH--hemoprotein reductase] = albendazole S-oxide + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
fenbendazole + O2 + reduced [NADPH--hemoprotein reductase] = fenbendazole S-oxide + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
albendazole monooxygenase (hydroxylating)
CYP2J2 is a microsomal cytochrome P450 monooxygenase that catalyzes the hydroxylation of the terminal carbon of the propylsulfanyl chain in albendazole, a broad-spectrum anthelmintic used against gastrointestinal nematodes and the larval stages of cestodes.
albendazole + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + hydroxyalbendazole + oxidized [NADPH--hemoprotein reductase].
fenbendazole monooxygenase (4'-hydroxylating)
CYP2C19 is microsomal cytochrome P450 monooxygenase that catalyzes the hydroxylation of the benzene ring of fenbendazole, a broad-spectrum anthelmintic used against gastrointestinal nematodes and the larval stages of cestodes.
This activity is also carried out by CYP2J2.
fenbendazole + O2 + reduced [NADPH--hemoprotein reductase] = 4'-hydroxyfenbendazole + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This cytochrome P450 (heme thiolate) enzyme has been characterized from the plant Oryza sativa (rice).
It may be involved in production of oryzadione.
ent-isokaurene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = ent-isokaurene-2beta,3beta-diol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase].
The enzyme has been characterized from the cyanogenic millipede Chamberlinius hualienensis.
Unlike plant enzymes that can catalyze this reaction (EC 1.14.14.44), this enzyme cannot act on phenylacetaldehyde oximes.
It can accept (4-hydroxyphenyl)acetonitrile, (2-methylphenyl)acetonitrile, and (3-methylphenyl)acetonitrile as substrates at a lower rate.
O2 + phenylacetonitrile + reduced [NADPH--hemoprotein reductase] = (R)-mandelonitrile + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from human tissue.
The enzyme will also act on menaquinone-4.
Prolonged action of CYP4F2, but not CYP4F11, on the omega hydroxyl group oxidizes it to the corresponding carboxylic acid.
CYP4F2 also oxidizes leukotriene B4; see EC 1.14.13.30.
O2 + phylloquinone + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + omega-hydroxyphylloquinone + oxidized [NADPH--hemoprotein reductase].
menaquinone-4 + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + omega-hydroxymenaquinone-4 + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from human eye tissue.
Defects in the enzyme are associated with Bietti crystalline corneoretinal dystrophy.
The enzyme also produces some 21-hydroxydocosahexaenoate.
Acts in a similar way on icosapentaenoic acid.
(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
long-chain fatty acid omega-monooxygenase
A cytochrome P450 (heme thiolate) enzyme.
The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1).
The plant enzyme CYP86A1 also acts on laurate (12:0).
The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (omega-1) position.
The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).
an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + octadecanoate + reduced [NADPH--hemoprotein reductase] = 18-hydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein found in plants.
The 3',5'-dihydroxyflavanone is formed via the 3'-hydroxyflavanone.
In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin).
The enzyme catalyzes the hydroxylation of 5,7,4'-trihydroxyflavanone (naringenin) at either the 3' position to form eriodictyol or at both the 3' and 5' positions to form 5,7,3',4',5'-pentahydroxyflavanone (dihydrotricetin).
The enzyme also catalyzes the hydroxylation of 3,5,7,3',4'-pentahydroxyflavanone (taxifolin) at the 5' position, forming ampelopsin.
a 3',5'-unsubstituted flavanone + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = a 3',5'-dihydroxyflavanone + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase].
Acts on a number of flavonoids, including the flavanone naringenin and the flavone apigenin.
Does not act on 4-coumarate or 4-coumaroyl-CoA.
a 3'-unsubstituted flavone + O2 + reduced [NADPH--hemoprotein reductase] = a 3'-hydroxyflavone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme thiolate) protein found in plants.
Also hydroxylates nerol and citronellol, cf. EC 1.14.14.84.
The recommended numbering of geraniol gives 8-hydroxygeraniol as the product rather than 10-hydroxygeraniol.
The cloned enzyme also catalyzed, but less efficiently, the 3'-hydroxylation of naringenin (cf. EC 1.14.14.82).
(2E)-geraniol + O2 + reduced [NADPH--hemoprotein reductase] = (6E)-8-hydroxygeraniol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.
linalool + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (6E)-8-oxolinalool + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
7-deoxyloganate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + loganate + oxidized [NADPH--hemoprotein reductase].
7-deoxyloganin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + loganin + oxidized [NADPH--hemoprotein reductase].
Catalyzes three successive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid.
ent-kaur-16-ene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = ent-kaur-16-en-19-oate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
The reaction involves the migration of the 2-phenyl group of the flavanone to the 3-position of the isoflavanone.
The 2-hydroxyl group is derived from the oxygen molecule.
EC 4.2.1.105 acts on the products with loss of water and formation of genistein and daidzein, respectively.
liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] = (2R,3S)-2,4',7-trihydroxyisoflavanone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(2S)-naringenin + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-2,3-dihydrogenistein + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein.
Also acts on biochanin A and other isoflavones with a 4'-methoxy group.
formononetin + O2 + reduced [NADPH--hemoprotein reductase] = calycosin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Acts on isoflavones with a 4'-methoxy group, such as formononetin and biochanin A.
EC 1.14.14.90 is less specific and acts on other isoflavones as well as 4'-methoxyisoflavones.
formononetin + O2 + reduced [NADPH--hemoprotein reductase] = 2'-hydroxyformononetin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Acts on daidzein, formononetin and genistein.
EC 1.14.14.89 has the same reaction but is more specific as it requires a 4'-methoxyisoflavone.
a 2'-unsubstituted isoflavone + O2 + reduced [NADPH--hemoprotein reductase] = a 2'-hydroxyisoflavone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
daidzein + O2 + reduced [NADPH--hemoprotein reductase] = 2'-hydroxydaidzein + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
genistein + O2 + reduced [NADPH--hemoprotein reductase] = 2'-hydroxygenistein + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme is involved in flavonoid biosynthesis.
(E)-cinnamate + O2 + reduced [NADPH--hemoprotein reductase] = (E)-4-coumarate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein found in Aspergillus fungi.
benzoate + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxybenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
3,9-dihydroxypterocarpan 6a-monooxygenase
A cytochrome P450 (heme-thiolate) protein found in soybean.
The product of the reaction is the biosynthetic precursor of the glyceollin phytoalexins.
(6aR,11aR)-3,9-dihydroxypterocarpan + O2 + reduced [NADPH--hemoprotein reductase] = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein found in mammals.
leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This plant enzyme catalyzes three steps in a pathway that leads to the biosynthesis of many sesquiterpenoid lactones.
(+)-(R)-germacrene A + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-oate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase
A cytochrome P450 (heme-thiolate) protein, found in plants.
It also acts on trans-5-O-(4-coumaroyl)shikimate.
O2 + reduced [NADPH--hemoprotein reductase] + trans-5-O-(4-coumaroyl)-D-quinate = 5-O-[(E)-caffeoyl]-D-quinate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
methyltetrahydroprotoberberine 14-monooxygenase
methyltetrahydroprotoberberine 14-hydroxylase
(S)-N-methylcanadine + O2 + reduced [NADPH--hemoprotein reductase] = allocryptopine + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein involved in benzophenanthridine alkaloid synthesis in higher plants.
O2 + protopine + reduced [NADPH--hemoprotein reductase] = 6-hydroxyprotopine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from peppermint (Mentha piperita).
(4S)-limonene + O2 + reduced [NADPH--hemoprotein reductase] = (1S,6R)-isopiperitenol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
dihydrosanguinarine + O2 + reduced [NADPH--hemoprotein reductase] = 10-hydroxydihydrosanguinarine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from the plant Thalictrum bulgaricum.
dihydrochelirubine + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydihydrochelirubine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein involved in benzylisoquinoline alkaloid synthesis in higher plants.
(S)-N-methylcoclaurine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-3'-hydroxy-N-methylcoclaurine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from the plant Madagascar periwinkle (Catharanthus roseus).
(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxytabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from the plant Rauvolfia serpentina.
Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
O2 + reduced [NADPH--hemoprotein reductase] + vinorine = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + vomilenine.
This microsomal cytochrome-P450 (heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
O2 + reduced [NADPH--hemoprotein reductase] + taxa-4(20),11-dien-5alpha-yl acetate = 10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This cytochrome-P450(heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
O2 + reduced [NADPH--hemoprotein reductase] + taxa-4(20),11-dien-5alpha-ol = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + taxa-4(20),11-dien-5alpha,13alpha-diol.
A cytochrome P450 (heme-thiolate) protein from plants.
Catalyzes three sucessive oxidations of ent-kaurenoic acid.
The second step includes a ring-B contraction giving the gibbane skeleton.
In pumpkin (Cucurbita maxima) ent-6alpha,7alpha-dihydroxykaur-16-en-19-oate is also formed.
ent-kaur-16-en-19-oate + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = gibberellin A12 + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
2,5-diketocamphane 1,2-monooxygenase oxygenating component
A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid.
Involved in the degradation of (+)-camphor.
Requires a dedicated NADH-FMN reductase (cf. EC 1.5.1.42).
Can accept several bicyclic ketones including (+)- and (-)-camphor and adamantanone.
The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
(1R,4R)-bornane-2,5-dione + FMNH2 + O2 = (1R,4R)-5-oxo-1,2-campholide + FMN + H(+) + H2O.
(1R,4R)-5-oxo-1,2-campholide = [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-en-1-yl]acetate + H(+).
The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
3-hydroxyindolin-2-one + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
2-hydroxy-1,4-benzoxazin-3-one monooxygenase
2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + O2 + reduced [NADPH--hemoprotein reductase] = DIBOA + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the phytoalexin momilactone.
It also acts similarly on 9beta-stemod-13(17)-ene.
9beta-pimara-7,15-diene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 9beta-pimara-7,15-dien-19-oate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the antifungal phytocassanes.
ent-cassa-12,15-diene + O2 + reduced [NADPH--hemoprotein reductase] = ent-11beta-hydroxycassa-12,15-diene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The recommended numbering of humulene gives 10-hydroxy-alpha-humulene as the product rather than 8-hydroxy-alpha-humulene as used by the literature.
alpha-humulene + O2 + reduced [NADPH--hemoprotein reductase] = 10-hydroxy-alpha-humulene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Cloned from the plant Artemisia annua (sweet wormwood).
Part of the biosynthetic pathway of artemisinin.
(+)-amorpha-4,11-diene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = (+)-artemisinate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
The enzyme from the plant Glycyrrhiza uralensis (licorice) is involved in the biosynthesis of the triterpenoid saponin glycyrrhizin.
The enzyme from the plant Medicago truncatula can also hydroxylate beta-amyrin.
11-oxo-beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = glycyrrhetinate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the saprophytic mold Aspergillus parasiticus.
(1'S)-averantin + O2 + reduced [NADPH--hemoprotein reductase] = (1'S,5'R)-5'-hydroxyaverantin + H2O + oxidized [NADPH--hemoprotein reductase].
(1'S)-averantin + O2 + reduced [NADPH--hemoprotein reductase] = (1'S,5'S)-5'-hydroxyaverantin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the mold Aspergillus parasiticus.
8-O-methylsterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B1 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase].
8-O-methyldihydrosterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B2 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase].
Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, fumitremorgins and verruculogen.
O2 + reduced [NADPH--hemoprotein reductase] + tryprostatin B = 6-hydroxytryprostatin B + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
Involved in the biosynthetic pathway of the indole alkaloid verruculogen.
fumitremorgin C + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 12alpha,13alpha-dihydroxyfumitremorgin C + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from ginseng (Panax ginseng).
Involved in the biosynthetic pathway of ginsenosides.
dammarenediol-II + O2 + reduced [NADPH--hemoprotein reductase] = (20S)-protopanaxadiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the rhizomes of ginseng (Panax ginseng).
(20S)-protopanaxadiol + O2 + reduced [NADPH--hemoprotein reductase] = (20S)-protopanaxatriol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
ent-sandaracopimaradien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oryzalexin E + oxidized [NADPH--hemoprotein reductase].
ent-sandaracopimaradien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oryzalexin D + oxidized [NADPH--hemoprotein reductase].
The dehydration of 3alpha-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous.
The enzyme from fungi also catalyzes the reaction of EC 1.14.14.125.
dihydromonacolin L carboxylate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + monacolin L carboxylate + oxidized [NADPH--hemoprotein reductase].
The enzyme from fungi also catalyzes the reaction of EC 1.14.14.124.
monacolin L carboxylate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + monacolin J carboxylate + oxidized [NADPH--hemoprotein reductase].
The enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro.
The enzyme from Medicago truncatula (barrel medic) (CYP716A12) can also convert alpha-amyrin and lupeol to ursolic acid and betulinic acid, respectively.
The enzyme from Maesa lanceolata (false assegai) (CYP16A75) does not catalyze the reaction to completion, resulting in accumulation of both intermediates.
beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4 H(+) + 4 H2O + oleanolate + 3 oxidized [NADPH--hemoprotein reductase].
The enzyme, found in insects except for Lepidoptera (moths and butterflies) is specific for methyl farnesoate (cf. EC 1.14.14.128).
methyl (2E,6E)-farnesoate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + juvenile hormone III + oxidized [NADPH--hemoprotein reductase].
The enzyme, found in Lepidoptera (moths and butterflies), is specific for farnesoate (cf. EC 1.14.14.127).
It is involved in the synthesis of juvenile hormone.
(2E,6E)-farnesoate + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + juvenile hormone III carboxylate + oxidized [NADPH--hemoprotein reductase].
The enzymes from solanaceous plants are involved in the biosynthesis of stigmatic estolide, a lipid-based polyester that forms a major component of the exudate.
(9Z)-octadecenoyl-CoA + O2 + reduced [NADPH--hemoprotein reductase] = (9Z)-18-hydroxyoctadecenoyl-CoA + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(9Z,12Z)-octadecadienoyl-CoA + O2 + reduced [NADPH--hemoprotein reductase] = (9Z,12Z)-18-hydroxyoctadecadienoyl-CoA + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme is involved in the synthesis of sporopollenin - a complex polymer found at the outer layer of spores and pollen.
It can also act on decanoate (C10), myristate (C14), and palmitate (C16) with lower activity.
The enzyme also produces a small amount of products that are hydroxylated at neighboring positions (C-6, C-8 and C-9).
dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 7-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein characterized from the plant Sinopodophyllum hexandrum.
The enzyme is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
(-)-bursehernin + O2 + reduced [NADPH--hemoprotein reductase] = (-)-5'-demethylyatein + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(-)-4'-demethyl-deoxypodophyllotoxin 4-hydroxylase
The enzyme produces the direct precursor to etoposide, a potent anticancer drug.
It can also act on (-)-deoxypodophyllotoxin with lower efficiency.
(-)-4'-desmethyl-deoxypodophyllotoxin + O2 + reduced [NADPH--hemoprotein reductase] = 4'-demethylepipodophyllotoxin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein that uses a flavodoxin-like redox partner to reduce the heme iron.
Isolated from the bacterium Citrobacter braakii, which can use 1,8-cineole as the sole source of carbon.
1,8-cineole + O2 + reduced [flavodoxin] = 2-endo-hydroxy-1,8-cineole + H(+) + H2O + oxidized [flavodoxin].
A cytochrome P450 (heme-thiolate) protein found in plants and participates in the biosynthesis of soybean saponins.
beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = 24-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + reduced [NADPH--hemoprotein reductase] + sophoradiol = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + soyasapogenol B.
dimethylallyl-3,6a,9-trihydroxypterocarpan cyclase
A cytochrome p-450 (heme-thiolate) protein purified from soybean.
(6aS,11aS)-2-dimethylallyl-3,6a,9-trihydroxypterocarpan + O2 + reduced [NADPH--hemoprotein reductase] = glyceollin II + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(6aS,11aS)-2-dimethylallyl-3,6a,9-trihydroxypterocarpan + O2 + reduced [NADPH--hemoprotein reductase] = glyceollin III + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(6aS,11aS)-4-dimethylallyl-3,6a,9-trihydroxypterocarpan + O2 + reduced [NADPH--hemoprotein reductase] = glyceollin I + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
A cytohrome P450 (heme-thiolate) protein isolated from the plant Rauvolfia serpentina.
10-deoxysarpagine + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + sarpagine.
Catalyzes the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone.
CO inhibits the reaction, but its effects can be reversed by the presence of blue light.
The 8'-hydroxyabscisate formed can be converted into (-)-phaseic acid, most probably spontaneously.
2-cis-(+)-abscisate + O2 + reduced [NADPH--hemoprotein reductase] = (+)-8'-hydroxyabscisate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from Mesocricetus auratus (golden hamster).
Expression of the gene for this enzyme is 50-fold higher in male compared to female hamsters.
lithocholate + O2 + reduced [NADPH--hemoprotein reductase] = 6beta-hydroxylithocholate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase
5beta-cholestane-3alpha,7alpha-diol 12alpha-monooxygenase
7alpha-hydroxy-4-cholesten-3-one 12alpha-monooxygenase
7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase
This is the key enzyme in the biosynthesis of the bile acid cholate.
The enzyme can also hydroxylate 5beta-cholestane-3alpha,7alpha-diol at the 25 and 26 position, but to a lesser extent.
5beta-cholestane-3alpha,7alpha-diol + O2 + reduced [NADPH--hemoprotein reductase] = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
7alpha-hydroxycholest-4-en-3-one + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
chenodeoxycholate + O2 + reduced [NADPH--hemoprotein reductase] = cholate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from licorice plants (Glycyrrhiza echinata L.).
The immediate product is likely 2-hydroxyliquiritigenin, which spontaneously rearranges to form licodione.
liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + licodione + oxidized [NADPH--hemoprotein reductase].
This microsomal cytochrome P450 (heme-thiolate) enzyme is rather specific for (+)-marmesin, although it can also accept 5-hydroxymarmesin to a much lesser extent.
Furanocoumarins protect plants from fungal invasion and herbivore attack.
(+)-columbianetin, the angular furanocoumarin analog of the linear furanocoumarin (+)-marmesin, acts as a competitive inhibitor even though it is not a substrate.
(7S)-marmesin + O2 + reduced [NADPH--hemoprotein reductase] = acetone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + psoralen.
8-dimethylallylnaringenin 2'-hydroxylase
A membrane-bound cytochrome P450 (heme-thiolate) protein that is associated with the endoplasmic reticulum.
This enzyme is specific for sophoraflavanone B as substrate.
Along with EC 2.5.1.70 and EC 2.5.1.71, this enzyme forms part of the sophoraflavanone G biosynthetic pathway.
O2 + reduced [NADPH--hemoprotein reductase] + sophoraflavanone B = H(+) + H2O + leachianone G + oxidized [NADPH--hemoprotein reductase].
The conversion of substrate into product involves the hydroxylation of the syn-methyl (C9), intramolecular cyclization to the hemiketal and dehydration to the furan.
This is the second cytochrome P450-mediated step of monoterpene metabolism in peppermint, with the other step being catalyzed by EC 1.14.14.99.
(R)-pulegone + O2 + reduced [NADPH--hemoprotein reductase] = (R)-menthofuran + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
This enzyme catalyzes a step in the pathway of abietic acid biosynthesis.
The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine).
Activity is induced by wounding of the plant tissue.
abieta-7,13-diene + O2 + reduced [NADPH--hemoprotein reductase] = abieta-7,13-dien-18-ol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine), and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine).
The recombinant enzyme catalyzes the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal.
abieta-7,13-dien-18-ol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = abieta-7,13-dien-18-oate + 3 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the plant Croton sublyratus.
(2E,6E,10E)-geranylgeraniol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + plaunotol.
3-epi-6-deoxocathasterone 23-monooxygenase
A cytochrome P450 (heme-thiolate) protein involved in brassinosteroid biosynthesis in plants.
The enzyme has a relaxed substrate specificity, and C-23 hydroxylation can occur at different stages in the pathway.
In Arabidopsis thaliana two isozymes, encoded by the CYP90C1 and CYP90D1 genes, have redundant activities.
3-epi-6-deoxocathasterone + O2 + reduced [NADPH--hemoprotein reductase] = 6-deoxotyphasterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(22S,24R)-22-hydroxy-5alpha-ergostan-3-one + O2 + reduced [NADPH--hemoprotein reductase] = 3-dehydro-6-deoxoteasterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This cytochrome P450 (heme-thiolate) enzyme from wild parsnip is involved in the formation of angular furanocoumarins.
Attacks its substrate by syn-elimination of hydrogen from C-3'.
(S)-columbianetin + O2 + reduced [NADPH--hemoprotein reductase] = acetone + angelicin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Kinetic studies suggest that 1beta-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3.
However the reverse order via 3alpha-hydroxyepiaristolochene does occur.
(+)-5-epi-aristolochene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = capsidiol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from chicory plants.
The enzyme hydroxylates carbon C-6 of germacra-1(10),4,11(13)-trien-12-oate to give 6alpha-hydroxygermacra-1(10),4,11(13)-trien-12-oate, which spontaneously cyclises to form the lactone ring.
germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = (+)-costunolide + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Hyoscymus muticus premnaspirodiene oxygenase
The enzyme from the plant Hyoscymus muticus also hydroxylates valencene at C-2 to give the alpha-hydroxy compound, nootkatol, and this is converted into nootkatone.
5-Epiaristolochene and epieremophilene are hydroxylated at C-2 to give a 2beta-hydroxy derivatives that are not oxidized further.
(-)-vetispiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] + solavetivone.
(+)-valencene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (+)-nootkatone + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
(+)-5-epi-aristolochene + O2 + reduced [NADPH--hemoprotein reductase] = 2beta-hydroxy-5-epi-aristolochene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
4-epi-eremophilene + O2 + reduced [NADPH--hemoprotein reductase] = 4-epi-eremophilene-2beta-ol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from the plant Glycyrrhiza uralensis (Chinese licorice) that participates in the glycyrrhizin biosynthesis pathway.
The enzyme is also able to oxidize 30-hydroxy-beta-amyrin to 11alpha,30-dihydroxy-beta-amyrin but this is not thought to be part of glycyrrhizin biosynthesis.
beta-amyrin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxo-beta-amyrin + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
indole + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + indolin-2-one + oxidized [NADPH--hemoprotein reductase].
This cytochrome P450 (heme-thiolate) enzyme acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol.
The enzyme catalyzes a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
3 O2 + obtusifoliol + 3 reduced [NADPH--hemoprotein reductase] = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
Involved in the degradation of (-)-camphor.
Requires a dedicated NADH--FMN reductase (cf. EC 1.5.1.42).
(1S,4S)-bornane-2,5-dione + FMNH2 + O2 = (1S,4S)-5-oxo-1,2-campholide + FMN + H(+) + H2O.
A cytochrome P450 (heme-thiolate) protein from the plant Arabidopsis thaliana.
This enzyme catalyzes two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin.
The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously.
The dehydrated product is then subject to a decarboxylation that produces an oxime.
L-tryptophan + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-(indol-3-yl)acetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase].
indolin-2-one + O2 + reduced [NADPH--hemoprotein reductase] = 3-hydroxyindolin-2-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome heme-thiolate protein (P450).
alpha-carotene + O2 + reduced [NADPH--hemoprotein reductase] = alpha-cryptoxanthin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + reduced [NADPH--hemoprotein reductase] + zeinoxanthin = H(+) + H2O + lutein + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme thiolate) enzyme characterized from maize.
The enzyme catalyzes the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3.
dolabradiene + O2 + reduced [NADPH--hemoprotein reductase] = 15,16-epoxydolabrene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
15,16-epoxydolabrene + O2 + reduced [NADPH--hemoprotein reductase] = 3beta-hydroxy-15,16-epoxydolabrene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme sequentially oxidizes(S)-beta-macrocarpene via alcohol and aldehyde intermediates to form zealexin A1, a maize phytoalexin that provides biochemical protection against fungal infection.
(S)-beta-macrocarpene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] + zealexin A1.
The enzyme, characterized from the plant Catharanthus roseus, is a cytochrome P450 (heme thiolate) protein.
It catalyzes three successive reactions in the pathway leading to biosynthesis of monoterpenoid indole alkaloids.
(+)-cis-trans-nepetalactol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 7-deoxyloganetate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme thiolate) protein characterized from rice, where it catalyzes the first step in C-glycosylation of multiple flavanones such as (2S)-naringenin, (2S)-eriodictyol, and (2S)-pinocembrin.
a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a 2-hydroxyflavanone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(S)-1-hydroxy-N-methylcanadine 13-hydroxylase
The enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.
(S)-1-hydroxy-N-methylcanadine + O2 + reduced [NADPH--hemoprotein reductase] = (13S,14R)-1,13-dihydroxy-N-methylcanadine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
fraxetin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + sideretin (reduced form).
A cytochrome P450 (heme-thiolate) protein characterized from the plant Arabidopsis thaliana.
Involved in biosynthesis of small cyanogenic compounds that take part in pathogen defense.
The enzyme also catalyzes the 5-hydroxylation of xanthotoxin.
indole-3-carbonyl nitrile + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-indole-3-carbonyl nitrile + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This cytochrome P450 (heme-thiolate) enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.
(S)-N-methylcanadine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-1-hydroxy-N-methylcanadine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
(13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine 8-hydroxylase
(13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + O2 + reduced [NADPH--hemoprotein reductase] = (13S,14R)-13-O-acetyl-1,8-dihydroxy-N-methylcanadine + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from the plant Helianthus annuus (common sunflower).
The cyclisation of 8beta-hydroxygermacra-1(10),4,11(13)-triene-12-oate to inunolide (12,8beta) does not seem to occur spontaneously.
The enzyme from Inula hupehensis also forms some 8alpha-hydroxygermacra-1(10),4,11(13)-triene-12-oate, which spontaneously cyclises to 8-epi-inunolide (12,8alpha) (cf. EC 1.14.14.170).
germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8beta-hydroxygermacra-1(10),4,11(13)-trien-12-oate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
8beta-hydroxygermacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = eupatolide + 2 H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein from the plant Inula hupehensis.
The enzyme also produces 8beta-hydroxygermacra-1(10),4,11(13)-triene-12-oate (EC 1.14.14.168).
germacra-1(10),4,11(13)-trien-12-oate + O2 + reduced [NADPH--hemoprotein reductase] = 8-epi-inunolide + 2 H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) protein isolated from the plant Maesa lanceolata (false assegai).
Involved in the biosynthesis of maesasaponins.
It also acts on some derivatives of beta-amyrin such as erythrodiol or oleanolic acid.
beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = 16alpha-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
3,5,6-trichloropyridin-2-ol monooxygenase
The enzyme, characterized from a number of bacterial species, participates in the degradation of 3,5,6-trichloropyridin-2-ol (TCP), a metabolite of the common organophosphorus insecticide chlorpyrifos.
The enzyme is a multifunctional flavin-dependent monooxygenase that displaces three chlorine atoms by attacking three different positions in the substrate.
Each reaction catalyzed by the enzyme displaces a single chlorine and results in formation of a dione, which must be reduced by FADH2 before the monooxygenase could catalyze the next step.
The large amount of FADH2 that is required is generated by a dedicated flavin reductase (TcpX).
3,5,6-trichloropyridin-2-ol + FADH2 + O2 = 3,6-dichloropyridine-2,5-dione + chloride + FAD + 2 H(+) + H2O.
3,6-dichloropyridine-2,5-diol + FADH2 + O2 = 6-chloro-3-hydroxypyridine-2,5-dione + chloride + FAD + 2 H(+) + H2O.
6-chloropyridine-2,3,5-triol + FADH2 + O2 = 3,6-dihydroxypyridine-2,5-dione + chloride + FAD + 3 H(+) + H2O.
The enzyme, characterized from a number of bacterial species, participates in the degradation of 2,4,6-trichlorophenol, a compound that has been used for decades as a wood preservative.
The enzyme is a multifunctional flavin-dependent monooxygenase that displaces two chlorine atoms by attacking two different positions in the substrate.
Each reaction catalyzed by the enzyme displaces a single chlorine and results in formation of a dione, which must be reduced by FADH2 before the monooxygenase could catalyze the second reaction.
The large amount of FADH2 that is required is generated by a dedicated flavin reductase (TcpB).
2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichlorobenzoquinone + chloride + FAD + H(+) + H2O.
2,6-dichlorohydroquinone + FADH2 + O2 = 2-chloro-6-hydroxy-1,4-benzoquinone + chloride + FAD + 2 H(+) + H2O.
A cytochrome P450 (heme-thiolate) protein found in plants, where it is part of the biosynthesis pathway of the red naphthoquinone pigment shikonin.
geranylhydroquinone + O2 + reduced [NADPH--hemoprotein reductase] = 3''-hydroxygeranylhydroquinone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme thiolate) enzyme found in some members of the Lamiaceae (mint family).
The enzyme from Rosmarinus officinalis (rosemary) is involved in biosynthesis of carnosic acid, while the enzyme from the Chinese medicinal herb Salvia miltiorrhiza is involved in the biosynthesis of the tanshinones, abietane-type norditerpenoid naphthoquinones that are the main lipophilic bioactive components found in the plant.
abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
This microsomal cytochrome-P450 (heme-thiolate) enzyme is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
The reaction includes rearrangement of the 4(5)-double bond to a 4(20)-double bond, possibly through allylic oxidation.
O2 + reduced [NADPH--hemoprotein reductase] + taxa-4,11-diene = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + taxa-4(20),11-dien-5alpha-ol.
ultra-long-chain fatty acid omega-hydroxylase
The enzyme, which is expressed in the epidermis of mammals, catalyzes the omega-hydroxylation of ultra-long-chain fatty acids (C28 to C36).
The products are incorporated into acylceramides, epidermis-specific ceramide species that are very important for skin barrier formation.
an omega-methyl-ultra-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-ultra-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase].
O2 + reduced [NADPH--hemoprotein reductase] + triacontanoate = H(+) + H2O + omega-hydroxy-triacontanoate + oxidized [NADPH--hemoprotein reductase].
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide.
(1R,4R)-camphor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[putidaredoxin] = (1R,4R,5R)-5-hydroxycamphor + H2O + 2 oxidized [2Fe-2S]-[putidaredoxin].
Some enzyme of this group are heme-thiolated proteins (P450).
Also hydroxylates fatty acids in the omega-position.
2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin].
Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone.
a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-hydroxysteroid + H2O + 2 oxidized [adrenodoxin].
corticosterone + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 18-hydroxycorticosterone + H2O + 2 oxidized [adrenodoxin].
cholesterol monooxygenase (side-chain-cleaving)
The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22.
The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6.
cholesterol + 6 H(+) + 3 O2 + 6 reduced [adrenodoxin] = 4-methylpentanal + 4 H2O + 6 oxidized [adrenodoxin] + pregnenolone.
Catalyzes the first step of glycine betaine synthesis.
Different enzymes are involved in the first reaction.
In plants, the reaction is catalyzed by this enzyme whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17.
choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = betaine aldehyde hydrate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta.
Ring A-reduced, aromatic, and 3beta-hydroxy-Delta4-steroids do not serve as substrates.
2 H(+) + O2 + progesterone + reduced 2[4Fe-4S]-[ferredoxin] = 15beta-hydroxyprogesterone + H2O + oxidized 2[4Fe-4S]-[ferredoxin].
The enzyme is involved in spheroidenone biosynthesis and in 2,2'-dioxospirilloxanthin biosynthesis.
The enzyme from Rhodobacter sphaeroides contains heme at its active site.
4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] + spheroidene = 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin] + spheroiden-2-one.
4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] + spirilloxanthin = 2-oxospirilloxanthin + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
2-oxospirilloxanthin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 2,2'-dioxospirilloxanthin + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
A cytochrome P450 monooxygenase from the bacterium Rhodococcus sp. NCIMB 9784.
(1R,4R)-camphor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[putidaredoxin] = (+)-6-endo-hydroxycamphor + H2O + 2 oxidized [2Fe-2S]-[putidaredoxin].
The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
1-deoxypentalenate + 2 H(+) + O2 + reduced 2[4Fe-4S]-[ferredoxin] = H2O + oxidized 2[4Fe-4S]-[ferredoxin] + pentalenate.
cyclo-L-leucyl-L-leucyl dipeptide oxidase
A P450 enzyme from the bacterium Bacillus subtilis.
The order of events during the overall reaction is unknown.
Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin.
cyclo(L-leucyl-L-leucyl) + 4 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin] + pulcherriminic acid.
The enzyme, found in pathogenic and nonpathogenic mycobacteria species, actinomycetes, and some proteobacteria, hydroxylates the omega-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate.
a methyl-branched lipid + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) = an omega-hydroxy-methyl-branched lipid + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster.
5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase
5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase
Catalyzes the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway.
Can also act on cholesterol, cholest-5-en-3beta,7alpha-diol, 7alpha-hydroxycholest-4-en-3-one, and 5beta-cholestane-3alpha,7alpha-diol.
The enzyme can also hydroxylate cholesterol at positions 24 and 25.
5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 + 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin].
The enzyme can perform up to 6 rounds of hydroxylation of the substrate calcitriol leading to calcitroic acid.
The human enzyme also shows 23-hydroxylating activity leading to 1,25 dihydroxyvitamin D3-26,23-lactone as end product while the mouse and rat enzymes do not.
calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitetrol + H2O + 2 oxidized [adrenodoxin].
calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2 oxidized [adrenodoxin] + secalciferol.
calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin].
(1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2 oxidized [adrenodoxin].
(1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin].
(1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2 + 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized [adrenodoxin].
This enzyme catalyzes a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants.
The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I.
While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12.
In (18)O2 labeling experiments, only the aldehyde oxygen is labeled, suggesting that the other oxygen atom may originate from H2O.
2 H(+) + O2 + pheophorbide a + 2 reduced [2Fe-2S]-[ferredoxin] = 2 oxidized [2Fe-2S]-[ferredoxin] + red chlorophyll catabolite.
25-hydroxycholecalciferol 1-monooxygenase
calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin].
2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = calcitetrol + H2O + 2 oxidized [adrenodoxin].
The enzyme, characterized from the bacterium Sorangium cellulosum, is a class I cytochrome P450, and uses ferredoxin as its electron donor.
It was shown to act on several C-19 steroid substrates, including testosterone, androstenedione, testosterone-acetate and 11-oxoandrostenedione.
2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + testosterone = 1alpha-hydroxytestosterone + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
androst-4-ene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 1alpha-hydroxyandrost-4-ene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
heme oxygenase (biliverdin-producing, ferredoxin)
The enzyme, found in plants, algae, and cyanobacteria, participates in the biosynthesis of phytochromobilin and phytobilins.
Unlike this enzyme, which uses ferredoxin as its electron donor, the electron source for the related mammalian enzyme (EC 1.14.14.18) is EC 1.6.2.4.
8 H(+) + heme b + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + CO + Fe(2+) + 3 H2O + 6 oxidized [2Fe-2S]-[ferredoxin].
Along with EC 1.23.5.1, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light.
It will also epoxidize lutein in some higher-plant species.
all-trans-zeaxanthin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = all-trans-violaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
An enzyme found in the bacterium Streptomyces griseolus.
calciol + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = calcidiol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
calcidiol + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = calcitriol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from the bacterium Sphingomonas sp. DC-6, initiates the degradation of several chloroacetanilide herbicides, including alachlor, acetochlor, and butachlor.
The enzyme is a Rieske non-heme iron oxygenase, and requires a ferredoxin and EC 1.18.1.3 for activity.
butachlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = butyl formate + H2O + N-(2,6-diethylphenyl)-2-chloroacetamide + 2 oxidized [2Fe-2S]-[ferredoxin].
Also acts on other carotenoids with a beta-end group.
In some species canthaxanthin is the preferred substrate.
all-trans-beta-carotene + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = all-trans-zeaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from several Pseudomonas strains, initiates p-cymene catabolism through hydroxylation of the methyl group.
The enzyme has a distinct preference for substrates containing at least an alkyl or heteroatom substituent at the para-position of toluene.
The electrons are provided by a reductase (EC 1.18.1.3) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster.
In Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity.
2 H(+) + O2 + p-cymene + 2 reduced [2Fe-2S]-[ferredoxin] = 4-isopropylbenzyl alcohol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from several Pseudomonas strains, catalyzes the first step in the degradation of toluenes and xylenes.
It has a broad substrate specificity and is also active with substituted compounds, such as chlorotoluenes.
The enzyme can also act on its products, producing gem-diols that spontaneously dehydrate to form aldehydes.
2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + toluene = benzyl alcohol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
2 H(+) + O2 + p-xylene + 2 reduced [2Fe-2S]-[ferredoxin] = 4-methylbenzyl alcohol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
2 H(+) + m-xylene + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3-methylbenzyl alcohol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
beta-dihydromenaquinone-9 omega-hydroxylase
The bacterial cytochrome P450 enzyme is involved in the biosynthesis of omega-sulfo-beta-dihydromenaquinone-9 by members of the Mycobacterium tuberculosis complex.
beta-dihydromenaquinone-9 + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + omega-hydroxy-beta-dihydromenaquinone-9 + 2 oxidized [2Fe-2S]-[ferredoxin].
cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]
This cytochrome P450 (heme-thiolate) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol.
It catalyzes the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol.
The products are exclusively in the (25R) conformation.
The enzyme also accepts cholesterol as a substrate.
The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin].
cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]
A cytochrome P450 (heme-thiolate) protein found in several bacterial pathogens.
The enzyme is involved in degradation of the host's cholesterol.
The products are exclusively in the (25S) conformation.
cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25S)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin].
The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis.
It forms a two-component system with a ferredoxin reductase (KshB).
The enzyme contains a Rieske-type iron-sulfur center and non-heme iron.
The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
A cytochrome P450 (heme-thiolate) protein involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
2-hydroxy-5-methyl-1-naphthoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 2,7-dihydroxy-5-methyl-1-naphthoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
A cytochrome P450 (heme-thiolate) protein found in the bacterium Streptomyces avermitilis.
The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.
4 H(+) + 2 O2 + pentalenene + 4 reduced [2Fe-2S]-[ferredoxin] = 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin] + pentalen-13-al.
Involved in the biosynthesis of a number of bacterial macrolide antibiotics containing a desosamine glycoside unit.
With narbomycin it hydroxylates at either C-12 to give pikromycin or C-14 to give neopikromycin or both positions to give narvopikromycin.
With 10-deoxymethymycin it hydroxylates at either C-10 to give methymycin or C-12 to give neomethymycin or both positions to give novamethymycin.
2 H(+) + narbomycin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + 2 oxidized [2Fe-2S]-[ferredoxin] + pikromycin.
2 H(+) + narbomycin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + neopikromycin + 2 oxidized [2Fe-2S]-[ferredoxin].
4 H(+) + narbomycin + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + novapikromycin + 4 oxidized [2Fe-2S]-[ferredoxin].
10-deoxymethymycin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + methymycin + 2 oxidized [2Fe-2S]-[ferredoxin].
10-deoxymethymycin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + neomethymycin + 2 oxidized [2Fe-2S]-[ferredoxin].
10-deoxymethymycin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + novamethymycin + 4 oxidized [2Fe-2S]-[ferredoxin].
20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
A cytochrome P450 (heme-thiolate) protein involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
20-oxo-5-O-beta-D-mycaminosyltylonolide + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 5-O-beta-D-mycaminosyltylonolide + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
A cytochrome P450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea.
The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
6-deoxyerythronolide B + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = erythronolide B + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
A cytochrome P450 (heme-thiolate) protein found in several bacterial species.
The enzyme, which is involved in sterol biosynthesis, catalyzes a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
The enzyme from Methylococcus capsulatus is fused to the ferredoxin by an alanine-rich linker.
a 14alpha-methyl steroid + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = a Delta(14) steroid + formate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from the bacterium Streptomyces thioluteus, is a bifunctional cytochrome P450 (heme-thiolate) protein that catalyzes both the hydroxylation of its substrate and formation of a furan ring, the final step in the biosynthesis of the antibiotic aureothin.
In the bacteria Streptomyces orinoci and Streptomyces spectabilis an orthologous enzyme catalyzes a similar reaction that forms spectinabilin.
4 H(+) + luteothin + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = aureothin + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, found in members of the Sphingobium genus, initiates the degradation of N,N-dimethyl-phenylurea herbicides by mono-N-demethylation.
The enzyme associates with additional proteins (a reductase and a [3Fe-4S] type ferredoxin) that are involved in the transfer of electrons from NAD(P)H to the active site.
a 1,1-dimethyl-3-phenylurea + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-methyl-3-phenylurea + formaldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
This enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes two sequential allylic oxidation reactions.
The substrate epi-isozizaene, which is formed by the action of EC 4.2.3.37 is first oxidized to yield the epimeric intermediates (5R)-albaflavenol and (5S)-albaflavenol, which can be further oxidized to yield the sesquiterpenoid antibiotic albaflavenone.
(+)-epi-isozizaene + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = albaflavenone + 3 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
With reduced pteridine as one donor, and incorporation of one atom of oxygen
The reaction involves an arene oxide which rearranges to give the phenolic hydroxy group.
This results in the hydrogen at C-4 migrating to C-3 and in part being retained, a process known as the NIH-shift.
The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96.
The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine.
Activated by phosphorylation, catalyzed by EC 2.7.11.27.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa.
Activated by phosphorylation, catalyzed by a Ca(2+)-activated protein kinase.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-hydroxy-L-tryptophan.
The enzyme cleaves alkylglycerols, but does not cleave alkenylglycerols (plasmalogens).
Requires phospholipids for full activity.
The product spontaneously breaks down to form a fatty aldehyde and glycerol.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 1-O-(1,2-saturated-alkyl)-sn-glycerol + O2 = (6R)-L-erythro-6,7-dihydrobiopterin + a 1-(1-hydroxyalkyl)-sn-glycerol + H2O.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + (S)-mandelate + O2 = (6R)-L-erythro-6,7-dihydrobiopterin + (S)-4-hydroxymandelate + H2O.
The enzyme, characterized from the bacterium Streptomyces coeruleorubidus, forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine), which is one of the building blocks in the biosynthesis of the uridyl peptide antibiotics pacidamycins.
The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96.
The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 3-hydroxy-L-phenylalanine.
With reduced ascorbate as one donor, and incorporation of one atom of oxygen
The enzyme, found in animals, binds two copper ions with distinct roles during catalysis.
dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2 monodehydro-L-ascorbate radical.
peptidylglycine alpha-amidating monooxygenase
The enzyme binds two copper ions with distinct roles during catalysis.
Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme.
The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalyzed by EC 4.3.2.5.
In mammals, the two activities are part of a bifunctional protein.
Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical.
1-aminocyclopropane-1-carboxylate oxidase
In the enzyme from plants, the ethylene has signaling functions such as stimulation of fruit-ripening.
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 + ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate.
With another compound as one donor, and incorporation of one atom of oxygen
Found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin.
The enzyme, which is activated upon binding molecular oxygen, can catalyze both a monophenolase reaction cycle or a diphenolase reaction cycle.
During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an O-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule.
The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule.
During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an O-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state.
The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state.
The second reaction is identical to that catalyzed by the related enzyme catechol oxidase (EC 1.10.3.1).
However, the latter can not catalyze the hydroxylation or monooxygenation of monophenols.
2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone.
cytidine monophosphoacetylneuraminate monooxygenase
The ferricytochrome b5 produced is reduced by NADH and EC 1.6.2.2.
The enzyme can be activated by Fe(2+) or Fe(3+).
CMP-N-acetyl-beta-neuraminate + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = CMP-N-glycoloyl-beta-neuraminate + 2 Fe(III)-[cytochrome b5] + H2O.
It is membrane-bound, in contrast to the soluble EC 1.14.13.25.
a quinol + methane + O2 = a quinone + H2O + methanol.
The enzyme, characterized from the plant Ricinus communis (castor bean), is involved in production of the 12-hydroxylated fatty acid ricinoleate.
The enzyme requires a cytochrome b5 as the electron donor.
1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-acyl-2-[(R)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + 2 Fe(III)-[cytochrome b5] + H2O.
The enzyme, which belongs to the familiy of endoplasmic reticular cytochrome b5-dependent enzymes, is involved in the biosynthesis of sphingolipids in eukaryotes.
Some enzymes are bifunctional and also catalyze EC 1.14.19.17.
a dihydroceramide + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a phytoceramide + 2 Fe(III)-[cytochrome b5] + H2O.
an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acyl-(4R)-4-hydroxysphinganine + 2 Fe(III)-[cytochrome b5] + H2O.
4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase
The enzyme, characterized from yeast and mammals, catalyzes the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis.
The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site.
The newly introduced 2-hydroxyl group has R-configuration.
an N-(1,2 saturated acyl)-(4R)-hydroxysphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-(2R-hydroxyacyl)-4R-hydroxysphinganine + 2 Fe(III)-[cytochrome b5] + H2O.
an N-(1,2 saturated very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-(2R-hydroxy-very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base + 2 Fe(III)-[cytochrome b5] + H2O.
dihydroceramide fatty acyl 2-hydroxylase
plant sphingolipid fatty acid 2-hydroxylase
The enzyme, characterized from plants, catalyzes the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to sphinganine during de novo ceramide synthesis.
The enzyme requires an external cytochrome b5 as the electron donor.
an N-(1,2-saturated acyl)sphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-[(2'R)-hydroxyacyl]sphinganine + 2 Fe(III)-[cytochrome b5] + H2O.
This enzyme is found in fungi and animals and catalyzes a step in the biosynthesis of important sterol molecules such as ergosterol and cholesterol, respectively.
The enzyme acts on the 4alpha-methyl group.
Subsequent decarboxylation by EC 1.1.1.170 occurs concomitantly with epimerization of the remaining 4beta-methyl into the 4alpha position, thus making it a suitable substrate for a second round of catalysis.
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O.
plant 4,4-dimethylsterol C-4alpha-methyl-monooxygenase
This plant enzyme catalyzes a step in the biosynthesis of sterols.
It acts on the 4alpha-methyl group of the 4,4-dimethylated intermediate 24-methylenecycloartanol and catalyzes three successive oxidations, turning it into a carboxyl group.
The carboxylate is subsequently removed by EC 1.1.1.418, which also catalyzes the epimerization of the remaining 4beta-methyl into the 4alpha position.
Unlike the fungal/animal enzyme EC 1.14.18.9, this enzyme is not able to remove the methyl group from C-4-monomethylated substrates.
That activity is performed in plants by a second enzyme, EC 1.14.18.11.
24-methylenecycloartanol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(24(1))-en-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O.
plant 4alpha-monomethylsterol monooxygenase
It acts on the methyl group of the 4alpha-methylated intermediates 24-ethylidenelophenol and 24-methylidenelophenol and catalyzes three successive oxidations, turning it into a carboxyl group.
The carboxylate is subsequently removed by EC 1.1.1.418.
Unlike the fungal/animal enzyme EC 1.14.18.9, this enzyme is not able to act on 4,4-dimethylated substrates.
That activity, which occurs earlier in the pathway, is performed in plants by a second enzyme, EC 1.14.18.10.
24-methylidenelophenol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-ergosta-7,24(24(1))-dien-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O.
The enzyme, characterized from yeast, is involved in phytosphingosine metabolism.
The reaction is mediated by iron(IV) peroxide and results in the release of a water molecule and a carbon dioxide molecule, shortening the substrate by a single carbon atom and forming an odd-numbered fatty acid.
Both oxygen atoms of the original carboxylate group are released - one as the leaving water molecule, the other as one of the oxygens of the carbon dioxide molecule.
The two oxygen atoms in the newly-formed carboxylate originate from the 2-hydroxy group and from molecular oxygen, respectively.
The other oxygen atom of the molecular oxygen is incorporated into the leaving CO2 molecule.
The enzyme from the yeast Saccharomyces cerevisiae is active at least toward C14 to C26 2-hydroxy fatty acids, but not against C8 2-hydroxy fatty acid.
a (2R)-2-hydroxy Cn-fatty acid + O2 = a Cn-1-fatty acid + H2O + CO2.
(R)-2-hydroxyhexadecanoate + O2 = CO2 + H2O + pentadecanoate.
With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
The liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2.
2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
stearoyl-[acyl-carrier-protein] 9-desaturase
The enzyme is found in the lumen of plastids, where de novo biosynthesis of fatty acids occurs, and acts on freshly synthesized saturated fatty acids that are still linked to acyl-carrier protein.
The enzyme determines the position of the double bond by its distance from the carboxylic acid end of the fatty acid.
It also acts on palmitoyl-[acyl-carrier-protein].
2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
long-chain fatty acid Delta(6)-desaturase
The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs.
It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid.
The human enzyme has a broad substrate range; it also acts on palmitoyl-CoA, generating sapienoyl-CoA, and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate.
The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase.
(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the protist Euglena gracilis and the microalga Rebecca salina, introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Delta(11) desaturation.
The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid.
It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate.
an (11Z,14Z)-icosadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
an (11Z,14Z,17Z)-icosatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an (8Z,11Z,14Z,17Z)-eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs.
In moths the enzyme participates in the biosynthesis of their sex pheromones.
The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0), that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0), while that from the moth Spodoptera littoralis accepts both substrates.
The enzyme contains three histidine boxes that are conserved in all desaturases.
It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase.
an 11,12-saturated fatty acyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an (11Z)-Delta(11)-fatty acyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9.
When acting on 19:1Delta(10) fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, toward the methyl-end of the fatty acid.
(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
2 H(+) + O2 + pentalenolactone F + 2 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin] + pentalenolactone.
The enzyme from the bacterium Lechevalieria aerocolonigenes catalyzes the initial step in the biosynthesis of rebeccamycin.
It utilizes molecular oxygen to oxidize the FADH2 cofactor, giving C4a-hydroperoxyflavin, which then reacts with chloride to produce a hypochlorite ion.
The latter reacts with an active site lysine to generate a chloramine, which chlorinates the substrate.
chloride + FADH2 + L-tryptophan + O2 = 7-chloro-L-tryptophan + FAD + 2 H2O.
The enzyme, characterized from the plant Limnanthes douglasii (meadowfoam), is involved in the biosynthesis of (5Z)-icos-5-enoate, an unusual monounsaturated fatty acid that makes up to 60% of the total fatty acids in Limnanthes sp. seed oil.
The enzyme only acts on saturated fatty acids.
eicosanoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z)-eicosenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
acyl-[acyl-carrier-protein] 4-desaturase
Delta(4)-palmitoyl-[acyl carrier protein] desaturase
The enzymes from the plants Coriandrum sativum (coriander) and Hedera helix are involved in biosynthesis of petroselinate [(6Z)-octadec-6-enoate], which is formed by elongation of (4Z)-hexadec-4-enoate.
The ivy enzyme can also act on oleoyl-[acyl-carrier protein] and palmitoleoyl-[acyl-carrier protein], generating the corresponding 4,9-diene.
2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in omega(9) unsaturated C18 or C20 fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing omega(9) bond, toward the carboxy end of the fatty acid (at the omega(13) position).
When acting on 20:2Delta(11,14) and 20:3Delta(11,14,17) substrates it introduces the new double bond between carbons 7 and 8.
The enzyme contains a cytochrome b5 domain that acts as the direct electron donor for the active site of the desaturase.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,9Z,12Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,9Z,12Z,15Z)-octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the the plant Sorghum bicolor, is involved in the biosynthesis of sorgoleone, an allelopathic compound produced in root hair cells.
The enzyme inserts a cis double bond at carbon 15.
When acting on its natural substrate, (9Z,12Z)-hexadeca-9,12-dienoyl-CoA, it produces a product with a terminal double bond.
(9Z,12Z)-hexadecadienoyl-CoA + AH2 + O2 = (9Z,12Z,15Z)-hexadecatrienoyl-CoA + A + 2 H2O.
The enzyme, characterized from the plant Calendula officinalis, converts a single cis double bond at position 9 of fatty acids incorporated into glycerolipids into two conjugated trans double bonds at positions 8 and 10.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + AH2 + O2 = A + a (8E,10E,12Z)-octadecatrienoyl-containing glycerolipid + 2 H2O.
The enzyme, characterized from the silk moth Bombyx mori, catalyzes a step in the pathway for the biosynthesis of bombykol, a sex pheromone produced by the moth.
The enzyme converts a single cis double bond at position 11 of (11Z)-hexadec-11-enoyl-CoA into conjugated 10 trans and 12 cis double bonds.
Prior to catalyzing this reaction, the enzyme catalyzes the introduction of the cis bond in position 11 (cf. EC 1.14.19.5).
(11Z)-hexadecenoyl-CoA + AH2 + O2 = (10E,12Z)-hexadecadienoyl-CoA + A + 2 H2O.
linoleoyl-lipid Delta(12) conjugase (11E,13Z-forming)
The enzyme, characterized from the plants Punica granatum (pomegranate) and Trichosanthes kirilowii (Mongolian snake-gourd), converts a single cis double bond at position 12 of linoleate incorporated into phosphatidylcholine into conjugated 11-trans and 13-cis double bonds.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13Z)-octadeca-9,11,13-trienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids.
The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide.
Unlike EC 1.14.19.29, this enzyme does not contain an integral cytochrome b5 domain and requires an external cytochrome b5.
The product serves as an important signaling molecules in mammals and is required for spermatide differentiation.
an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans and from the diatom Thalassiosira pseudonana, introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids.
The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase.
The homologous enzymes from higher plants, EC 1.14.19.29, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers.
an N-acylsphing-4-enine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4E,8E)-4-sphinga-4,8-dienine ceramide + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the marine diatom Thalassiosira pseudonana, produces an all-trans product.
Similar triunsaturated sphingoid bases are found in some marine invertebrates.
a (4E,8E)-4-sphinga-4,8-dienine ceramide + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 2 Fe(III)-[cytochrome b5] + 2 H2O + N-acyl-(4E,8E,10E)-sphingatrienine.
This enzyme, found in eukaryotic organisms, catalyzes the introduction of a double bond between the C5 and C6 carbons of the B ring of Delta(7)-sterols, to yield the corresponding Delta(5,7)-sterols.
The enzymes from yeast, plants and vertebrates act on avenasterol, episterol, and lathosterol, respectively.
The enzyme is located at the endoplasmic reticulum and is membrane bound.
a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O.
2 Fe(II)-[cytochrome b5] + 2 H(+) + lathosterol + O2 = 7-dehydrocholesterol + 2 Fe(III)-[cytochrome b5] + 2 H2O.
episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from several organisms including the worm Caenorhabditis elegans, the fly Drosophila melanogaster, and the ciliate Tetrahymena thermophila, is a Rieske oxygenase.
In insects it participates in the the biosythesis of ecdysteroid hormones.
The electrons are transferred from NAD(P)H via an electron transfer chain likely to include ferredoxin reductase and ferredoxin.
The enzyme differs from regular desaturases, such as EC 1.14.19.20, which are cytochrome b5-dependent and contain the three His-boxes that are typical to most desaturases.
cholesterol + H(+) + NADPH + O2 = 7-dehydrocholesterol + 2 H2O + NADP(+).
cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O + NAD(+).
acyl-lipid omega-6 desaturase (cytochrome b5)
This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 carbons away from the methyl end of the fatty acid.
The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond.
The most common substrates are oleoyl groups attached to either sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine.
a (9Z)-octadecenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
acyl-lipid (n+3)-(Z)-desaturase (ferredoxin)
acyl-lipid omega(6)-desaturase (ferredoxin)
This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids.
The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, toward the methyl end of the fatty acid.
The native substrates are oleoyl (18:1 Delta(9)) and (Z)-hexadec-7-enoyl (16:1 Delta(7)) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an omega(6) desaturase.
However, when acting on palmitoleoyl groups(16:1 Delta(9)), the enzyme introduces the second double bond at position 12 (omega(4)), indicating it is an (n+3) desaturase.
a (9Z)-octadecenoyl-containing glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
Involved in sex pheromone synthesis in the Lepidoptera (moths).
The enzyme from the moth Spodoptera littoralis prefers 13:0 and 14:0 substrates.
The product is formed by the stereospecific removal of the pro-R H at C-11 and the pro-S H at C-12.
an 11,12-saturated fatty acyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an (11E)-Delta(11)-fatty acyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
acyl-lipid omega-3 desaturase (cytochrome b5)
This microsomal enzyme introduces a cis double bond three carbons away from the methyl end of a fatty acid incorporated into a glycerolipid.
The distance from the carboxylic acid end of the molecule does not have an effect.
The plant enzyme acts on carbon 15 of linoleoyl groups incorporated into both the sn-1 and sn-2 positions of the glycerol backbone of phosphatidylcholine and other phospholipids, converting them into alpha-linolenoyl groups.
The enzyme from the fungus Mortierella alpina acts on gamma-linolenoyl and arachidonoyl groups, converting them into stearidonoyl and icosapentaenoyl groups, respectively.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
acyl-[acyl-carrier-protein] 6-desaturase
The enzyme, characterized from the endosperm of the plant Thunbergia alata (black-eyed Susan vine), introduces a cis double bond at carbon 6 of several saturated acyl-[acyl-carrier protein]s.
It is most active with palmitoyl-[acyl-carrier protein] (16:0), but can also act on myristoyl-[acyl-carrier protein] (14:0) and stearoyl-[acyl-carrier protein] (18:0).
The position of the double bond is determined by its distance from the carboxyl end of the fatty acid.
2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (6Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from the cyanobacterium Nostoc sp. 36, introduces a cis double bond at carbon 9 of palmitoyl groups (16:0) attached to the sn-2 position of glycerolipids.
a 1-acyl-2-hexadecanoyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-acyl-2-[(9Z)-hexadecenoyl]-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 9 of stearoyl groups (18:0) attached to the sn-1 position of glycerolipids.
The enzyme is non-specific with respect to the polar head group of the glycerolipid.
1-octadecanoyl 2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-[(9Z)-octadecenoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzymes from higher plants convert sphinganine, 4E-sphing-4-enine and phytosphinganine into E/Z-mixtures of Delta(8)-desaturated products displaying different proportions of geometrical isomers depending on plant species.
The nature of the actual desaturase substrate has not yet been studied experimentally.
The enzymes contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase.
The homologous enzymes from some yeasts and diatoms, EC 1.14.19.18, act on sphing-4-enine ceramides and produce only the trans isomer.
an N-acyl-(4R)-4-hydroxysphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4R,8E)-4-hydroxysphingenine ceramide + 2 Fe(III)-[cytochrome b5] + 2 H2O.
an N-acyl-(4R)-4-hydroxysphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (4R,8Z)-4-hydroxysphing-8-enine ceramide + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, which has been characterized from multiple organisms including the moss Physcomitrella patens, the marine microalga Rebecca salina, and the filamentous fungus Mortierella alpina, introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond.
The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
an (8Z,11Z,14Z,17Z)-eicosatetraenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond.
The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate.
The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
a (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
a (7Z,10Z,13Z,16Z)-docosatetraenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4Z,7Z,10Z,13Z,16Z)-docosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, found in the moth Ostrinia furnacalis (Asian corn borer), produces a mixture of (E)- and (Z)- isomers.
The products are subsequently truncated by partial beta-oxidation to a blend of 12(E/Z)-tetradec-12-enoyl-CoA, which are converted to the species-specific sex pheromones (E)- and (Z)-tetradec-12-enoyl acetates.
2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (14E)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (14Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
Delta(12) acyl-lipid conjugase (11E,13E-forming)
The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13.
The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13E)-octadecatrienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13E,15Z)-octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzymes from the plants Dimorphotheca sinuata (African daisy) and Vernicia fordii (tung oil tree) insert a trans double bond in position C-12 of oleate and palmitoleate incorporated into glycerolipids.
The enzyme introduces the new double bond at a position three carbons away from an existing double bond at position 9, toward the methyl end of the fatty acid.
The enzyme from tung oil tree also possesses the activity of EC 1.14.19.33.
a (9Z)-octadecenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12E)-octadecadienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
a (9Z)-hexadecenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12E)-hexadecadienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
sn-2 acyl-lipid omega-3 desaturase (ferredoxin)
This plastidial enzyme desaturates 16:2 fatty acids attached to the sn-2 position of glycerolipids to 16:3 fatty acids, and converts18:2 to 18:3 in both the sn-1 and sn-2 positions.
It acts on all 16:2- or 18:2-containing chloroplast membrane lipids, including phosphatidylglycerol, monogalactosyldiacylglycerol, digalactosyldiaclyglycerol, and sulfoquinovosyldiacylglycerol.
The enzyme introduces a cis double bond at a location 3 carbons away from the methyl end of the fatty acid.
a (7Z,10Z)-hexadecadienoyl-containing glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a (7Z,10Z,13Z)-hexadecatrienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
sn-1 acyl-lipid omega-3 desaturase (ferredoxin)
The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 15 of linoleoyl and gamma-linolenoyl groups attached to the sn-1 position of glycerolipids.
The enzyme is an omega desaturase, and determines the location of the double bond by counting three carbons from the methyl end of the fatty acid.
It is non-specific with respect to the polar head group of the glycerolipid.
a 1-[(6Z,9Z,12Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-[(6Z,9Z,12Z,15Z)-octadectetraenoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
a 1-[(9Z,12Z)-octadecdienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-[(9Z,12Z,15Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
acyl-CoA 5-desaturase (non-methylene-interrupted)
The enzyme, characterized from the plant Anemone leveillei, introduces a cis double bond at carbon 5 of acyl-CoAs that do not contain a double bond at position 8.
In vivo it forms non-methylene-interrupted polyunsaturated fatty acids such as sciadonate and juniperonate.
When expressed in Arabidopsis thaliana the enzyme could also act on unsaturated substrates such as palmitoyl-CoA.
(11Z,14Z)-eicosadienoyl-CoA + AH2 + O2 = (5Z,11Z,14Z)-eicosatrienoyl-CoA + A + 2 H2O.
(11Z,14Z,17Z)-eicosatrienoyl-CoA + AH2 + O2 = (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + A + 2 H2O.
(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the moss Ceratodon purpureus, converts the double bond at position 6 of gamma-linolenate and stearidonate into a triple bond.
The product of the latter, dicranin, is the main fatty acid found in C. purpureus.
The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site.
The enzyme also has the activity of EC 1.14.19.47.
(6Z,9Z,12Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12Z)-octadeca-9,12-dien-6-ynoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(6Z,9Z,12Z,15Z)-octadecatetraenoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,12Z,15Z)-octadeca-9,12,15-trien-6-ynoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the plant Crepis alpina, converts the double bond at position 12 of linoleate into a triple bond.
The product is the main fatty acid found in triacylglycerols in the seed oil of Crepis alpina.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z)-octadec-9-en-12-ynoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
hex-5-enoyl-[acyl-carrier protein] acetylenase
The enzyme, characterized from the marine cyanobacterium Moorea producens, is involved in production of the ion channel blocker jamaicamide A.
It is specific for hexanoate or hex-5-enoate loaded onto a dedicated acyl-carrier protein (JamC), which is encoded by a gene in the same operon.
5-hexenoyl-[ACP] + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 5-hexynoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
2 H(+) + hexanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 5-hexenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, found in yeast and plants, catalyzes the introduction of a double bond between the C-22 and C-23 carbons of certain sterols.
In yeast the enzyme acts on ergosta-5,7,24(28)-trien-3beta-ol, a step in the biosynthesis of ergosterol.
The enzyme from the plant Arabidopsis thaliana acts on sitosterol and 24-epi-campesterol, producing stigmasterol and brassicasterol, respectively.
5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+).
H(+) + NADPH + O2 + sitosterol = 2 H2O + NADP(+) + stigmasterol.
The enzyme introduces a cis double bond at carbon 7 of a palmitoyl group attached to the sn-2 position of glycerolipids.
The enzyme from the plant Arabidopsis thaliana is specific for palmitate in monogalactosyldiacylglycerol.
a 1-acyl-2-hexadecanoyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-acyl-2-[(7Z)-hexadecenoyl]-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
palmitoyl-[glycerolipid] 3-(E)-desaturase
The enzyme introduces an unusual trans double bond at carbon 3 of a palmitoyl group attached to the sn-2 position of glycerolipids.
The enzyme from the plant Arabidopsis thaliana is specific for palmitate in phosphatidylglycerol.
The enzyme from tobacco can also accept oleate and alpha-linolenate if present at the sn-2 position of phosphatidylglycerol.
a 1-acyl-2-hexadecanoyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-acyl-2-[(3E)-hexadec-3-enoyl]-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
acyl-CoA 5-desaturase (methylene-interrupted)
The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8.
The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyze the desaturation of dihomo-gamma-linoleate ((8Z,11Z,14Z)-icosa-8,11,14-trienoate) and (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively.
The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome.
(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 12 of oleoyl groups (18:1) attached to the sn-1 position of glycerolipids.
The enzyme is a methyl-end desaturase, introducing the new double bond between a pre-existing double bond and the methyl-end of the fatty acid.
a 1-[(9Z)-octadecenoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-[(9Z,12Z)-octadecdienoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 6 of linoleoyl groups (18:2) attached to the sn-1 position of glycerolipids.
The enzyme is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid.
a 1-[(9Z,12Z)-octadecdienoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-[(6Z,9Z,12Z)-octadectrienoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Delta(9) cis double bond.
The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase.
(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis can also act, with lower efficiency, on 2-butanol, converting it to but-1-en-3-ol.
Depending on the substrate, the enzyme also catalyzes EC 1.14.13.229.
2-methylbutan-2-ol + H(+) + NADPH + O2 = 3-hydroxy-3-methylbut-1-ene + 2 H2O + NADP(+).
Characterized from the bacterium Streptomyces aureofaciens.
The enzyme forms a lysine chloramine intermediate on an internal lysine residue before transferring the chlorine to the substrate.
It is stereo-selective for the 4S (natural) isomer of tetracycline.
chloride + FADH2 + O2 + tetracycline = 7-chlorotetracycline + FAD + H(+) + 2 H2O.
The enzyme, characterized from Narcissus aff pseudonarcissus (daffodil), forms the two enantiomers of the Amaryllidacea alkaloid noroxomaritidine by catalyzing intramolecular oxidative para-para' phenol coupling.
The oxidation involves molecular oxygen without its incorporation into the product.
4'-O-methylnorbelladine + O2 + reduced [NADPH--hemoprotein reductase] = (10bS,4aR)-noroxomaritidine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
4'-O-methylnorbelladine + O2 + reduced [NADPH--hemoprotein reductase] = (10bR,4aS)-noroxomaritidine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Involved in the biosynthesis of the quaternary benzylisoquinoline alkaloid magnoflorine in the plant Coptis japonica.
(S)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] = (S)-corytuberine + 2 H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
bifunctional dihydrocamalexate synthase/camalexin synthase
This P450 enzyme, which has been characterized from the plant Arabidopsis thaliana, catalyzes the last two steps in the biosynthesis of camalexin, the main phytoalexin in that plant.
The enzyme catalyzes two successive oxidation events.
During the first of oxidation the enzyme introduces a C-N double bond, liberating hydrogen cyanide, and during the second oxidation it catalyzes a decarboxylation.
2-(L-cystein-S-yl)-2-(1H-indol-3-yl)-acetonitrile + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = camalexin + CO2 + 2 H(+) + 4 H2O + hydrogen cyanide + 2 oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme thiolate) enzyme found in vertebrates.
The enzyme is also active with retinal and retinoic acid.
all-trans-retinol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = all-trans-3,4-didehydroretinol + 2 H2O + 2 oxidized [adrenodoxin].
The enzyme from Papaver rhoeas (field poppy) is specific for (S)-reticuline and does not act on the (R)-form.
The enzyme from Papaver somniferum (opium poppy), which is involved in the biosynthesis of morphine and related alkaloids, forms a fusion protein with EC 1.5.1.27, which catalyzes the reduction of 1,2-dehydroreticuline to (R)-reticuline, thus forming an epimerase system that converts (S)-reticuline to (R)-reticuline.
(S)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] = 1,2-dehydroreticuline + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
4-hydroxybenzoate brominase (decarboxylating)
The enzyme, described from epiphytic marine bacteria of the genera Pseudoalteromonas and Marinomonas, is an unusual single-component FAD-dependent halogenase that contains a distinct NAD(P)H binding domain and does not require an additional flavin reductase for activity.
The enzyme catalyzes a bromination of its substrate, followed by a second bromination concurrent with decarboxylation.
4-hydroxybenzoate + 2 bromide + 5 H(+) + 2 NADPH + 2 O2 = 2,4-dibromophenol + CO2 + 4 H2O + 2 NADP(+).
3,4-dihydroxybenzoate + 2 bromide + 5 H(+) + 2 NADPH + 2 O2 = 3,5-dibromobenzene-1,2-diol + CO2 + 4 H2O + 2 NADP(+).
1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase
The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a flavin-dependent chlorinase that participates in the biosynthesis of the antibacterial and antifungal compound pyoluteorin.
(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 2 chloride + 2 FADH2 + 2 O2 = (4,5-dichloro-1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 2 FAD + 4 H2O.
1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase
The enzyme, characterized from marine bacteria of the Pseudoalteromonas genus, belongs to a family of FAD-dependent halogenases that act on acyl-carrier protein-tethered substrates.
It catalyzes three successive rounds of bromination.
While the order has not been verified, it is believed to resemble that of EC 1.14.19.56, due to significant sequence homology.
Reduced FAD is provided in situ by a dedicated reductase and diffuses into the active site, where it reacts with the oxygen and bromide ion, resulting in formation of a bromoamine intermediate on a catalytic lysine side chain, and the eventual transfer of the bromide to the substrate.
The enzyme from Pseudoalteromonas luteoviolacea 2ta16 is specific for bromide and does not accept chloride.
(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 3 bromide + 3 FADH2 + 3 O2 = (3,4,5-tribromo-1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 3 FAD + 6 H2O.
The enzyme from the bacterium Streptomyces rugosporus catalyzes halogenation of the C-5 position of tryptophan during the biosynthesis of the antibiotic compound pyrroindomycin B.
chloride + FADH2 + L-tryptophan + O2 = 5-chloro-L-tryptophan + FAD + 2 H2O.
The enzyme is a flavin-dependent halogenase that has been described from several bacterial species.
chloride + FADH2 + L-tryptophan + O2 = 6-chloro-L-tryptophan + FAD + 2 H2O.
chloride + D-tryptophan + FADH2 + O2 = 6-chloro-D-tryptophan + FAD + 2 H2O.
The enzyme, characterized from the bacterium Kutzneria sp. 744, works in tandem with EC 1.14.19.9 to generate 6,7-dichloro-L-tryptophan, which is incorporated as a pyrroloindoline in the kutznerides family of natural products.
It has a 120-fold preference for 7-chloro-L-tryptophan over L-tryptophan as substrate.
7-chloro-L-tryptophan + chloride + FADH2 + O2 = 6,7-dichloro-L-tryptophan + FAD + 2 H2O.
The enzyme, characterized from the bacterium Bradyrhizobium elkanii, catalyzes the final step in the biosynthesis of the nodulation enhancer compound rhizobitoxine.
dihydrorhizobitoxine + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin] + rhizobitoxine.
Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.
loganin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + secologanin.
A cytochrome P450 (heme-thiolate) enzyme catalyzing an oxidative reaction that does not incorporate oxygen into the product.
Catalyzes a step in the biosynthesis of (-)-maackiain, the main pterocarpan phytoalexin in chickpea (Cicer arietinum).
calycosin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + pseudobaptigenin.
O2 + pratensein + reduced [NADPH--hemoprotein reductase] = 5-hydroxypseudobaptigenin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
A cytochrome P450 (heme-thiolate) protein catalyzing an oxidative reaction that does not incorporate oxygen into the product.
Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.
(S)-cheilanthifoline + O2 + reduced [NADPH--hemoprotein reductase] = (S)-stylopine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(S)-scoulerine oxidase (methylenedioxy-bridge-forming)
Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline by the oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine.
Cf. EC 1.14.19.73 which catalyzes a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-nandinine.
(S)-scoulerine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-cheilanthifoline + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product.
Reaction of two molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.
(R)-N-methylcoclaurine + (S)-N-methylcoclaurine + O2 + reduced [NADPH--hemoprotein reductase] = berbamunine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(R)-reticuline oxidase (C-C phenol-coupling)
Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.
(R)-reticuline + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] + salutaridine.
(S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming)
The enzyme catalyzes an oxidative reaction that does not incorporate oxygen into the product.
Oxidation of the methoxyphenol group of the alkaloid tetrahydrocolumbamine results in the formation of the methylenedioxy bridge of canadine.
(S)-tetrahydrocolumbamine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-canadine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
This cytochrome-P450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product.
The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation.
2 flaviolin + H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,3'-biflaviolin + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
2 flaviolin + H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,8'-biflaviolin + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
A cytochrome P450 (heme-thiolate) protein from the bacterium Mycobacterium tuberculosis catalyzing an oxidative reaction that does not incorporate oxygen into the product.
cyclo(L-tyrosyl-L-tyrosyl) + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 2 H2O + mycoclysin + 2 oxidized [2Fe-2S]-[ferredoxin].
The protein from the fungus Aspergillus fumigatus also has activity with tryprostatin B forming demethoxyfumitremorgin C.
Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.
O2 + reduced [NADPH--hemoprotein reductase] + tryprostatin A = fumitremorgin C + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
The enzyme from the plants Sinopodophyllum hexandrum and Podophyllum peltatum catalyzes the formation of a methylenedioxy-bridge.
It is involved in the biosynthesis of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
(-)-matairesinol + O2 + reduced [NADPH--hemoprotein reductase] = (-)-pluviatolide + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
A cytochrome P450 (heme-thiolate) enzyme found in plants.
Forms the methylenedioxy bridge of the protoberberine alkaloid (S)-nandinine by the oxidative ring closure of adjacent phenolic and methoxy groups of (S)-scoulerine.
Cf. EC 1.14.19.65, which catalyzes a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-cheilanthifoline.
(S)-scoulerine + O2 + reduced [NADPH--hemoprotein reductase] = (S)-nandinine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
Isolated from Sesamum indicum (sesame) and S. radiatum (black sesame).
(+)-pinoresinol + O2 + reduced [NADPH--hemoprotein reductase] = (+)-piperitol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
(+)-piperitol + O2 + reduced [NADPH--hemoprotein reductase] = (+)-sesamin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
very-long-chain acyl-lipid omega-9 desaturase
The enzyme, characterized from the plant Arabidopsis thaliana, acts on both 24:0 and 26:0 fatty acids, introducing a cis double bond at a position 9 carbons from the methyl end.
These very-long-chain fatty acids are found as a minor component of seed lipids, but also in the membrane phosphatidylethanolamine and phosphatidylserine, in sphingolipids, as precursors and components of cuticular and epicuticular waxes, and in suberin.
a 1-hexacosanoyl-2-acyl-phosphoglycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-[(17Z)-hexacos-17-enoyl]-2-acyl-phosphoglycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
a 1-tetracosanoyl-2-acyl-phosphoglycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a 1-[(15Z)-tetracos-15-enoyl]-2-acyl-phosphoglycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O.
The rice enzyme channels flavanones to the biosynthesis of tricin O-linked conjugates.
a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a flavone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase].
2-acyl-1-alkyl-sn-glycero-3-phosphoethanolamine desaturase
alkylacylglycerophosphoethanolamine desaturase
The enzyme catalyzes the introduction of a double bond at position 1 of the alkyl group attached by an ether bond at the sn-1 position of plasmanylethanolamine, generating a vinyl ether-containing plasmenylethanolamine.
The enzyme is found in animals and some bacteria, but not in plants, fungi, or most aerobic bacteria.
1-(1,2-saturated alkyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + 2 Fe(III)-[cytochrome b5] + 2 H2O.
decanoyl-[acyl-carrier protein] acetylenase
The enzyme, characterized from the bacterium Teredinibacter turnerae, is specific for decanoyl-[acyl-carrier protein].
Activity is maximal when decanoate is loaded onto a dedicated acyl-carrier protein (TtuC), which is encoded by a gene in the same operon.
decanoyl-[ACP] + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = dec-9-ynoyl-[ACP] + 4 H2O + 4 oxidized [2Fe-2S]-[ferredoxin].
H(+) + NADPH + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 H2O + NADP(+).
H(+) + NADPH + O2 + versicolorin B = 2 H2O + NADP(+) + versicolorin A.
With 2-oxoglutarate as one donor, and the other dehydrogenated
Forms part of the penicillin biosynthesis pathway.
2-oxoglutarate + O2 + penicillin N = CO2 + deacetoxycephalosporin C + H2O + succinate.
The enzyme is involved in the biosynthesis of the carbapenem beta-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
It catalyzes a stereoinversion at C(5) and introduces a double bond between C-2 and C-3.
(3S,5S)-carbapenam-3-caboxylate + 2-oxoglutarate + O2 = (5R)-carbapenem-3-carboxylate + CO2 + H2O + succinate.
Is involved in the pathway by which many flowering plants make anthocyanin flower pigments (glycosylated anthocyandins).
Hydroxylates the C-3 carbon, followed by a trans diaxial elimination, forming a C-2,C-3 enol.
The product loses a second water molecule to form anthocyanidins.
When assayed in vitro, non-enzymic epimerization of the product can lead to formation of dihydroflavanols.
Thus when the substrate is leucocyanidin, a mixture of (+)-taxifolin and (+)-epitaxifolin are formed.
The enzyme can also oxidize the formed (+)-taxifolin to quercetin (cf. EC 1.14.20.6).
2-oxoglutarate + a (2R,3S,4S)-leucoanthocyanidin + O2 = a 4-H-anthocyanidin with a 3-hydroxy group + CO2 + 2 H2O + succinate.
(2R,3S,4S)-leucocyanidin + 2-oxoglutarate + O2 = (4S)-2,3-dehydroleucocyanidin + CO2 + H(+) + H2O + succinate.
(2R,3S,4S)-3,4-leucopelargonidin + 2-oxoglutarate + O2 = (4S)-2,3-dehydroleucopelargonidin + CO2 + H(+) + H2O + succinate.
The enzyme, which has been found in rice and in members of the Apiaceae (a plant family), is a member of the 2-oxoglutarate-dependent dioxygenases, and requires ascorbate and Fe(2+) for full activity.
2-oxoglutarate + a flavanone + O2 = a flavone + CO2 + H2O + succinate.
(2S)-naringenin + 2-oxoglutarate + O2 = apigenin + CO2 + H(+) + H2O + succinate.
flavonoid 2-oxoglutarate-dependent dioxygenase
In addition to the desaturation of (2R,3R)-dihydroflavonols to flavonols, the enzyme from the satsuma Citrus unshiu also has a non-specific activity that trans-hydroxylates the flavanones (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to kaempferol and (2R,3R)-dihydrokaempferol, respectively.
2-oxoglutarate + a (2R,3R)-dihydroflavonol + O2 = a flavonol + CO2 + H2O + succinate.
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
In the other reaction (EC 1.13.12.19) the enzyme catalyzes the dioxygenation of 2-oxoglutarate forming ethylene and three molecules of carbon dioxide.
The enzyme catalyzes two cycles of the ethylene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethylene and succinate is 2:1.
2-oxoglutarate + L-arginine + O2 = (S)-1-pyrroline-5-carboxylate + CO2 + guanidine + H(+) + H2O + succinate.
The enzyme, characterized from the plant Sinopodophyllum hexandrum, is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
It catalyzes the closure of the central six-membered ring in the aryltetralin scaffold.
(-)-yatein + 2-oxoglutarate + O2 = (-)-deoxypodophyllotoxin + CO2 + H2O + succinate.
The enzyme is a member of the Fe(2+), 2-oxoglutarate-dependent oxygenases and requires Fe(2+).
It has been characterized from bacteria that form the isonitrile-functionalized compound paerucumarin.
(2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + 2-oxoglutarate + O2 = (2E)-3-(4-hydroxyphenyl)-2-isocyanoprop-2-enoate + CO2 + H2O + succinate.
tyrosine isonitrile desaturase/decarboxylase
The enzyme, characterized from the bacterium Xenorhabdus nematophila, is involved in rhabduscin biosynthesis.
The enzyme is a member of the Fe(2+), 2-oxoglutarate-dependent oxygenases.
It is similar to EC 1.14.20.9; however, the latter does not catalyze a decarboxylation of the substrate.
(2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + 2-oxoglutarate + H(+) + O2 = 4-[(E)-2-isocyanoethenyl]phenol + 2 CO2 + H2O + succinate.
3-[(Z)-2-isocyanoethenyl]-1H-indole synthase
The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, participates in the biosynthesis of hapalindole-type alkaloids.
The enzyme catalyzes an Fe(2+), 2-oxoglutarate-dependent monooxygenation at C-3, which is followed by decarboxylation and dehydration, resulting in the generation of a cis C-C double bond.
(2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + 2-oxoglutarate + H(+) + O2 = 3-[(Z)-2-isocyanoethenyl]-1H-indole + 2 CO2 + H2O + succinate.
3-[(E)-2-isocyanoethenyl]-1H-indole synthase
The enzyme has been characterized from an unidentified soil bacterium.
It catalyzes an Fe(2+), 2-oxoglutarate-dependent monooxygenation at C-3, which is followed by decarboxylation and dehydration, resulting in the generation of a trans C-C double bond.
(2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + 2-oxoglutarate + H(+) + O2 = 3-[(E)-2-isocyanovinyl]indole + 2 CO2 + H2O + succinate.
(6S)-6-hydroxyhyoscyamine + 2-oxoglutarate + O2 = CO2 + H(+) + H2O + scopolamine + succinate.
The enzyme, characterized from hapalindole-type alkaloids-producing cyanobacteria, is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyzes the chlorination of its substrates in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
2-oxoglutarate + chloride + H(+) + hapalindole U + O2 = CO2 + H2O + hapalindole G + succinate.
12-epi-fischerindole U + 2-oxoglutarate + chloride + H(+) + O2 = 12-epi-fischerindole G + CO2 + H2O + succinate.
L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
The enzyme, characterized from the bacterium Pseudomonas syringae, participates in syringomycin E biosynthesis.
The enzyme is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyzes the chlorination of its substrate in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
2-oxoglutarate + chloride + H(+) + L-threonyl-[peptidyl-carrier protein] + O2 = 4-chloro-L-threonyl-[peptidyl-carrier protein] + CO2 + H2O + succinate.
With NADH or NADPH as one donor, and the other dehydrogenated
Acts both as a dioxygenase and as a peroxidase.
(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2.
AH2 + kynurenate + O2 = 7,8-dihydro-7,8-dihydroxykynurenate + A.
A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) catalyzes both this reaction and that catalyzed by EC 1.14.99.12.
AH2 + O2 + progesterone = A + H2O + testosterone acetate.
17beta-estradiol + AH2 + O2 = 6beta-hydroxyestradiol-17beta + A + H2O.
androst-4-ene-3,17-dione 17-oxidoreductase
A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) catalyzes both this reaction and that catalyzed by EC 1.14.99.4.
AH2 + androst-4-ene-3,17-dione + O2 = A + H2O + testololactone.
AH2 + O2 + progesterone = 11alpha-hydroxyprogesterone + A + H2O.
4-methoxybenzoate monooxygenase (O-demethylating)
The bacterial enzyme consists of a ferredoxin-type protein and an iron-sulfur flavoprotein (FMN).
Also acts on 4-ethoxybenzoate, N-methyl-4-aminobenzoate and toluate.
The fungal enzyme acts best on veratrate.
4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + A + formaldehyde + H2O.
phylloquinone monooxygenase (2,3-epoxidizing)
AH2 + O2 + phylloquinone = 2,3-epoxyphylloquinone + A + H2O.
Latia-luciferin monooxygenase (demethylating)
Latia luciferin is (E)-2-methyl-4-(2,6,6-trimethyl-1-cyclohex-1-yl)-1-buten-1-ol formate.
The reaction possibly involves two enzymes, an oxygenase followed by a monooxygenase for the actual light-emitting step.
AH2 + Latia luciferin + 2 O2 = A + CO2 + formate + H(+) + H2O + hnu + oxidized Latia luciferin.
An enzyme from insect fat body or malpighian tubules.
NADPH can act as ultimate hydrogen donor.
AH2 + ecdysone + O2 = 20-hydroxyecdysone + A + H2O.
3-hydroxybenzoate + AH2 + O2 = 2,3-dihydroxybenzoate + A + H2O.
An enzyme system involving a flavoprotein (FMN) and two iron-sulfur proteins.
AH2 + O2 + pregna-4,9(11)-diene-3,20-dione = 9,11alpha-epoxypregn-4-ene-3,20-dione + A + H2O.
Also oxidizes 2,5-dihydroxypyridine, but does not act on 3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine.
2-hydroxypyridine + AH2 + O2 = 2,5-dihydroxypyridine + A + H2O.
Catalyzes the final step in the formation of the amino acid hypusine in eukaryotic initiation factor 5A (eIF-5A) (formerly eIF-4D).
[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O.
The enzyme has a high specificity for monoprenyl isoflavone.
The product of the prenyl epoxidation reaction contains an oxygen atom derived from O2, but not from H2O.
It is slowly and nonenzymically converted into the corresponding dihydrofurano derivative.
7-O-methylluteone + NADPH + H(+) + O2 = dihydrofurano derivatives + NADP(+) + H2O.
Highly specific for thiophene-2-carbonyl-CoA.
Tetrazolium salts can act as electron acceptors.
AH2 + O2 + thiophene-2-carbonyl-CoA = 5-hydroxythiophene-2-carbonyl-CoA + A + H(+) + H2O.
Unlike most other sterol hydroxylases, this enzyme is not a cytochrome P450.
Instead, it uses diiron cofactors to catalyze the hydroxylation of hydrophobic substrates.
The diiron cofactor can be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through interactions with clustered histidine or glutamate residues.
In cell cultures, this enzyme down-regulates cholesterol synthesis and the processing of sterol regulatory element binding proteins (SREBPs).
AH2 + cholesterol + O2 = 25-hydroxycholesterol + A + H2O.
Electrons are derived indirectly from ubiquinol.
AH2 + NH4(+) + O2 = A + H(+) + H2O + hydroxylamine.
Little activity with neurosporene or lycopene.
Involved in the biosynthesis of C30 carotenoids such as staphyloxanthin.
The enzyme oxidizes each methyl group to the hydroxymethyl and then a dihydroxymethyl group, followed by the spontaneous loss of water to give an aldehyde group.
4 AH2 + all-trans-4,4'-diapolycopene + 4 O2 = 4 A + all-trans-4,4'-diapolycopene-4,4'-dial + 6 H2O.
The enzyme participates in the Rut pyrimidine catabolic pathway.
FMNH2 + NADH + O2 + uracil = (Z)-3-ureidoacrylate + FMN + H(+) + H2O + NAD(+).
FMNH2 + NADH + O2 + thymine = (Z)-2-methylureidoacrylate + FMN + H(+) + H2O + NAD(+).
Isolated from the plant Larrea tridentata (creosote bush).
The enzyme has a strong preference for the 3' position of (+)-larreatricin.
(+)-larreatricin + AH2 + O2 = (+)-3'-hydroxylarreatricin + A + H2O.
heme oxygenase (staphylobilin-producing)
This enzyme, which is found in some pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host's hemoglobin.
The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % delta-staphylobilin, respectively.
5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + delta-staphylobilin + Fe(2+) + formaldehyde + 4 H2O.
5 AH2 + 2 H(+) + heme b + 4 O2 = 5 A + beta-staphylobilin + Fe(2+) + formaldehyde + 4 H2O.
gamma-glutamyl hercynylcysteine S-oxide synthase
The enzyme, found in bacteria, is specific for both hercynine and gamma-L-glutamyl-L-cysteine.
It is part of the biosynthesis pathway of ergothioneine.
gamma-L-glutamyl-L-cysteine + hercynine + O2 = gamma-L-glutamyl-hercynylcysteine S-oxide + H2O.
The enzyme, found in fungal species, is part of a fusion protein that also has the the activity of EC 2.1.1.44.
The enzyme can also use L-selenocysteine to produce hercynylselenocysteine, which can be converted to selenoneine.
hercynine + L-cysteine + O2 = H2O + S-(hercyn-2-yl)-L-cysteine S-oxide.
L-cysteinyl-L-histidinylsulfoxide synthase
The enzyme participates in ovothiol biosynthesis.
It also has some activity as EC 1.13.11.20, and can perform the reaction of EC 1.14.99.50.
L-cysteine + L-histidine + O2 = H2O + L-alanin-3-yl L-histidin-5-yl sulfoxide.
The enzyme cleaves chitin in an oxidative manner, releasing fragments of chitin with an N-acetylamino-D-glucono-1,5-lactone at the reducing end.
The initially formed lactone at the reducing end of the shortend chitin chain quickly hydrolyzes spontaneously to the aldonic acid.
In vitro ascorbate can serve as reducing agent.
[(1->4)-N-acetyl-beta-D-glucosaminyl]n+m + reduced acceptor + O2 = [(1->4)-N-acetyl-beta-D-glucosaminyl]m-1-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O.
lytic cellulose monooxygenase (C1-hydroxylating)
This enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner.
The cellulose fragments that are formed contain a D-glucono-1,5-lactone residue at the reducing end, which hydrolyzes quickly and spontaneously to the aldonic acid.
The electrons are provided in vivo by the cytochrome b domain of EC 1.1.99.18.
Ascorbate can serve as the electron donor in vitro.
[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = [(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-glucosyl]n + acceptor + H2O.
The enzyme cleaves starch in an oxidative manner.
It releases fragments of starch with a D-glucono-1,5-lactone at the reducing end.
The initially formed alpha-D-glucono-1,5-lactone at the reducing end of the shortend amylose chain quickly hydrolyzes spontaneously to the aldonic acid.
In vitro ascorbate has been found to be able to serve as reducing agent.
starch + reduced acceptor + O2 = D-glucono-1,5-lactone-terminated malto-oligosaccharides + short-chain malto-oligosaccharides + acceptor + H2O.
lytic cellulose monooxygenase (C4-dehydrogenating)
The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end.
Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue (cf. EC 1.14.99.54).
[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + acceptor + H2O.
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization.
The enzyme binds two stacked protoheme molecules per monomer.
Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde; instead, it forms unique products, named mycobilins, that retain the alpha-meso-carbon at the ring cleavage site as an aldehyde group.
EC 1.6.2.4 can act as electron donor in vitro.
3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + Fe(2+) + 3 H2O + mycobilin a.
3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + Fe(2+) + 3 H2O + mycobilin b.
heme oxygenase (biliverdin-IX-beta and delta-forming)
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, differs from EC 1.14.15.20 in that the heme substrate is rotated by approximately 110 degrees within the active site, resulting in cleavage at a different part of the ring.
It forms a mixture of about 70% biliverdin-IX-delta and 30% biliverdin-IX-beta.
3 AH2 + 3 H(+) + heme b + 3 O2 = 3 A + biliverdin delta + CO + Fe(2+) + 3 H2O.
3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + biliverdin beta + CO + Fe(2+) + 3 H2O.
Isolated from the fungus Psilocybe cubensis.
Involved in the biosynthesis of the psychoactive compound psilocybin.
AH2 + O2 + tryptamine = 4-hydroxytryptamine + A + H2O.
6-methoxy-3-methyl-2-(all-trans-polyprenyl)-1,4-benzoquinol 5-hydroxylase
The enzyme catalyzes the last hydroxylation reaction during the biosynthesis of ubiquinone.
a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O.
Isolated from the bacterium Streptomyces melanosporofaciens M1614-43f2.
Involved in the biosynthesis of cyclooctatin.
AH2 + cyclooctat-9-en-7-ol + O2 = A + cyclooctat-9-ene-5,7-diol + H2O.
AH2 + cyclooctat-9-ene-5,7-diol + O2 = A + cyclooctatin + H2O.
The enzyme, studied from algae, plants, fungi, and bacteria, adds an oxo group at position 4 of a carotenoid beta ring.
It is involved in the biosynthesis of carotenoids such as astaxanthin and flexixanthin.
The enzymes does not act on beta rings that are hydroxylated at position 3, such as in zeaxanthin (cf. EC 1.14.99.64).
The enzyme from the yeast Xanthophyllomyces dendrorhous is bifuntional and also catalyzes the activity of EC 1.14.15.24.
2 AH2 + all-trans-beta-carotene + 2 O2 = 2 A + echinenone + 3 H2O.
2 AH2 + echinenone + 2 O2 = 2 A + canthaxanthin + 3 H2O.
The enzyme has a similar activity to that of EC 1.14.99.63, but unlike that enzyme is able to also act on zeaxanthin.
2 AH2 + all-trans-zeaxanthin + 2 O2 = 2 A + all-trans-adonixanthin + 3 H2O.
2 AH2 + all-trans-adonixanthin + 2 O2 = 2 A + all-trans-(3S,3'S)-astaxanthin + 3 H2O.
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase
The enzyme, characterized from the bacterium Streptomyces venezuelae, participates in the biosynthesis of the antibiotic chloramphenicol.
It carries an oxygen-bridged dinuclear iron cluster.
The native electron donor remains unknown, and the enzyme was assayed in vitro using sodium dithionite.
The enzyme only acts on its substrate when it is loaded onto the peptidyl-carrier domain of the CmlP non-ribosomal peptide synthase.
4-amino-L-phenylalanyl-[peptidyl-carrier protein] + AH2 + O2 = (2R)-2-(4-aminophenyl)-L-seryl-[peptidyl-carrier protein] + A + H2O.
[histone-H3]-N(6),N(6)-dimethyl-L-lysine(4) FAD-dependent demethylase
The enzyme specifically removes methyl groups from mono- and dimethylated lysine(4) of histone 3.
During the reaction the substrate is oxidized by the FAD cofactor of the enzyme to generate the corresponding imine, which is subsequently hydrolyzed in the form of formaldehyde.
The enzyme is similar to flavin amine oxidases, and differs from all other known histone lysine demethylases, which are iron(II)- and 2-oxoglutarate-dependent dioxygenases.
The physiological electron acceptor is not known with certainty. In vitro the enzyme can use oxygen, which is reduced to hydrogen peroxide, but generation of hydrogen peroxide in the chromatin environment is unlikely as it will result in oxidative damage of DNA.
2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3].
alpha-N-dichloroacetyl-p-aminophenylserinol N-oxygenase
The enzyme, isolated from the bacterium Streptomyces venezuelae, is involved in the biosynthesis of the antibiotic chloramphenicol.
It contains a carboxylate-bridged binuclear non-heme iron cluster.
The components of the native electron chain have not been identified, although the immediate donor is likely to be an iron-sulfur protein.
The reaction mechanism involves formation of an extremely stable peroxo intermediate that catalyzes three individual two-electron oxidations via a hydroxylamine and a nitroso intermediates without releasing the intermediates.
AH2 + alpha-N-dichloroacetyl-p-aminophenylserinol + 2 O2 = A + chloramphenicol + 2 H2O.
The enzyme, characterized from the bacterium Streptomyces thioluteus, catalyzes an early step in the biosynthesis of the antibiotic aureothin.
The native electron donor has not been identified, but is likely an iron-sulfur protein.
The reaction mechanism involves formation of an extremely stable peroxo intermediate that catalyzes three two-electron oxidations via a hydroxylamine and dihydroxylamine intermediates.
4-aminobenzoate + AH2 + 2 O2 = 4-nitrobenzoate + A + 2 H2O.
tRNA 2-(methylsulfanyl)-N(6)-isopentenyladenosine(37) hydroxylase
tRNA 2-(methylsulfanyl)-N(6)-dimethylallyladenosine(37) hydroxylase
tRNA 2-methylthio-N(6)-isopentenyl adenosine(37) hydroxylase
The enzyme, found only within a small subset of facultative anaerobic bacteria, belongs to the nonheme diiron family.
The enzyme from Salmonella typhimurium was shown to catalyze a stereoselective (E) hydroxylation at the terminal C(4)-position of the prenyl group.
2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + AH2 + O2 = A + H2O + N(6)-[(2E)-4-hydroxy-3-methylbut-2-en-1-yl]-2-(methylsulfanyl)adenosine(37) in tRNA.
carotenoid 9,10(9',10')-cleavage dioxygenase
Presumably the enzyme acts twice on zeaxanthin cleaving 3-hydroxy-beta-ionone off each 3-hydroxy end group.
all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial.
2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin].
Fe(II)2-[transferrin] + H(+) + NAD(+) = Fe(III)2-[transferrin] + NADH.
cyanocobalamin reductase (cyanide-eliminating)
cyanocobalamin reductase (NADPH, cyanide-eliminating)
cyanocobalamin reductase (NADPH; CN-eliminating)
NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating)
The mammalian enzyme, which is cytosolic, can bind internalized cyanocobalamin and process it to cob(II)alamin by removing the upper axial ligand.
The product remains bound to the protein, which, together with its interacting partner MMADHC, transfers it directly to downstream enzymes involved in adenosylcobalamin and methylcobalamin biosynthesis.
In addition to its decyanase function, the mammalian enzyme also catalyzes an entirely different chemical reaction with alkylcobalamins, using the thiolate of glutathione for nucleophilic displacement, generating cob(I)alamin and the corresponding glutathione thioether (cf. EC 2.5.1.151).
2 cob(II)alamin-[cyanocobalamin reductase] + 2 hydrogen cyanide + NADP(+) = 2 apo-[cyanocobalamin reductase] + 2 cyanocob(III)alamin + H(+) + NADPH.
The enzyme catalyzes the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron.
The plant enzyme is involved in the transport of iron across plant plasma membranes.
The enzyme from the bacterium Paracoccus denitrificans can also reduce chromate.
2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH.
[methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing)
methionine synthase cob(II)alamin reductase (methylating)
The substrate of the enzyme is the inactivated cobalt(II) form of EC 2.1.1.13.
Electrons are transferred from NADPH to FAD to FMN.
H(+) + 2 methylcob(III)alamin-[methionine synthase] + NADP(+) + 2 S-adenosyl-L-homocysteine = 2 cob(II)alamin-[methionine synthase] + NADPH + 2 S-adenosyl-L-methionine.
The enzyme, which is widespread among bacteria, catalyzes the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron.
The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolyzed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine.
2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH.
The enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus is not active with uncomplexed Fe(III).
Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life.
They are formed from two subunits that coassemble in various ratios to form a spherical protein shell.
Thousands of mineralized iron atoms are stored within the core of the structure.
The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction.
4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide.
The enzyme, which belongs to the multicopper oxidase family, is found in many bacterial strains.
It oxidizes soluble Mn(II) to insoluble manganese oxides.
Since the enzyme is localized to the outer surface of the cell, its activity usually results in encrustation of the cells by the oxides.
The physiological function of bacterial Mn(II) oxidation remains unclear.
The enzyme, characterized from the bacterium Escherichia coli, is involved in copper tolerance under aerobic conditions.
The enzyme contains a substrate binding (type 1) copper site and a trinuclear copper center (consisting of type 2 and type 3 copper sites) in which oxygen binding and reduction takes place.
It also contains a methionine rich region that can bind additional copper ions. In vitro, if the substrate binding site is occupied by copper(II), the enzyme can function as a laccase-type quinol oxidase.
However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.
The enzyme in Acidithiobacillus ferrooxidans is a component of an electron transfer chain from Fe(II), comprising this enzyme, the copper protein rusticyanin, cytochrome c4, and cytochrome c oxidase (EC 7.1.1.9).
Fe(II) + rusticyanin = Fe(III) + reduced rusticyanin.
[Co(II) methylated amine-specific corrinoid protein] reductase
Methyltrophic corrinoid proteins must have the cobalt atom in the active cobalt(I) state to become methylated.
Because the cobalt(I)/cobalt(II) transformation has a very low redox potential the corrinoid cofactor is subject to adventitious oxidation to the cobalt(II) state, which renders the proteins inactive.
This enzyme, characterized from the methanogenic archaeon Methanosarcina barkeri, reduces cobalt(II) back to cobalt(I), restoring activity.
The enzyme acts on the corrinoid proteins involved in methanogenesis from methylamine, dimethylamine, and trimethylamine, namely MtmC, MtbC, and MttC, respectively.
While in vitro the enzyme can use Ti(III)-citrate as the electron donor, the in vivo donor is not known.
The enzyme from Methanosarcina barkeri contains a C-terminal [4Fe-4S] ferredoxin-like domain.
AH2 + ATP + 2 Co(II)-[methylamine-specific corrinoid protein] + H2O = A + ADP + 2 Co(I)-[methylamine-specific corrinoid protein] + 3 H(+) + phosphate.
AH2 + ATP + 2 Co(II)-[dimethylamine-specific corrinoid protein] + H2O = A + ADP + 2 Co(I)-[dimethylamine-specific corrinoid protein] + 3 H(+) + phosphate.
AH2 + ATP + 2 Co(II)-[trimethylamine-specific corrinoid protein] + H2O = A + ADP + 2 Co(I)-[trimethylamine-specific corrinoid protein] + 3 H(+) + phosphate.
CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system
cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase
cytidine diphospho-4-keto-6-deoxy-D-glucose reductase
NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase
One forms an enzyme-bound adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine phosphate, in which the 3-hydroxy group has been removed.
The second catalyzes the reduction of this adduct by NAD(P)H and release of the CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate.
CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H2O + NAD(+) = CDP-4-dehydro-6-deoxy-alpha-D-glucose + H(+) + NADH.
CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + H2O + NADP(+) = CDP-4-dehydro-6-deoxy-alpha-D-glucose + H(+) + NADPH.
Catalyzes the synthesis of catechin, catechin-4beta-ol (leucocyanidin) and the related flavan-3-ols afzelechin and gallocatechin, which are initiating monomers in the synthesis of plant polymeric proanthocyanidins or condensed tannins.
While 2,3-trans-3,4-cis-leucocyanidin is the preferred flavan-3,4-diol substrate, 2,3-trans-3,4-cis-leucodelphinidin and 2,3-trans-3, 4-cis-leucopelargonidin can also act as substrates, but more slowly.
NADH can replace NADPH but is oxidized more slowly.
(2R,3S)-catechin + H2O + NADP(+) = (2R,3S,4S)-leucocyanidin + H(+) + NADPH.
Acts on a variety of purines and aldehydes, including hypoxanthine.
The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein.
The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum center.
The mammallian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4).
During purification the enzyme is largely converted to an O2-dependent form, EC 1.17.3.2.
The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion.
H2O + NAD(+) + xanthine = H(+) + NADH + urate.
H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine.
The enzyme is capable of acting on a variety of nicotinate analogs to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate.
The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide.
H2O + NADP(+) + nicotinate = 6-hydroxynicotinate + H(+) + NADPH.
4-hydroxy-tetrahydrodipicolinate reductase
The substrate of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate, and the enzyme was classified accordingly as EC 1.3.1.26.
Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual substrate of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and that its activity includes a dehydration step, and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate reductase.
However, the identity of the substrate is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all.
(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH.
(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH.
The enzyme from most aerobic organisms is devoid of redox-active centers but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centers, flavin and a molybdenum center.
Together with EC 1.12.1.2, forms a system previously known as formate hydrogenlyase.
Characterized from the bacterium Moorella thermoacetica.
formate dehydrogenase (NAD(+), ferredoxin)
electron-bifurcating formate dehydrogenase
The enzyme complex, isolated from the bacterium Gottschalkia acidurici, couples the reduction of NAD(+) and the reduction of ferredoxin with formate via flavin-based electron bifurcation.
2 formate + NAD(+) + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 CO2 + H(+) + NADH + 2 reduced [2Fe-2S]-[ferredoxin].
This two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases, but differs from most other members of this family.
While most members contain an FAD cofactor, the large subunit of this enzyme contains three c-type cytochromes, enabling it to interact with the electron transfer chain, probably by delivering the electrons to a cytochrome oxidase.
2 Fe(III)-[cytochrome] + H2O + nicotinate = 6-hydroxynicotinate + 2 Fe(II)-[cytochrome] + 2 H(+).
2 Fe(III)-[cytochrome c] + H2O + lupanine = 17-hydroxylupanine + 2 Fe(II)-[cytochrome c] + 2 H(+).
formate dehydrogenase (cytochrome c-553)
The enzyme has been characterized from the bacterium Desulfovibrio vulgaris.
In vitro, yeast cytochrome c, ferricyanide and phenazine methosulfate can act as acceptors.
2 Fe(III)-[cytochrome c553] + formate = CO2 + 2 Fe(II)-[cytochrome c553] + H(+).
2-amino-4-hydroxypteridine + O2 = 2-amino-4,7-dihydroxypteridine + chemical entity.
Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1.
Under some conditions the product is mainly superoxide rather than peroxide: R-H + H2O + 2 O2 = ROH + 2 O2(.-) + 2 H(+).
The mammallian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4).
During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2).
H2O + hypoxanthine + O2 = H2O2 + xanthine.
6,8-dihydroxypurine + H2O + O2 = H2O2 + urate.
The enzyme also has a catalytically essential, labile selenium that can be removed by reaction with cyanide.
In Bacillus niacini, this enzyme is required for growth on nicotinic acid.
6-hydroxynicotinate + H2O + O2 = 2,6-dihydroxynicotinate + H2O2.
Even though oxygen is consumed, molecular oxygen is not incorporated into the product.
Catalysis starts by incorporation of an oxygen atom from a water molecule into the substrate.
The naphthalene-1,2,4,8-tetrol intermediate is then oxidized by molecular oxygen, which is reduced to water.
Also acts on 1,4-naphthoquinone, naphthazarin and 2-chloro-1,4-naphthoquinone.
2 juglone + O2 = 2 3,5-dihydroxy-1,4-naphthoquinone + 2 H(+).
This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair.
There are three types of this enzyme differing in their cofactors.
Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin.
In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical.
The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues.
A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position.
The disulfide bridge is reduced by the action of thioredoxin.
[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate.
[thioredoxin]-disulfide + dADP + H2O = [thioredoxin]-dithiol + ADP.
[thioredoxin]-disulfide + dUDP + H2O = [thioredoxin]-dithiol + UDP.
[thioredoxin]-disulfide + dGDP + H2O = [thioredoxin]-dithiol + GDP.
[thioredoxin]-disulfide + dCDP + H2O = [thioredoxin]-dithiol + CDP.
ribonucleoside-triphosphate reductase (thioredoxin)
The enzyme, characterized from the bacterium Lactobacillus leichmannii, is similar to class II ribonucleoside-diphosphate reductase (cf. EC 1.17.4.1); however, it is specific for the triphosphate versions of its substrates.
The enzyme contains an adenosylcobalamin cofactor that is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue.
This radical attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoacyl) radical.
[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-triphosphate.
vitamin-K-epoxide reductase (warfarin-sensitive)
The enzyme catalyzes the reduction of vitamin K 2,3-epoxide, which is formed by the activity of EC 4.1.1.90, back to its phylloquinol active form.
The enzyme forms a tight complex with EC 5.3.4.1, which transfers the required electrons from newly-synthesized proteins by catalyzing the formation of disulfide bridges.
The enzyme acts on the epoxide forms of both phylloquinone (vitamin K1) and menaquinone (vitamin K2).
Inhibited strongly by (S)-warfarin and ferulenol.
[protein]-disulfide + H2O + phylloquinone = 2,3-epoxyphylloquinone + [protein]-dithiol.
[protein]-disulfide + phylloquinol = [protein]-dithiol + phylloquinone.
vitamin-K-epoxide reductase (warfarin-insensitive)
Vitamin K 2,3-epoxide is reduced to 3-hydroxy- (and 2-hydroxy-) vitamin K by 1,4-dithiothreitol, which is oxidized to a disulfide.
Not inhibited by warfarin (cf. EC 1.17.4.4).
3-hydroxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + oxidized dithiothreitol = 1,4-dithiothreitol + 2,3-epoxyphylloquinone.
phenylacetyl-CoA:acceptor oxidoreductase
The enzyme is specific for phenylacetyl-CoA as substrate.
Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates.
The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen.
Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone.
A second enzyme, EC 3.1.2.25 converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
2 a ubiquinone + H2O + phenylacetyl-CoA = 2 a ubiquinol + phenylglyoxylyl-CoA.
This enzyme, characterized from the soil bacterium Pseudomonas sp. CBB1, catalyzes the incorporation of an oxygen atom originating from a water molecule into position C-8 of caffeine.
The enzyme utilizes short-tail ubiquinones as the preferred electron acceptor.
a ubiquinone + caffeine + H2O = 1,3,7-trimethylurate + a ubiquinol.
caffeine + H2O + ubiquinone-0 = 1,3,7-trimethylurate + ubiquinol-0.
Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm.
The system generates proton motive force under anaerobic conditions.
a quinone + formate + H(+) = a quinol + CO2.
a menaquinone + formate + H(+) = a menaquinol + CO2.
formate + H(+) + menaquinone-8 = CO2 + menaquinol-8.
a ubiquinone + formate + H(+) = a ubiquinol + CO2.
(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin)
(E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis.
Bacteria have a similar enzyme that uses flavodoxin rather than ferredoxin (cf. EC 1.17.7.3).
The enzyme from the plant Arabidopsis thaliana is active with photoreduced 5-deazaflavin but not with flavodoxin.
(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
This enzyme, which is present in plant chloroplasts, carries out the second step in the conversion of chlorophyll b to chlorophyll a (cf. EC 1.1.1.294).
chlorophyll a + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 7(1)-hydroxychlorophyll a + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
chlorophyllide a + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 7(1)-hydroxychlorophyllide a + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin)
Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis that is found in most bacteria.
Plants and cyanobacteria have a similar enzyme that utilizes ferredoxin rather than flavodoxin (cf. EC 1.17.7.1).
(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin].
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase
Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase.
This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis.
This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts.
The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and prenyl diphosphate.
H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin].
This enzyme, isolated from the bacteria Rhodopseudomonas palustris and Zymomonas mobilis, participates, along with EC 2.5.1.103 and EC 4.2.3.156, in the conversion of all-trans-farnesyl diphosphate to squalene.
Eukaryotes achieve the same goal in a single step, catalyzed by EC 2.5.1.21.
FAD + H(+) + H2O + squalene = FADH2 + hydroxysqualene.
4-methylphenol dehydrogenase (hydroxylating)
p-cresol-(acceptor) oxidoreductase (hydroxylating)
This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit.
The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water.
The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm.
The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
4-methylphenol + H2O + 4 oxidized [azurin] = 4-hydroxybenzaldehyde + 4 H(+) + 4 reduced [azurin].
This enzyme, characterized from the bacterium Pseudomonas sp SG-MS2, catalyzes the incorporation of an oxygen atom originating from a water molecule into position C-6 of the lignan (+)-pinoresinol.
The enzyme consists of a flavoprotein subunit and a c-type cytochrome subunit.
Electrons that originate in the substrate are transferred via the FAD cofactor and the cytochrome subunit to the blue-copper protein azurin.
(+)-pinoresinol + H2O + 2 oxidized [azurin] = (+)-6-hydroxypinoresinol + 2 H(+) + 2 reduced [azurin].
bacteriochlorophyllide c C-7(1)-hydroxylase
The enzyme, found in green sulfur bacteria (Chlorobiaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme.
It catalyzes two consecutive hydroxylation reactions of the C-7 methyl group of bacteriochlorophyllide c to form a geminal diol intermediate that spontaneously dehydrates to produce the formyl group of bacteriochlorophyllide e.
a bacteriochlorophyllide c + H2O + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + a bacteriochlorophyllide e + 2 H(+) + 2 L-methionine.
a bacteriochlorophyllide d + H2O + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + a bacteriochlorophyllide f + 2 H(+) + 2 L-methionine.
coenzyme F420-dependent formate dehydrogenase
coenzyme F420 reducing formate dehydrogenase
The enzyme from methanogenic archaea is a involved in formate-dependent H2 production.
formate + 2 H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = CO2 + reduced coenzyme F420-(gamma-L-Glu)(n).
Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase.
The two enzymes form the formate-hydrogen lyase complex.
The enzyme contains a selenocysteine residue.
Involved in the anaerobic catabolism of ethylbenzene by denitrifying bacteria.
Ethylbenzene is the preferred substrate; the enzyme from some strains oxidizes propylbenzene, 1-ethyl-4-fluorobenzene, 3-methylpent-2-ene and ethylidenecyclohexane.
p-benzoquinone or ferrocenium can act as electron acceptor.
A + ethylbenzene + H2O = (S)-1-phenylethanol + AH2.
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration.
However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate and not via hydration of a 24(25) double bond.
In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate.
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + A + H2O = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + AH2.
Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 3.5.2.1 and EC 3.5.1.95.
Mammals, plants and other microorganisms utilize the reductive pathway, comprising EC 1.3.1.1 or EC 1.3.1.2, EC 3.5.2.2 and EC 3.5.1.6, with the ultimate degradation products being an L-amino acid, NH3 and CO2.
A + H2O + uracil = AH2 + barbiturate + H(+).
A + H2O + thymine = 5-methylbarbiturate + AH2 + H(+).
This enzyme catalyzes the last step in the bacterial biosynthetic pathway to queuosine, the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn.
Two types of enzymes are known to catalyze this activity.
QueG enzymes are cobalamin-dependent, while QueH enzymes contain a [4Fe-4S] metallocluster along with an adjacent coordinated iron metal.
AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA.
The enzyme, characterized from the bacterium Castellaniella defragrans 65Phen, hydroxylates the R- and S-enantiomers at a similar rate.
The in vivo electron acceptor may be a heterodimeric electron transfer flavoprotein (ETF).
(4S)-limonene + A + H2O = (4S)-perillyl alcohol + AH2.
(4R)-limonene + A + H2O = (4R)-perillyl alcohol + AH2.
The enzyme catalyzes the conversion of heme o to heme a by two successive hydroxylations of the methyl group at C-8, using water as the oxygen source.
The first hydroxylation forms heme i, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme a.
The electrons produced by the reaction are transferred to a heme b cofactor.
However, the electron acceptor that is used to restore the heme b cofactor to its oxidized state is still not known (both a thioredoxin-like protein and menaquinol have been proposed).
2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a.
The enzyme, characterized from the bacterium Sterolibacterium denitrificans, participates in the anaerobic degradation of cholesterol.
The enzyme can accept several substrates including vitamin D3.
The enzyme contains a bis(guanylyl molybdopterin) cofactor, five [Fe-S] clusters, and one heme b.
A + cholest-4-en-3-one + H2O = 25-hydroxycholest-4-en-3-one + AH2.
A + cholest-1,4-dien-3-one + H2O = 25-hydroxycholest-1,4-dien-3-one + AH2.
A + cholest-4,6-dien-3-one + H2O = 25-hydroxycholest-4,6-dien-3-one + AH2.
7-dehydrocholesterol + A + H2O = AH2 + cholesta-5,7-dien-3beta,25-diol.
3-oxocholestane + A + H2O = 25-hydroxy 3-oxocholestane + AH2.
3-oxo-Delta(1)-steroid hydratase/dehydrogenase
The enzyme, characterized from the bacterium Steroidobacter denitrificans, is involved in the anaetrobic degradation of steroids.
It is specific to 3-oxo-Delta(1)-steroids such as androsta-1-ene-3,17-dione and Delta(1)-dihydrotestosterone and does not act on 3-oxo-Delta(4)-steroids.
A + a 3-oxo-Delta(1)-steroid + H2O = a steroid 1,3-dione + AH2.
A + Delta(1)-dihydrotestosterone + H2O = 17beta-hydroxyandrostan-1,3-dione + AH2.
5alpha-androst-1-ene-3,17-dione + A + H2O = 5alpha-androstan-1,3,17-trione + AH2.
Acting on iron-sulfur proteins as donors
dihydronicotinamide adenine dinucleotide-rubredoxin reductase
reduced nicotinamide adenine dinucleotide-rubredoxin reductase
rubredoxin-nicotinamide adenine dinucleotide reductase
The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin.
The reaction does not occur when NADPH is substituted for NADH.
H(+) + NAD(+) + 2 reduced [rubredoxin] = NADH + 2 oxidized [rubredoxin].
In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin.
H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin].
The reaction is written for a [2Fe-2S] ferredoxin, which is characteristic of some mono- and dioxygenase systems.
Some anaerobic bacteria have a 2[4Fe-4S] ferredoxin, which transfers two electrons.
H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin].
rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase
The enzyme reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient.
H(+) + NADP(+) + 2 reduced [rubredoxin] = NADPH + 2 oxidized [rubredoxin].
The enzyme from Pseudomonas putida reduces putidaredoxin.
Involved in the camphor monooxygenase system (see EC 1.14.15.1).
H(+) + NAD(+) + 2 reduced [2Fe-2S]-[putidaredoxin] = NADH + 2 oxidized [2Fe-2S]-[putidaredoxin].
nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
The enzyme, which transfers electrons from NADPH to adrenodoxin molecules, is the first component in the mitochondrial cytochrome P450 electron transfer systems, and is involved in the biosynthesis of all steroid hormones.
H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized [adrenodoxin].
ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase ferredoxin-specific)
The enzyme from the aerobic bacterium Ralstonia sp. U2 donates electrons to both EC 1.14.12.12 and EC 1.14.13.172.
The enzyme from Pseudomonas NCIB 9816 is specific for the ferredoxin associated with naphthalene dioxygenase.
The enzyme is a complex of two components (namely dinitrogen reducatse and dinitrogenase).
Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component.
Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine.
The reduction is initiated by formation of hydrogen in stoichiometric amounts.
Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia.
In the absence of a suitable substrate, hydrogen is slowly formed.
Ferredoxin may be replaced by flavodoxin (see EC 1.19.6.1).
The enzyme does not reduce CO (cf. EC 1.18.6.2).
16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate.
This enzyme, originally isolated from the bacterium Azotobacter vinelandii, is a complex of two components (namely dinitrogen reductase and dinitrogenase).
Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of ATP, transfers an electron from ferredoxin to the dinitrogenase component.
Dinitrogenase is a vanadium-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazine and hydrazine.
Compared with EC 1.18.6.1, this enzyme produces more dihydrogen and consumes more ATP per dinitrogen molecule being reduced.
Unlike EC 1.18.6.1, this enzyme can also use CO as substrate, producing ethylene, ethane and propane.
40 ATP + 40 H2O + N2 + 12 reduced [2Fe-2S]-[ferredoxin] = 40 ADP + 26 H(+) + 3 H2 + 2 NH4(+) + 12 oxidized [2Fe-2S]-[ferredoxin] + 40 phosphate.
This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis.
In photosynthetic organisms it is involved in the photosynthetic electron transport chain.
NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized [flavodoxin].
Composed of two components, dinitrogen reductase and dinitrogenase, that can be separated but are both required for nitrogenase activity.
Dinitrogen reductase is a [4Fe-4S] protein, which, at the expense of ATP, transfers electrons from a dedicated flavodoxin to dinitrogenase.
Dinitrogenase is a protein complex that contains either a molybdenum-iron cofactor, a vanadium-iron cofactor, or an iron-iron cofactor, that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia.
The reduction is initiated by formation of hydrogen.
The enzyme can also reduce acetylene to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia.
Some enzymes utilize ferredoxin rather than flavodoxin as the electron donor (see EC 1.18.6.1).
16 ATP + 16 H2O + N2 + 4 reduced [flavodoxin] = 16 ADP + 18 H(+) + H2 + 2 NH4(+) + 4 oxidized [flavodoxin] + 16 phosphate.
Acting on phosphorus or arsenic in donors
NADP(+) is a poor substitute for NAD(+) in the enzyme from Pseudomonas stutzeri WM88.
H2O + NAD(+) + phosphonate = H(+) + NADH + phosphate.
Unlike EC 1.20.9.1 it does not use azurin as acceptor.
arsenite + 2 Fe(III)-[cytochrome c] + H2O = arsenate + 2 Fe(II)-[cytochrome c] + 3 H(+).
arsenate reductase (glutathione/glutaredoxin)
The enzyme is part of a system for detoxifying arsenate.
The substrate binds to a catalytic cysteine residue, forming a covalent thiolate--As(V) intermediate.
A tertiary intermediate is then formed between the arsenic, the enzyme's cysteine, and a glutathione cysteine.
This intermediate is reduced by glutaredoxin, which forms a dithiol with the glutathione, leading to the dissociation of arsenite.
Thus reduction of As(V) is mediated by three cysteine residues: one in ArsC, one in glutathione, and one in glutaredoxin.
Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7; in other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway that produces non-toxic organoarsenical compounds; cf. EC 1.20.4.4.
[glutaredoxin]-dithiol + arsenate + glutathione + H(+) = arsenite + glutathionyl-S-S-[glutaredoxin] + H2O.
The product, methylarsonite, is biologically methylated by EC 2.1.1.137 to form cacodylic acid.
2 glutathione + H(+) + methylarsonate = glutathione disulfide + H2O + methylarsonous acid.
Reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate.
The substrate arseno-mycothiol is formed by EC 2.8.4.2.
A second mycothiol recycles mycoredoxin and forms mycothione.
[mycoredoxin]-L-cysteine + arseno-mycothiol + H(+) = [mycoredoxin]-S-mycothiol-L-cysteine + arsenite.
The enzyme, characterized in bacteria of the Firmicutes phylum, is specific for thioredoxin.
It has no activity with glutaredoxin (cf. EC 1.20.4.1).
Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7; in other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway that produces non-toxic organoarsenical compounds.
The enzyme also has the activity of EC 3.1.3.48.
[thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-disulfide + arsenite + H2O.
The enzyme also uses a c-type cytochrome or O2 as acceptors.
arsenite + H2O + 2 oxidized [azurin] = arsenate + 3 H(+) + 2 reduced [azurin].
Unlike EC 1.20.4.1 reduced glutaredoxin cannot serve as a reductant.
A + arsenite + H2O = AH2 + arsenate + H(+).
Catalyzing the reaction X-H + Y-H = 'X-Y'
The enzyme activity has only been demonstrated in the direction of 3-deiodination.
2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH.
The enzyme, characterized from Corynebacterium strains able to grow on 2,4-dichlorobenzoate, forms part of the 2,4-dichlorobenzoate degradation pathway.
4-chlorobenzoyl-CoA + chloride + NADP(+) = 2,4-dichlorobenzoyl-CoA + NADPH.
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = 2 H2O + isopenicillin N.
Oxidation of the O-methoxyphenol structure forms the methylenedioxy group of berberine.
2 columbamine + O2 = 2 berberine + 2 H2O.
Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge ('berberine bridge') of (S)-tetrahydroprotoberberines.
The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants.
(S)-reticuline + O2 = (S)-scoulerine + H(+) + H2O2.
sulochrin oxidase [(+)-bisdechlorogeodin-forming]
Also acts on several diphenols and phenylenediamines, but has low affinity for these substrates.
Involved in the biosynthesis of mold metabolites related to the antibiotic griseofulvin.
2 H(+) + O2 + 2 sulochrin = 2 (2S)-bisdechlorogeodin + 2 H2O.
sulochrin oxidase [(-)-bisdechlorogeodin-forming]
2 H(+) + O2 + 2 sulochrin = 2 (2R)-bisdechlorogeodin + 2 H2O.
Plays a key role in the yellow coloration of flowers such as Antirrhinum majus (snapdragon).
The enzyme is a homolog of plant polyphenol oxidase and catalyzes two separate chemical transformations, i.e. 3-hydroxylation and oxidative cyclization (2',-dehydrogenation).
H2O2 activates reaction (1) but inhibits reaction (2).
Originally considered to act on the phenol but now thought to mainly act on the 4'-O-beta-glucoside in vivo.
2',4,4',6'-tetrahydroxychalcone 4'-O-beta-D-glucoside + H(+) + O2 = aureusidin 6-O-beta-glucoside + H2O.
2 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + 2 H(+) + O2 = 2 aureusidin 6-O-beta-glucoside + 2 H2O.
2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + H(+) + O2 = bracteatin 6-O-beta-glucoside + H2O.
Delta(1)-tetrahydrocannabinolic acid synthase
Part of the cannabinoids biosynthetic pathway in the plant Cannabis sativa.
The enzyme can also convert cannabinerolate (the (Z)-isomer of cannabigerolate) to Delta(9)-THCA with lower efficiency.
The traditional numbering called Delta(9)-tetrahydrocannabinolate, Delta(1)-tetrahydrocannabinolate.
Systematic peripheral numbering is now recommended.
cannabigerolate + O2 = Delta(9)-tetrahydrocannabinolate + H2O2.
cannabinerolate + O2 = Delta(9)-tetrahydrocannabinolate + H2O2.
Part of the cannabinoids biosynthetic pathway of the plant Cannabis sativa.
The enzyme can also convert cannabinerolate to cannabidiolate with lower efficiency.
cannabigerolate + O2 = cannabidiolate + H2O2.
A pyruvoyl- and L-selenocysteine-containing enzyme found in a number of Clostridial species.
The pyruvoyl group, located on the PrdA subunit, binds the substrate, while the selenocysteine residue, located on the PrdB subunit, attacks the alpha-C-atom of D-proline, leading to a reductive cleavage of the C-N-bond of the pyrrolidine ring and formation of a selenoether.
The selenoether is cleaved by a cysteine residue of PrdB, resulting in a mixed selenide-sulfide bridge, which is restored to its reduced state by another selenocysteine protein, PrdC.
5-aminopentanoate is released from PrdA by hydrolysis, regenerating the pyruvoyl moiety.
The resulting mixed selenide-sulfide bridge in PrdC is reduced by NADH.
5-aminopentanoate + [PrdC protein]-Se-L-selenocysteinyl-S-L-cysteine = [PrdC protein]-L-selenocysteine/L-cysteine + D-proline.
The reaction is observed only in the direction of glycine reduction.
The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C.
Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release.
Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate.
Only subunit B distinguishes this enzyme from EC 1.21.4.3 and EC 1.21.4.4.
[thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) = [thioredoxin]-dithiol + glycine + H(+) + phosphate.
The reaction is observed only in the direction of sarcosine reduction.
Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for sarcosine binding and methylamine release.
Only subunit B distinguishes this enzyme from EC 1.21.4.2 and EC 1.21.4.4.
[thioredoxin]-disulfide + acetyl phosphate + H2O + methylamine = [thioredoxin]-dithiol + H(+) + phosphate + sarcosine.
The reaction is observed only in the direction of betaine reduction.
Only subunit B distinguishes this enzyme from EC 1.21.4.2 and EC 1.21.4.3.
[thioredoxin]-disulfide + acetyl phosphate + H2O + trimethylamine = [thioredoxin]-dithiol + glycine betaine + H(+) + phosphate.
tetrachlorohydroquinone reductive dehalogenase
The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, converts tetrachlorohydroquinone to 2,6-dichlorohydroquinone in two steps, via 2,3,6-trichlorohydroquinone, using glutathione as the reducing agent.
The enzyme is sensitive to oxidation - when an internal L-cysteine residue is oxidized, the enzyme produces 2,3,5-trichloro-6-(glutathion-S-yl)-hydroquinone and 2,6-dichloro-3-(glutathion-S-yl)-hydroquinone instead of its normal products.
2,6-dichlorohydroquinone + chloride + glutathione disulfide + H(+) = 2,3,6-trichlorohydroquinone + 2 glutathione.
2,3,6-trichlorohydroquinone + chloride + glutathione disulfide = 2,3,5,6-tetrachlorohydroquinone + 2 glutathione.
cyclic dehypoxanthinyl futalosine synthase
This enzyme is a member of the 'AdoMet radical' (radical SAM) family.
The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
dehypoxanthine futalosine + S-adenosyl-L-methionine = 5'-deoxyadenosine + cyclic dehypoxanthinylfutalosinate + H(+) + L-methionine.
The enzyme is a dimeric heme-protein oxidase that catalyzes the oxidative dimerization of two L-tryptophan-derived molecules to form dichlorochromopyrrolic acid, the precursor for the fused six-ring indolocarbazole scaffold of rebeccamycin.
In vivo the enzyme uses hydrogen peroxide, formed by the enzyme upstream in the biosynthetic pathway (EC 1.4.3.23) as the electron acceptor.
However, the enzyme is also able to catalyze the reaction using molecular oxygen.
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + H(+) + 2 H2O + NH4(+).
2 2-iminio-3-(indol-3-yl)propanoate + H2O2 = chromopyrrolate + H(+) + 2 H2O + NH4(+).
anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase
This radical AdoMet enzyme participates in the biosynthesis of chlorophyllide a in anaerobic bacteria, catalyzing the formation of an isocyclic ring.
The same transformation is achieved in aerobic organisms by the oxygen-dependent EC 1.14.13.81.
H2O + Mg-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 4 H(+) + 3 L-methionine.
This bacterial enzyme, which is a member of the radical SAM protein family, catalyzes the formation of a C-C bond between C-4 of glutamate and C-3 of tyrosine residues of the PqqA protein (which are separated by three amino acid residues).
This is the first enzymic step in the biosynthesis of the bacterial enzyme cofactor pyrroloquinoline quinone (PQQ).
The reaction is dependent on the presence of flavodoxin and the accessory protein PqqD.
[PQQ precursor protein] + S-adenosyl-L-methionine = 5'-deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-methionine.
cytochrome c and various dyes can act as acceptor.
A + beta-cyclopiazonate = AH2 + alpha-cyclopiazonate.
The enzyme activity has only been demonstrated in the direction of 5-deiodination.
This removal of the 5-iodine, i.e. from the inner ring, largely inactivates the hormone thyroxine.
3,3',5'-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine.
The enzyme activity has only been demonstrated in the direction of 5'-deiodination, which renders the thyroid hormone more active.
The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics.
For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide.
3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine.
tetrachloroethene reductive dehalogenase
This enzyme allows the common pollutant tetrachloroethene to support bacterial growth and is responsible for disposal of a number of chlorinated hydrocarbons by this organism.
The enzyme also reduces trichloroethene to dichloroethene.
Although the physiological reductant is unknown, the supply of reductant in some organisms is via reduced menaquinone, itself formed from molecular hydrogen, via EC 1.12.5.1.
Methylviologen can act as electron donor.
A + chloride + H(+) + trichloroethene = AH2 + tetrachloroethene.
(+)-pinoresinol-(+)-lariciresinol reductase
The reaction is catalyzed in vivo in the opposite direction to that shown.
A multifunctional enzyme that further reduces the product to the lignan (-)-secoisolariciresinol (EC 1.23.1.2).
Isolated from the plants Forsythia intermedia, Thuja plicata (western red cedar), Linum perenne (perennial flax) and Linum corymbulosum.
The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol.
(+)-lariciresinol + NADP(+) = (+)-pinoresinol + H(+) + NADPH.
A multifunctional enzyme that also reduces (+)-pinoresinol (EC 1.23.1.1).
(-)-secoisolariciresinol + NADP(+) = (+)-lariciresinol + H(+) + NADPH.
(-)-pinoresinol-(-)-lariciresinol reductase
A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol (EC 1.23.1.4).
Isolated from the plants Thuja plicata (western red cedar), Linum perenne (perennial flax) and Arabidopsis thaliana (thale cress).
(-)-lariciresinol + NADP(+) = (-)-pinoresinol + H(+) + NADPH.
A multifunctional enzyme that also reduces (-)-pinoresinol (EC 1.23.1.3).
Isolated from the plants Thuja plicata (western red cedar) and Linum corymbulosum.
(+)-secoisolariciresinol + NADP(+) = (-)-lariciresinol + H(+) + NADPH.
Along with EC 1.14.15.21, this enzyme forms part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts.
It is activated by a low pH of the thylakoid lumen (produced by high light intensity).
Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II.
In higher plants the enzyme reacts with all-trans-diepoxides, such as violaxanthin, and all-trans-monoepoxides, but in the alga Mantoniella squamata, only the diepoxides are good substrates.
all-trans-violaxanthin + 2 L-ascorbate = all-trans-zeaxanthin + 2 H2O + 2 L-dehydroascorbate.
Flavins or benzylviologen can act as acceptor.
1,2,3,5-Tetrahydroxybenzene acts as a cosubstrate for the conversion of pyrogallol into phloroglucinol, and for a number of similar isomerizations.
The enzyme is provisionally listed here, but might be considered as the basis for a new class in the transferases, analogous to the aminotransferases.
1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,2,3,5-tetrahydroxybenzene + 1,3,5-trihydroxybenzene.
[formate-C-acetyltransferase]-activating enzyme
[pyruvate formate-lyase]-activating enzyme
formate acetyltransferase activating enzyme
formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving)
PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving)
pyruvate formate-lyase 1 activating enzyme
A single glycine residue in EC 2.3.1.54 is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter.
The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue.
glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin].
The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma).
Nitrate, nitrite, chlorate and sulfate are not substrates.
A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
H2O + menaquinone-8 + selenite = menaquinol-8 + selenate.
Contains chlorophyll, phylloquinones, carotenoids and [4Fe-4S] clusters.
Cytochrome c6 can act as an alternative electron donor, and flavodoxin as an alternative acceptor in some species.
hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin].
nicotinamide + S-adenosyl-L-methionine = 1-methylnicotinamide + S-adenosyl-L-homocysteine.
guanidinoacetate + S-adenosyl-L-methionine = creatine + H(+) + S-adenosyl-L-homocysteine.
thetin--homocysteine S-methyltransferase
dimethylsulfonioacetate + L-homocysteine = (methylsulfanyl)acetate + H(+) + L-methionine.
Some other hydroxyindoles also act as acceptor, more slowly.
N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin + S-adenosyl-L-homocysteine.
betaine--homocysteine S-methyltransferase
glycine betaine + L-homocysteine = L-methionine + N,N-dimethylglycine.
The mammalian enzymes act more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols.
a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine.
nicotinate + S-adenosyl-L-methionine = N-methylnicotinate + S-adenosyl-L-homocysteine.
histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine.
H2S and a variety of alkyl, aryl and heterocyclic thiols and hydroxy thiols can act as acceptors.
a thiol + S-adenosyl-L-methionine = a methyl thioether + H(+) + S-adenosyl-L-homocysteine.
The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.
L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-methionine.
L-homocysteine + S-adenosyl-L-methionine = H(+) + L-methionine + S-adenosyl-L-homocysteine.
magnesium protoporphyrin IX methyltransferase
(-)-S-adenosyl-L-methionine:magnesium-protoporphyrin IX methyltransferase
magnesium-protoporphyrin O-methyltransferase
S-adenosyl-L-methionine:magnesium-protoporphyrin O-methyltransferase
S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase
S-adenosylmethioninemagnesium protoporphyrin methyltransferase
S-adenosylmethionine-magnesium protoporphyrin methyltransferase
Mg-protoporphyrin IX + S-adenosyl-L-methionine = Mg-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-homocysteine.
L-methionine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine.
5-methyltetrahydrofolate--homocysteine S-methyltransferase
5-methyltetrahydrofolate--homocysteine transmethylase
B12 N(5)-methyltetrahydrofolate homocysteine methyltransferase
methionine synthase (cobalamin-dependent)
methyltetrahydrofolate--homocysteine vitamin B12 methyltransferase
N(5)-methyltetrahydrofolate--homocysteine cobalamin methyltransferase
N(5)-methyltetrahydrofolate methyltransferase
N(5)-methyltetrahydrofolic--homocysteine vitamin B12 transmethylase
N-methyltetrahydrofolate:L-homocysteine methyltransferase
tetrahydropteroylglutamate methyltransferase
tetrahydropteroylglutamic methyltransferase
The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II).
Reactivation by reductive methylation is catalyzed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system.
For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8.
In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2).
Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, which acts only on the triglutamate.
(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine.
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
cobalamin-independent methionine synthase
methionine synthase (cobalamin-independent)
methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase
tetrahydropteroylglutamate-homocysteine transmethylase
The enzyme from Escherichia coli also requires a reducing system.
Unlike EC 2.1.1.13 this enzyme does not contain cobalamin.
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate.
5-methyltetrahydropteroyltri-L-glutamate + L-selenohomocysteine = L-selenomethionine + tetrahydropteroyltri-L-glutamate.
Oleic acid is the most effective fatty acid acceptor.
a fatty acid + S-adenosyl-L-methionine = a fatty acid methyl ester + S-adenosyl-L-homocysteine.
methylene-fatty-acyl-phospholipid synthase
unsaturated-phospholipid methyltransferase
The enzyme transfers a methyl group to the 10-position of a Delta(9)-olefinic acyl chain in phosphatidylglycerol, phosphatidylinositol, or, more slowly, phosphatidylethanolamine; subsequent proton transfer produces a 10-methylene group (cf. EC 2.1.1.79).
1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(10-methylene)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine.
phosphatidylethanolamine N-methyltransferase
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + a (1->4)-alpha-D-glucooligosaccharide = S-adenosyl-L-homocysteine + an oligosaccharide containing 6-methyl-D-glucose units.
trimethylsulfonium--tetrahydrofolate N-methyltransferase
(6S)-5,6,7,8-tetrahydrofolate + trimethylsulfonium = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + dimethyl sulfide + H(+).
Thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine.
Inhibited by 5-methyltetrahydrofolate pentaglutamate.
Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3.
glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + sarcosine.
methylamine--glutamate N-methyltransferase
L-glutamate + methylamine = N-methyl-L-glutamate + NH4(+).
carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine.
Acts on a wide variety of simple alkyl-, methoxy- and halo-phenols.
phenol + S-adenosyl-L-methionine = anisole + H(+) + S-adenosyl-L-homocysteine.
2-iodophenol + S-adenosyl-L-methionine = 1-iodo-2-methoxybenzene + H(+) + S-adenosyl-L-homocysteine.
Has some activity on phenylethylamine analogs.
S-adenosyl-L-methionine + tyramine = H(+) + N-methyltyramine + S-adenosyl-L-homocysteine.
Acts on various phenylethanolamines; converts noradrenaline into adrenaline.
phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-methylphenylethanolamine + S-adenosyl-L-homocysteine.
(R)-noradrenaline + S-adenosyl-L-methionine = (R)-adrenaline + H(+) + S-adenosyl-L-homocysteine.
tRNA (guanine(46)-N(7))-methyltransferase
The enzyme specifically methylates guanine(46) at N(7) in tRNA.
guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine.
tRNA (guanosine(18)-2'-O)-methyltransferase
The enzyme catalyzes the methylation of guanosine(18) in tRNA.
guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine.
tRNA (uracil(54)-C(5))-methyltransferase
5-methyluridine(54) tRNA methyltransferase
transfer RNA uracil(54) 5-methyltransferase
Unlike this enzyme, EC 2.1.1.74 uses 5,10-methylenetetrahydrofolate and FADH2 to supply the atoms for methylation of U54.
S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine.
deoxyribonucleic (cytosine-5-)-methyltransferase
deoxyribonucleic acid (cytosine-5-)-methyltransferase
deoxyribonucleic acid modification methylase
methylphosphotriester-DNA methyltransferase
site-specific DNA-methyltransferase (cytosine-specific)
See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine.
Puromycin is the antibiotic derived from N(6)-dimethyladenosine by replacing the 3'-hydroxy group with an amino group and acylating this with 4-O-methyltyrosine.
O-demethylpuromycin + S-adenosyl-L-methionine = H(+) + puromycin + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase
myo-inositol + S-adenosyl-L-methionine = 1D-3-O-methyl-myo-inositol + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase
S-adenosylmethionine:myo-inositol 3-methyltransferase
myo-inositol + S-adenosyl-L-methionine = 1D-1-O-methyl-myo-inositol + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-4-methionine:sterol Delta(24)-methyltransferase
S-adenosyl-L-methionine:Delta(24(23))-sterol methyltransferase
Acts on a range of sterols with a 24(25)-double bond in the side chain.
While zymosterol is the preferred substrate it also acts on desmosterol, 5alpha-cholesta-7,24-dien-3beta-ol, 5alpha-cholesta-5,7,24-trien-3beta-ol, 4alpha-methylzymosterol and others.
S-Adenosyl-L-methionine attacks the Si face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
S-adenosyl-L-methionine + zymosterol = fecosterol + H(+) + S-adenosyl-L-homocysteine.
cycloartenol + S-adenosyl-L-methionine = 24-methylenecycloartanol + H(+) + S-adenosyl-L-homocysteine.
The enzyme prefers flavones with vicinal 3',4'-dihydroxyl groups.
a 3'-hydroxyflavone + S-adenosyl-L-methionine = a 3'-methoxyflavone + H(+) + S-adenosyl-L-homocysteine.
Part of the biosynthetic pathway of ergothioneine.
L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + 3 S-adenosyl-L-homocysteine.
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP.
The enzyme catalyzes the methylation of daidzein and genistein.
It does not methylate naringenin, apigenin, luteolin or kaempferol.
a 4'-hydroxyisoflavone + S-adenosyl-L-methionine = a 4'-methoxyisoflavone + H(+) + S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Streptomyces griseus, is involved in the biosynthesis of the antibacterial drug indolmycin.
indole-3-pyruvate + S-adenosyl-L-methionine = (R)-3-(indol-3-yl)-2-oxobutanoate + H(+) + S-adenosyl-L-homocysteine.
An enzyme of very broad specificity; many primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.
a primary amine + S-adenosyl-L-methionine = a methylated primary amine + H(+) + S-adenosyl-L-homocysteine.
a secondary amine + S-adenosyl-L-methionine = a methylated secondary amine + H(+) + S-adenosyl-L-homocysteine.
a tertiary amine + S-adenosyl-L-methionine = a methylated tertiary amine + H(+) + S-adenosyl-L-homocysteine.
Methylates the 11-carboxy group of the monoterpenoid loganate.
loganate + S-adenosyl-L-methionine = loganin + S-adenosyl-L-homocysteine.
putrescine + S-adenosyl-L-methionine = H(+) + N-methylputrescine + S-adenosyl-L-homocysteine.
dCMP is methylated by formaldehyde in the presence of tetrahydrofolate.
CMP, dCTP and CTP can act as acceptor, more slowly.
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dCMP = 5-methyldeoxycytidine 5'-phosphate + 7,8-dihydrofolate.
an adenosine in tRNA + S-adenosyl-L-methionine = an N(6)-methyladenosine in tRNA + H(+) + S-adenosyl-L-homocysteine.
messenger ribonucleate guanine 7-methyltransferase
messenger RNA guanine 7-methyltransferase
The terminal N(7)-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine.
messenger RNA (nucleoside-2'-)-methyltransferase
mRNA (nucleoside-2'-O)-methyltransferase
This enzyme catalyzes the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules.
This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses.
The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine.
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine.
[cytochrome c]-lysine N-methyltransferase
cytochrome c-specific protein-lysine methyltransferase
cytochrome c-specific protein methylase III
L-lysyl-[cytochrome c] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[cytochrome c] + S-adenosyl-L-homocysteine.
[calmodulin]-L-lysine + S-adenosyl-L-methionine = [calmodulin]-N(6)-methyl-L-lysine + H(+) + S-adenosyl-L-homocysteine.
tRNA 5-(aminomethyl)-2-thiouridylate-methyltransferase
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate.
5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine.
mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase
mRNA containing an N(6),2'-O-dimethyladenosine cap.
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + H(+) + S-adenosyl-L-homocysteine.
methylated-DNA--[protein]-cysteine S-methyltransferase
This protein is involved in the repair of methylated DNA.
Unlike EC 3.2.2.20 and EC 3.2.2.21, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide.
Since the methyl transfer is irreversible, the enzyme can only catalyze a single turnover.
a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein].
a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein].
3-demethylubiquinol 3-O-methyltransferase
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
3-demethylubiquinone-9 3-methyltransferase
5-demethylubiquinone-9 methyltransferase
This enzyme is involved in ubiquinone biosynthesis.
Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units.
However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.
The enzymes from yeast, Escherichia coli and rat also catalyze the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reaction that is classified as EC 2.1.1.114).
a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine.
3-demethylubiquinol-9 + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + ubiquinol-9.
3-demethylubiquinol-6 + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + ubiquinol-6.
3-demethylubiquinol-7 + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + ubiquinol-7.
3-demethylubiquinol-8 + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + ubiquinol-8.
3-demethylubiquinol-10 + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + ubiquinol-10.
As well as licodione [1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)-1,3-propanedione], the 2''-hydroxy-derivative and isoliquiritigenin can act as acceptors, more slowly.
licodione + S-adenosyl-L-methionine = 2'-O-methyllicodione + H(+) + S-adenosyl-L-homocysteine.
Also acts, more slowly, on thiopyrimidines and aromatic thiols.
S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
mercaptopurine + S-adenosyl-L-methionine = 6-methylthiopurine + H(+) + S-adenosyl-L-homocysteine.
6-thioguanine + S-adenosyl-L-methionine = 6-methylthioguanine + H(+) + S-adenosyl-L-homocysteine.
3,4-dihydroxybenzaldehyde and catechol can act as acceptor, more slowly.
(E)-caffeate + S-adenosyl-L-methionine = (E)-ferulate + H(+) + S-adenosyl-L-homocysteine.
5-hydroxyfuranocoumarin 5-O-methyltransferase
Converts bergaptol into bergapten, which has therapeutic potential in the treatment of psoriasis as it has photosensitizing and antiproliferative activities.
Methylates the 5-hydroxy group of some hydroxy- and methylcoumarins, such as 5-hydroxyxanthotoxin, but has little activity on non-coumarin phenols; caffeate, 5-hydroxyferulate and daphnetin are not substrates.
Cu(2+), Zn(2+) and Co(2+) cause enzyme inhibition.
a 5-hydroxyfurocoumarin + S-adenosyl-L-methionine = a 5-methoxyfurocoumarin + H(+) + S-adenosyl-L-homocysteine.
bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-L-homocysteine.
5-hydroxyxanthotoxin + S-adenosyl-L-methionine = isopimpinellin + S-adenosyl-L-homocysteine.
8-hydroxyfuranocoumarin 8-O-methyltransferase
Converts xanthotoxol into xanthotoxin, which has therapeutic potential in the treatment of psoriasis as it has photosensitizing and antiproliferative activities.
Methylates the 8-hydroxy group of some hydroxy- and methylcoumarins, but has little activity on non-coumarin phenols.
an 8-hydroxyfurocoumarin + S-adenosyl-L-methionine = an 8-methoxyfurocoumarin + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + xanthotoxol = H(+) + S-adenosyl-L-homocysteine + xanthotoxin.
phosphatidyl-N-methylethanolamine N-methyltransferase
Also catalyzes the transfer of a further methylgroup, producing phosphatidylcholine.
1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine.
1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine.
site-specific DNA-methyltransferase (adenine-specific)
This is a large group of enzymes, most of which form so-called 'restriction-modification systems', with nucleases that possess similar site specificity (the nucleases are listed as either EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5).
a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine.
methylenetetrahydrofolate--tRNA-(uracil(54)-C(5))-methyltransferase [NAD(P)H-oxidizing]
folate/FAD-dependent tRNA T54 methyltransferase
Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified.
One almost universal post-translational modification is the conversion of U(54) into ribothymidine in the TPsiC loop, and this modification is found in most species studied to date.
Unlike this enzyme, which uses 5,10-methylenetetrahydrofolate and NAD(P)H to supply the atoms for methylation of U(54), EC 2.1.1.35 uses S-adenosyl-L-methionine.
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+).
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NADP(+).
Naringenin (5,7,4'-trihydroxyflavanone) can also act as an acceptor, but more slowly.
apigenin + S-adenosyl-L-methionine = acacetin + H(+) + S-adenosyl-L-homocysteine.
Related enzymes bring about the 3-O-methylation of other flavonols, such as galangin and kaempferol.
quercetin + S-adenosyl-L-methionine = 3',4',5,7-tetrahydroxy-3-methoxyflavone + H(+) + S-adenosyl-L-homocysteine.
protein-L-isoaspartate(D-aspartate) O-methyltransferase
L-isoaspartyl protein carboxyl methyltransferase
protein beta-aspartate O-methyltransferase
D-aspartate (but not L-aspartate) residues in proteins can also act as acceptors.
[protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine.
[protein]-D-aspartate + S-adenosyl-L-methionine = [protein]-D-aspartate methyl ester + S-adenosyl-L-homocysteine.
Also acts on isoorientin 2''-O-rhamnoside.
Involved in the biosynthesis of flavones.
isoorientin + S-adenosyl-L-methionine = H(+) + isoscoparin + S-adenosyl-L-homocysteine.
cyclopropane-fatty-acyl-phospholipid synthase
Adds a methylene group across the 9,10 position of a Delta(9)-olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol forming a cyclopropane derivative (cf. EC 2.1.1.16).
1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine.
methyl-accepting chemotaxis protein O-methyltransferase
Forms ester groups with L-glutamate residues in a number of membrane proteins.
L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine.
Involved with EC 2.1.1.76 and EC 2.1.1.83 in the methylation of quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum.
Does not act on flavones, dihydroflavonols, or their glucosides.
3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine.
3,7-dimethylquercetin 4'-O-methyltransferase
3,7-dimethylquercitin 4'-O-methyltransferase
3,7-Dimethylquercetagetin can also act as acceptor.
Involved with EC 2.1.1.76 and EC 2.1.1.82 in the methylation of quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum.
3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine = 3',5-dihydroxy-3,4',7-trimethoxyflavone + H(+) + S-adenosyl-L-homocysteine.
methylquercetagetin 6-O-methyltransferase
The enzymes from Chrysosplenium americanum also methylates 3,7,3'-trimethylquercetagetin at the 6-position.
3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,6,7-trimethoxyflavone + S-adenosyl-L-homocysteine.
Highly specific for histidine residues, for example, in actin.
L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine.
tetrahydromethanopterin S-methyltransferase
N(5)-methyltetrahydromethanopterin--coenzyme M methyltransferase
tetrahydromethanopterin methyltransferase
Involved in the formation of methane from CO in methanogenic archaea.
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 Na(+)(out).
pyridine + S-adenosyl-L-methionine = N-methylpyridinium + S-adenosyl-L-homocysteine.
8-hydroxyquercetin 8-O-methyltransferase
8-hydroxyquercitin 8-O-methyltransferase
Also acts on 8-hydroxykaempferol, but not on the glycosides of 8-hydroxyflavonols.
An enzyme from the flower buds of Lotus corniculatus.
3,3',4',5,7,8-hexahydroxyflavone + S-adenosyl-L-methionine = 3,3',4',5,7-pentahydroxy-8-methoxyflavone + H(+) + S-adenosyl-L-homocysteine.
tetrahydrocolumbamine 2-O-methyltransferase
Involved in the biosynthesis of the berberine alkaloids.
(S)-tetrahydrocolumbamine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + tetrahydropalmatine.
methanol--corrinoid protein Co-methyltransferase
methanol--5-hydroxybenzimidazolylcobamide Co-methyltransferase
The enzyme, which catalyzes the transfer of methyl groups from methanol to a methanol-specific corrinoid protein (MtaC), is involved in methanogenesis from methanol.
Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state.
During methylation the cobalt is oxidized to the Co(III) state.
Free cob(I)alamin can substitute for the corrinoid protein in vitro.
Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen.
Co(I)-[methanol-specific corrinoid protein] + H(+) + methanol = H2O + methyl-Co(III)-[methanol-specific corrinoid protein].
Oximes of C4 to C6 aldehydes can act as acceptors.
The most active substrate is 2-methylbutyraldoxime.
2-methylpropanal oxime + S-adenosyl-L-methionine = 2-methylpropanal O-methyloxime + H(+) + S-adenosyl-L-homocysteine.
11-demethyl-17-deacetylvindoline 11-methyltransferase
11-O-demethyl-17-O-deacetylvindoline O-methyltransferase
S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O-methyltransferase
Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.
16-hydroxytabersonine + S-adenosyl-L-methionine = 16-methoxytabersonine + H(+) + S-adenosyl-L-homocysteine.
The enzymes from plants and photosynthetic bacteria have similar efficiency with the gamma and delta isomers of tocopherols and tocotrienols.
gamma-tocopherol + S-adenosyl-L-methionine = (+)-alpha-tocopherol + H(+) + S-adenosyl-L-homocysteine.
delta-tocopherol + S-adenosyl-L-methionine = beta-tocopherol + H(+) + S-adenosyl-L-homocysteine.
gamma-tocotrienol + S-adenosyl-L-methionine = alpha-tocotrienol + H(+) + S-adenosyl-L-homocysteine.
delta-tocotrienol + S-adenosyl-L-methionine = beta-tocotrienol + H(+) + S-adenosyl-L-homocysteine.
Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide, 1,4-dithiane and many other thioethers.
dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + trimethylsulfonium.
3-hydroxyanthranilate 4-C-methyltransferase
Involved in the biosynthesis of the antibiotic actinomycin in Streptomyces antibioticus.
3-hydroxyanthranilate + S-adenosyl-L-methionine = 3-hydroxy-4-methylanthranilate + H(+) + S-adenosyl-L-homocysteine.
This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14.
Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314).
In the archaeon Pyrococcus horikoshii the enzyme acts on His(600) of elongation factor 2.
2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine.
3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase
16-methoxy-2,3-dihydro-3-hydroxytabersonine methyltransferase
16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase
S-adenosyl-L-methionine:16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase
Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle Catharanthus roseus.
(3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + S-adenosyl-L-methionine = deacetoxyvindoline + H(+) + S-adenosyl-L-homocysteine.
protein-S-isoprenylcysteine O-methyltransferase
isoprenylcysteine carboxylmethyltransferase
prenylated protein carboxyl methyltransferase
prenylcysteine carboxyl methyltransferase
C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, more slowly.
[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine.
The 3-hydroxyl group of a 2-O-methyl-6-deoxy-D-allose residue in the macrolide antibiotic macrocin acts as methyl acceptor.
macrocin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + tylosin.
The 2-hydroxyl group of a 6-deoxy-D-allose residue in demethylmacrocin acts as methyl acceptor.
Also acts on demethyllactenocin giving lactenocin.
Involved in the biosynthesis of the macrolide antibiotic tylosin.
demethylmacrocin + S-adenosyl-L-methionine = H(+) + macrocin + S-adenosyl-L-homocysteine.
The enzyme may catalyze the transfer of two further methyl groups to the product.
phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N-methylethanolamine phosphate + S-adenosyl-L-homocysteine.
N-methylethanolamine phosphate + S-adenosyl-L-methionine = H(+) + N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine.
N,N-dimethylethanolamine phosphate + S-adenosyl-L-methionine = H(+) + phosphocholine + S-adenosyl-L-homocysteine.
trans-caffeoyl-CoA 3-O-methyltransferase
(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine.
N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase
Involved in the biosynthesis of phytoalexins.
N-benzoyl-4-hydroxyanthranilate + S-adenosyl-L-methionine = H(+) + N-benzoyl-4-methoxyanthranilate + S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Streptomyces laurentii, is involved in thiostrepton biosynthesis.
It is a radical SAM enzyme that contains a [4Fe-4S] center and a cobalamin cofactor.
The enzyme first transfers the methyl group from SAM to the bound cobalamin, followed by transfer from methylcobalamin to L-tryptophan, resulting in retention of the original methyl group configuration.
The second transfer is likely to involve a CH3 radical species formed from methylcobalamin by the concerted action of a partially ligated radical SAM [4Fe-4S](2+/1+) center.
L-tryptophan + S-adenosyl-L-methionine = 2-methyl-L-tryptophan + H(+) + S-adenosyl-L-homocysteine.
uroporphyrinogen-III C-methyltransferase
adenosylmethionine-uroporphyrinogen III methyltransferase
S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase
This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2.
It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III.
The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4).
In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction.
Also involved in the biosynthesis of cobalamin.
2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine.
3,4-Dehydro-6-hydroxymellein can also act as acceptor.
6-Methoxymellein is a phytoalexin produced by carrot tissue.
6-hydroxymellein + S-adenosyl-L-methionine = 6-methoxymellein + H(+) + S-adenosyl-L-homocysteine.
demethylsterigmatocystin 6-O-methyltransferase
Dihydrodemethylsterigmatocystin can also act as acceptor.
Involved in the biosynthesis of aflatoxins in fungi.
6-demethylsterigmatocystin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + sterigmatocystin.
S-adenosyl-L-methionine:sterigmatocystin 7-O-methyltransferase
Dihydrosterigmatocystin can also act as acceptor.
S-adenosyl-L-methionine + sterigmatocystin = 8-O-methylsterigmatocystin + H(+) + S-adenosyl-L-homocysteine.
dihydrosterigmatocystin + S-adenosyl-L-methionine = 8-O-methyldihydrosterigmatocystin + H(+) + S-adenosyl-L-homocysteine.
Involved in the biosynthesis of acridine alkaloids in plant tissues.
anthranilate + S-adenosyl-L-methionine = H(+) + N-methylanthranilate + S-adenosyl-L-homocysteine.
glucuronoxylan D-glucuronate + n S-adenosyl-L-methionine = glucuronoxylan 4-O-methyl-D-glucuronate + n H(+) + n S-adenosyl-L-homocysteine.
site-specific DNA-methyltransferase (cytosine-N(4)-specific)
This is a large group of enzymes, the majority of which, with enzymes of similar site specificity listed as EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5, form so-called restriction-modification systems.
a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine.
polyprenyldihydroxybenzoate methyltransferase
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
dihydroxyhexaprenylbenzoate methyltransferase
The enzymes from yeast and rat also catalyze the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively (this activity is classified as EC 2.1.1.64).
3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine.
3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-hexaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine.
3,4-dihydroxy-5-all-trans-heptaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-heptaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine.
3,4-dihydroxy-5-all-trans-octaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-octaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine.
3,4-dihydroxy-5-all-trans-nonaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-nonaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine.
3,4-dihydroxy-5-all-trans-decaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-decaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine.
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase
(RS)-tetrahydrobenzylisoquinoline N-methyltransferase
Broad substrate specificity for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines; including coclaurine, norcoclaurine, isococlaurine, norarmepavine, norreticuline and tetrahydropapaverine.
Both R- and S-enantiomers are methylated.
Participates in the pathway leading to benzylisoquinoline alkaloid synthesis in plants.
The physiological substrate is likely to be coclaurine.
Was earlier termed norreticuline N-methyltransferase.
However, norreticuline has not been found to occur in nature and that name does not reflect the broad specificity of the enzyme for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines.
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-methionine = H(+) + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline + S-adenosyl-L-homocysteine.
3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase
Involved in isoquinoline alkaloid metabolism in plants.
Has also been shown to catalyze the methylation of (RS)-laudanosoline, (S)-3'-hydroxycoclaurine and (RS)-7-O-methylnoraudanosoline.
(S)-3'-hydroxy-N-methylcoclaurine + S-adenosyl-L-methionine = (S)-reticuline + H(+) + S-adenosyl-L-homocysteine.
The product of this reaction is a precursor for protoberberine alkaloids in plants.
(S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine.
The product of this reaction is a protoberberine alkaloid that is widely distributed in the plant kingdom.
Distinct in specificity from EC 2.1.1.88.
columbamine + S-adenosyl-L-methionine = H(+) + palmatine + S-adenosyl-L-homocysteine.
10-hydroxydihydrosanguinarine 10-O-methyltransferase
Part of the pathway for synthesis of benzophenanthridine alkaloids in plants.
10-hydroxydihydrosanguinarine + S-adenosyl-L-methionine = dihydrochelirubine + H(+) + S-adenosyl-L-homocysteine.
12-hydroxydihydrochelirubine 12-O-methyltransferase
Part of the pathway for synthesis of benzophenanthridine alkaloid macarpine in plants.
12-hydroxydihydrochelirubine + S-adenosyl-L-methionine = dihydromacarpine + H(+) + S-adenosyl-L-homocysteine.
6-O-methylnorlaudanosoline 5'-O-methyltransferase
Nororientaline is a precursor of the alkaloid papaverine.
6-O-methylnorlaudanosoline + S-adenosyl-L-methionine = H(+) + nororientaline + S-adenosyl-L-homocysteine.
(S)-tetrahydroprotoberberine N-methyltransferase
tetrahydroprotoberberine cis-N-methyltransferase
Involved in the biosynthesis of isoquinoline alkaloids in plants.
(S)-canadine + S-adenosyl-L-methionine = (S)-N-methylcanadine + S-adenosyl-L-homocysteine.
[cytochrome c]-methionine S-methyltransferase
S-adenosyl-L-methionine + [cytochrome c]-methionine = S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine.
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase
The enzyme catalyzes three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39).
Only the three methylated form is observed.
The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13).
L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L-homocysteine.
(RS)-norcoclaurine 6-O-methyltransferase
The enzyme will also catalyze the 6-O-methylation of (RS)-norlaudanosoline to form 6-O-methyl-norlaudanosoline, but this alkaloid has not been found to occur in plants.
norcoclaurine + S-adenosyl-L-methionine = coclaurine + H(+) + S-adenosyl-L-homocysteine.
(S)-norcoclaurine + S-adenosyl-L-methionine = (S)-coclaurine + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase
The enzyme from Vigna umbellata is highly specific for S-adenosyl-L-methionine.
The enzyme also methylates 1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5-pentahydroxycyclohexanone, D,L-2,3,4,6/5-pentacyclohexanone and 2,2'-anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than that of myo-inositol.
myo-inositol + S-adenosyl-L-methionine = 1D-4-O-methyl-myo-inositol + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine--precorrin-2 methyltransferase
This enzyme participates in the aerobic (late cobalt insertion) cobalamin biosynthesis pathway.
See EC 2.1.1.151 for the equivalent enzyme that participates in the anaerobic cobalamin biosynthesis pathway.
precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A + S-adenosyl-L-homocysteine.
The enzyme, which participates in the aerobic (late cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyzes a crucial reaction where the tetrapyrrole ring contracts as a result of methylation of C-17.
See EC 2.1.1.272 for the corresponding enzyme that participates in the anaerobic cobalamin biosynthesis pathway.
precorrin-3B + S-adenosyl-L-methionine = 3 H(+) + precorrin-4 + S-adenosyl-L-homocysteine.
precorrin-6B C(5,15)-methyltransferase (decarboxylating)
precorrin-6Y C(5,15)-methyltransferase (decarboxylating)
The enzyme participates in the aerobic (late cobalt insertion) adenosylcobalamin biosynthesis pathway.
The enzyme from the bacterium Pseudomonas denitrificans is a fusion protein with two active sites; one catalyzes the methylation at C-15 followed by decarboxylation of the C-12 acetate side chain, while the other catalyzes the methylation at C-5.
The corresponding activities in the anaerobic adenosylcobalamin biosynthesis pathway are catalyzed by EC 2.1.1.196 and EC 2.1.1.289.
precorrin-6B + 2 S-adenosyl-L-methionine = CO2 + 3 H(+) + precorrin-8X + 2 S-adenosyl-L-homocysteine.
In the aerobic (late cobalt insertion) cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A.
The first of the four steps is carried out by EC 1.14.13.83 (CobG), yielding precorrin-3B as the product.
This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5, and precorrin-6A, respectively.
See EC 2.1.1.271 for the C(11)-methyltransferase enzyme that participates in the anaerobic cobalamin biosynthesis pathway.
precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-adenosyl-L-homocysteine.
The enzyme from Trichoderma virgatum, when cultured in the presence of halogenated phenol, also acts on a range of mono-, di- and trichlorophenols.
2,4,6-trichlorophenol + S-adenosyl-L-methionine = 2,4,6-trichloroanisole + S-adenosyl-L-homocysteine.
An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes or detoxification of inorganic arsenous acid in animals.
The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism), from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues via a disulfide bond cascade pathway.
Most of the substrates undergo two methylations and are converted to dimethylarsinous acid.
However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane.
Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system.
The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
[thioredoxin]-dithiol + arsenic triglutathione + 2 H2O + S-adenosyl-L-methionine = [thioredoxin]-disulfide + 3 glutathione + H(+) + methylarsonous acid + S-adenosyl-L-homocysteine.
2 [thioredoxin]-dithiol + arsenic triglutathione + H2O + 2 S-adenosyl-L-methionine = 2 [thioredoxin]-disulfide + dimethylarsinous acid + 3 glutathione + 2 H(+) + 2 S-adenosyl-L-homocysteine.
3 [thioredoxin]-dithiol + arsenic triglutathione + 3 S-adenosyl-L-methionine = 3 [thioredoxin]-disulfide + 3 glutathione + 3 H(+) + 3 S-adenosyl-L-homocysteine + trimethylarsine.
3'-demethylstaurosporine O-methyltransferase
3'-demethoxy-3'-hydroxystaurosporine O-methyltransferase
Catalyzes the final step in the biosynthesis of staurosporine, an alkaloidal antibiotic that is a potent inhibitor of protein kinases, especially protein kinase C.
3'-demethylstaurosporine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + staurosporine.
The enzyme is specific for the (S)-isomer of coclaurine.
Norcoclaurine can also act as an acceptor.
(S)-coclaurine + S-adenosyl-L-methionine = (S)-N-methylcoclaurine + H(+) + S-adenosyl-L-homocysteine.
jasmonic acid carboxyl methyltransferase
9,10-Dihydrojasmonic acid is a poor substrate for the enzyme.
The enzyme does not convert 12-oxo-phytodienoic acid (a precursor of jasmonic acid), salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters.
Enzyme activity is inhibited by the presence of divalent cations, e.g., Ca(2+), Cu(2+), Mg(2+) and Zn(2+).
jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate + S-adenosyl-L-homocysteine.
S-Adenosyl-L-methionine methylates the Si face of the 24(25)-double bond with elimination of a hydrogen atom from the pro-Z methyl group at C-25.
cycloartenol + S-adenosyl-L-methionine = cyclolaudenol + H(+) + S-adenosyl-L-homocysteine.
24-methylenelophenol C-24(1)-methyltransferase
This is the second methylation step of plant sterol biosynthesis (cf. EC 2.1.1.142).
24-methylidenelophenol + S-adenosyl-L-methionine = (Z)-24-ethylidenelophenol + H(+) + S-adenosyl-L-homocysteine.
Also catalyzes the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly.
While the enzyme from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate as the product, that from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.145).
S-adenosyl-L-methionine + trans-aconitate = (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine.
While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144).
S-adenosyl-L-methionine + trans-aconitate = (E)-2-(methoxycarbonylmethyl)but-2-enedioate + S-adenosyl-L-homocysteine.
Acts on eugenol and chavicol as well as isoeugenol.
S-adenosyl-L-methionine + trans-isoeugenol = H(+) + S-adenosyl-L-homocysteine + trans-isomethyleugenol.
2 NADPH + palmatine + S-adenosyl-L-methionine = corydaline + 2 NADP(+) + S-adenosyl-L-homocysteine.
All thymidylate synthases catalyze a reductive methylation involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5-position of dUMP and a two electron reduction of the methylene group to a methyl group.
Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a source of reducing equivalents, which are derived from NADPH.
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+).
The enzyme from alfalfa can methylate daidzein, genistein and 6,7,4'-trihydroxyisoflavone but not flavones or flavanones.
a 7-hydroxyisoflavone + S-adenosyl-L-methionine = a 7-methoxyisoflavone + H(+) + S-adenosyl-L-homocysteine.
cobalt-factor II C(20)-methyltransferase
Cobalt-precorrin-2 C(20)-methyltransferase
This enzyme participates in the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway.
See EC 2.1.1.130 for the equivalent enzyme that participates in the aerobic cobalamin biosynthesis pathway.
Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 + H(+) + S-adenosyl-L-homocysteine.
The enzyme, which participates in the aerobic (late cobalt insertion) cobalamin biosythesis pathway, catalyzes two reactions - the methylation of carbon C(1) of precorrin-5, and its deacetylation, forming precorrin-6A.
See EC 2.1.1.195 for the C(1)-methyltransferase that participates in the anaerobic cobalamin biosynthesis pathway.
H2O + precorrin-5 + S-adenosyl-L-methionine = acetate + 2 H(+) + precorrin-6A + S-adenosyl-L-homocysteine.
vitexin 2''-O-rhamnoside 7-O-methyltransferase
The flavonoids vitexin and isovitexin 2''-O-arabinoside do not act as substrates for the enzyme from oats (Avena sativa).
S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = 7-O-methylvitexin 2''-O-beta-L-rhamnoside + H(+) + S-adenosyl-L-homocysteine.
isoliquiritigenin 2'-O-methyltransferase
While EC 2.1.1.154 can use licodione as a substrate, EC 2.1.1.65 cannot use isoliquiritigenin as a substrate.
isoliquiritigenin + S-adenosyl-L-methionine = 2'-O-methylisoliquiritigenin + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase
The enzyme acts on the hydroxy group in the 4'-position of some flavones, flavanones and isoflavones.
Kaempferol, apigenin and kaempferol triglucoside are substrates, as is genistein, which reacts more slowly.
Compounds with an hydroxy group in the 3' and 4' positions, such as quercetin and eriodictyol, do not act as substrates.
kaempferol + S-adenosyl-L-methionine = H(+) + kaempferide + S-adenosyl-L-homocysteine.
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process.
This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157.
Differs from EC 2.1.1.20, as it can further methylate the product of the first reaction.
Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction.
glycine + 2 S-adenosyl-L-methionine = 2 H(+) + N,N-dimethylglycine + 2 S-adenosyl-L-homocysteine.
sarcosine/dimethylglycine N-methyltransferase
sarcosine-dimethylglycine methyltransferase
sarcosine dimethylglycine N-methyltransferase
The first enzyme, EC 2.1.1.156, leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of this enzyme.
Both of these enzymes can catalyze the formation of N,N-dimethylglycine from sarcosine.
The reactions are strongly inhibited by S-adenosyl-L-homocysteine.
2 S-adenosyl-L-methionine + sarcosine = glycine betaine + 2 H(+) + 2 S-adenosyl-L-homocysteine.
The enzyme is specific for xanthosine, as XMP and xanthine cannot act as substrates.
The enzyme does not have N(1)- or N(3)- methylation activity.
This is the first methylation step in the production of caffeine.
S-adenosyl-L-methionine + xanthosine = 7-methylxanthosine + S-adenosyl-L-homocysteine.
Can also catalyze the conversion of paraxanthine into caffeine, although the paraxanthine pathway is considered to be a minor pathway for caffeine biosynthesis.
This is the third enzyme in the caffeine biosynthesis pathway.
7-methylxanthine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + theobromine.
Paraxanthine is the best substrate for this enzyme but the paraxanthine pathway is considered to be a minor pathway for caffeine biosynthesis.
S-adenosyl-L-methionine + theobromine = caffeine + H(+) + S-adenosyl-L-homocysteine.
1,7-dimethylxanthine + S-adenosyl-L-methionine = caffeine + H(+) + S-adenosyl-L-homocysteine.
This enzyme, from the marine cyanobacterium Synechococcus sp. strain WH8102, differs from EC 2.1.1.157 in that it cannot use sarcosine as an alternative substrate.
Betaine is a 'compatible solute' that enables cyanobacteria to cope with osmotic stress by maintaining a positive cellular turgor.
N,N-dimethylglycine + S-adenosyl-L-methionine = glycine betaine + H(+) + S-adenosyl-L-homocysteine.
glycine/sarcosine/dimethylglycine N-methyltransferase
glycine sarcosine dimethylglycine N-methyltransferase
Unlike EC 2.1.1.156, EC 2.1.1.157 and EC 2.1.1.161, this enzyme, from the halophilic methanoarchaeon Methanohalophilus portucalensis, can methylate glycine and all of its intermediates to form the compatible solute betaine.
glycine + 3 S-adenosyl-L-methionine = glycine betaine + 3 H(+) + 3 S-adenosyl-L-homocysteine.
2-heptaprenyl-1,4-naphthoquinone methyltransferase
The enzyme catalyzes the last step in menaquinone biosynthesis.
It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase).
The enzyme from Escherichia coli also catalyzes the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3-octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone.
The enzyme probably acts on menaquinol rather than menaquinone.
a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine.
6-methoxy-2-all-trans-octaprenyl-1,4-benzoquinone + S-adenosyl-L-methionine = 3-methyl-6-methoxy-2-all-trans-octaprenyl-1,4-benzoquinone + H(+) + S-adenosyl-L-homocysteine.
a 2-demethylmenaquinone + S-adenosyl-L-methionine = a menaquinone + H(+) + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-8 + S-adenosyl-L-methionine = H(+) + menaquinol-8 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-6 + S-adenosyl-L-methionine = H(+) + menaquinol-6 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-7 + S-adenosyl-L-methionine = H(+) + menaquinol-7 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-9 + S-adenosyl-L-methionine = H(+) + menaquinol-9 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-10 + S-adenosyl-L-methionine = H(+) + menaquinol-10 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-11 + S-adenosyl-L-methionine = H(+) + menaquinol-11 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-12 + S-adenosyl-L-methionine = H(+) + menaquinol-12 + S-adenosyl-L-homocysteine.
2-demethylmenaquinol-13 + S-adenosyl-L-methionine = H(+) + menaquinol-13 + S-adenosyl-L-homocysteine.
demethylrebeccamycin-D-glucose O-methyltransferase
Catalyzes the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes.
The enzyme is able to use a wide variety substrates, tolerating variation on the imide heterocycle, deoxygenation of the sugar moiety, and even indolocarbazole glycoside anomers.
4'-demethylrebeccamycin + S-adenosyl-L-methionine = H(+) + rebeccamycin + S-adenosyl-L-homocysteine.
This enzyme contributes to the methyl halide emissions from Arabidopsis.
iodide + S-adenosyl-L-methionine = iodomethane + S-adenosyl-L-homocysteine.
chloride + S-adenosyl-L-methionine = chloromethane + S-adenosyl-L-homocysteine.
bromide + S-adenosyl-L-methionine = bromomethane + S-adenosyl-L-homocysteine.
23S rRNA (uridine(2552)-2'-O)-methyltransferase
Um(2552) 23S ribosomal RNA methyltransferase
The enzyme catalyzes the 2'-O-methylation of the universally conserved U2552 in the A loop of 23S rRNA.
S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase
Spb1p is a site-specific 2'-O-ribose RNA methyltransferase that catalyzes the formation of 2'-O-methylguanosine(2922), a universally conserved position of the catalytic center of the ribosome that is essential for translation.
2'-O-methylguanosine(2922) is formed at a later stage of the processing, during the maturation of of the 27S pre-rRNA.
In absence of snR52, Spb1p can also catalyze the formation of uridine(2921).
guanosine(2922) in 27S pre-rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2922) in 27S pre-rRNA + H(+) + S-adenosyl-L-homocysteine.
21S rRNA (uridine(2791)-2'-O)-methyltransferase
The enzyme catalyzes the methylation of uridine(2791) of mitochondrial 21S rRNA.
S-adenosyl-L-methionine + uridine(2791) in 21S rRNA = 2'-O-methyluridine(2791) in 21S rRNA + H(+) + S-adenosyl-L-homocysteine.
tricetin 3',4',5'-O-trimethyltransferase
The enzyme from Triticum aestivum catalyzes the sequential O-methylation of tricetin via 3'-O-methyltricetin, 3',5'-O-methyltricetin to 3',4',5'-O-trimethyltricetin.
3 S-adenosyl-L-methionine + tricetin = 3',4',5'-O-trimethyltricetin + 3 H(+) + 3 S-adenosyl-L-homocysteine.
16S rRNA (guanine(527)-N(7))-methyltransferase
The enzyme specifically methylates guanine(527) at N(7) in 16S rRNA.
guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine.
16S rRNA (guanine(966)-N(2))-methyltransferase
The enzyme efficiently methylates guanine(966) of the assembled 30S subunits in vitro.
Protein-free 16S rRNA is not a substrate for RsmD.
The enzyme specifically methylates guanine(966) at N(2) in 16S rRNA.
guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine.
16S rRNA (guanine(1207)-N(2))-methyltransferase
The enzyme reacts well with 30S subunits reconstituted from 16S RNA transcripts and 30S proteins but is almost inactive with the corresponding free RNA.
The enzyme specifically methylates guanine(1207) at N(2) in 16S rRNA.
guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine.
23S rRNA (guanine(2445)-N(2))-methyltransferase
The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate.
The enzyme specifically methylates guanine(2445) at N(2) in 23S rRNA.
guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine.
23S rRNA (guanine(1835)-N(2))-methyltransferase
ribosomal RNA large subunit methyltransferase G
The enzyme specifically methylates guanine(1835) at N(2) in 23S rRNA.
guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine.
The enzymes from Oryza sativa (ROMT-15 and ROMT-17) catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers.
In contrast with the wheat enzyme (EC 2.1.1.167, tricetin 3',4',5'-O-trimethyltransferase), tricetin dimethyl ether is not converted to its 3',4',5'-trimethylated ether derivative.
The enzymes from Hordeum vulgare (HvOMT1) and from Zea mays (ZmOMT1) form the 3',5'-dimethyl derivative as the major product.
2 S-adenosyl-L-methionine + tricetin = 3',5'-di-O-methyltricetin + 2 H(+) + 2 S-adenosyl-L-homocysteine.
16S rRNA (cytosine(967)-C(5))-methyltransferase
The enzyme specifically methylates cytosine(967) at C(5) in 16S rRNA.
cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (pseudouridine(1915)-N(3))-methyltransferase
YbeA does not methylate uridine at position 1915.
pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine.
16S rRNA (cytosine(1407)-C(5))-methyltransferase
The enzyme specifically methylates cytosine(1407) at C(5) in 16S rRNA.
cytidine(1407) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(1407) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine.
16S rRNA (guanine(1405)-N(7))-methyltransferase
The enzyme from the antibiotic-producing bacterium Micromonospora zionensis specifically methylates guanine(1405) at N(7) in 16S rRNA, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins.
guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(1405) in 16S rRNA + S-adenosyl-L-homocysteine.
16S rRNA (adenine(1408)-N(1))-methyltransferase
The enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N(1)-methylation at position adenine(1408).
adenosine(1408) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(1408) in 16S rRNA + S-adenosyl-L-homocysteine.
23S rRNA (adenine(1618)-N(6))-methyltransferase
The recombinant YbiN protein is able to methylate partially deproteinized 50 S ribosomal subunit, but neither the completely assembled 50 S subunits nor completely deproteinized 23 S rRNA.
adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine.
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase
KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine(1518) and adenine(1519) in 16S rRNA.
Strains lacking the methylase are resistant to kasugamycin.
adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine.
18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase
DIM1 is involved in pre-rRNA processing.
adenosine(1779)/adenosine(1780) in 18S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1779)/N(6)-dimethyladenosine(1780) in 18S rRNA + 4 S-adenosyl-L-homocysteine.
23S rRNA (adenine(2085)-N(6))-dimethyltransferase
ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at adenine(2085).
adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(6)-dimethyladenosine(2085) in 23S rRNA + 2 S-adenosyl-L-homocysteine.
23S rRNA (guanosine(2251)-2'-O)-methyltransferase
The enzyme catalyzes the methylation of guanosine(2251), a modification conserved in the peptidyltransferase domain of 23S rRNA.
guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (cytidine(2498)-2'-O)-methyltransferase
cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (guanine(745)-N(1))-methyltransferase
The enzyme specifically methylates guanine(745) at N(1) in 23S rRNA.
guanosine(745) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(745) in 23S rRNA + S-adenosyl-L-homocysteine.
23S rRNA (guanine(748)-N(1))-methyltransferase
tylosin-resistance methyltransferase RlmA(II)
The enzyme specifically methylates guanine(748) at N(1) in 23S rRNA.
The methyltransferase RlmA(II) confers resistance to the macrolide antibiotic tylosin in the drug-producing strain Streptomyces fradiae.
guanosine(748) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(748) in 23S rRNA + S-adenosyl-L-homocysteine.
23S rRNA (uracil(747)-C(5))-methyltransferase
The enzyme specifically methylates uracil(747) at C(5) in 23S rRNA.
S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (uracil(1939)-C(5))-methyltransferase
The enzyme specifically methylates uracil(1939) at C(5) in 23S rRNA.
The enzyme contains an [4Fe-4S] cluster coordinated by four conserved cysteine residues.
S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (cytosine(1962)-C(5))-methyltransferase
The enzyme specifically methylates cytosine(1962) at C(5) in 23S rRNA.
cytidine(1962) in 23S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(1962) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (adenine(2503)-C(2))-methyltransferase
S-adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group.
RlmN first transfers an CH2 group to a conserved cysteine (Cys(355) in Escherichia coli), the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen.
The formed radical forms a covalent intermediate with the adenine group of the tRNA.
RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis.
The enzyme methylates adenosine by a radical mechanism with CH2 from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine(2503) of 23S rRNA.
It will also methylate 8-methyladenosine(2503) of 23S rRNA (cf. EC 2.1.1.224).
adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine.
adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine.
16S rRNA (uracil(1498)-N(3))-methyltransferase
The enzyme specifically methylates uracil(1498) at N(3) in 16S rRNA.
S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine.
cobalt-precorrin-5B (C(1))-methyltransferase
This enzyme catalyzes the C-1 methylation of cobalt-precorrin-5B in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis.
See EC 2.1.1.152 for the C-1 methyltransferase that participates in the aerobic cobalamin biosynthesis pathway.
Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine.
cobalt-precorrin-6B (C(15))-methyltransferase [decarboxylating]
cobalt-precorrin-6Y (C(15))-methyltransferase [decarboxylating]
This enzyme, which participates in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway, catalyzes both methylation at C-15 and decarboxylation of the C-12 acetate side chain of cobalt-precorrin-6B.
The equivalent activity in the aerobic adenosylcobalamin biosynthesis pathway is catalyzed by the bifunctional enzyme EC 2.1.1.132.
Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine.
malonyl-[acyl-carrier protein] O-methyltransferase
Involved in an early step of biotin biosynthesis in Gram-negative bacteria.
This enzyme catalyzes the transfer of a methyl group to the omega-carboxyl group of malonyl-[acyl-carrier protein] forming a methyl ester.
The methyl ester is recognized by the fatty acid synthetic enzymes, which process it via the fatty acid elongation cycle to give pimelyl-[acyl-carrier-protein] methyl ester.
While the enzyme can also accept malonyl-CoA, it has a much higher activity with malonyl-[acyl-carrier protein].
malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine.
16S rRNA (cytidine(1402)-2'-O)-methyltransferase
RsmI catalyzes the 2'-O-methylation of cytidine(1402) and RsmH (EC 2.1.1.199) catalyzes the N(4)-methylation of cytidine(1402) in 16S rRNA.
Both methylations are necessary for efficient translation initiation at the UUG and GUG codons.
cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine.
16S rRNA (cytosine(1402)-N(4))-methyltransferase
RsmH catalyzes the N(4)-methylation of cytosine(1402) and RsmI (EC 2.1.1.198) catalyzes the 2'-O-methylation of cytosine(1402) in 16S rRNA.
cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine.
tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase
In Escherichia coli TrmJ is the only methyltransferase responsible for the formation of 2'-O-methylcytidine(32) in tRNA.
No methylation of cytosine(34) in tRNA(Leu)(CAA).
In vitro the enzyme 2'-O-methylates cytidine(34) of tRNA(Ser1) and uridine(32) of tRNA(Gln2).
cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine.
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase
For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant.
The bifunctional enzyme from E.coli also catalyzes the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163).
a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine.
2-methoxy-6-all-trans-hexaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-hexaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine.
2-methoxy-6-all-trans-heptaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-heptaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine.
2-methoxy-6-all-trans-octaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine.
2-methoxy-6-all-trans-nonaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-nonaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine.
2-methoxy-6-all-trans-decaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine = 6-methoxy-3-methyl-2-all-trans-decaprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine.
multisite-specific tRNA:(cytosine-C(5))-methyltransferase
The enzyme from Saccharomyces cerevisiae is responsible for complete 5-methylcytosine methylations of yeast tRNA.
The incidence of modification depends on the cytosine position in tRNA.
At positions 34 and 40, 5-methylcytosine is found only in two yeast tRNAs (tRNA(Leu)(CUA) and tRNA(Phe)(GAA), respectively), whereas most other elongator yeast tRNAs bear either 5-methylcytosine(48) or 5-methylcytosine(49), but never both in the same tRNA molecule.
The formation of 5-methylcytosine(34) and 5-methylcytosine(40) is a strictly intron-dependent process, whereas the formation of 5-methylcytosine(48) and 5-methylcytosine(49) is an intron-independent process.
cytidine(34) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(34) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine.
cytidine(40) in tRNA precursor + S-adenosyl-L-methionine = 5-methylcytidine(40) in tRNA precursor + H(+) + S-adenosyl-L-homocysteine.
cytidine(48) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(48) in tRNA + H(+) + S-adenosyl-L-homocysteine.
cytidine(49) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(49) in tRNA + H(+) + S-adenosyl-L-homocysteine.
tRNA (cytosine(34)-C(5))-methyltransferase
The human enzyme is specific for C(5)-methylation of cytosine(34) in tRNA precursors.
The intron in the human pre-tRNA(Leu)(CAA) is indispensable for the C(5)-methylation of cytosine in the first position of the anticodon.
It is not able to form 5-methylcytosine at positions 48 and 49 of human and yeast tRNA precursors.
tRNA (cytosine(38)-C(5))-methyltransferase
The eukaryotic enzyme catalyzes methylation of cytosine(38) in the anti-codon loop of tRNA(Asp)(GTC), tRNA(Val)(AAC) and tRNA(Gly)(GCC).
Methylation by Dnmt2 protects tRNAs against stress-induced cleavage by ribonuclease.
cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine.
tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase
The enzyme from Saccharomyces cerevisiae catalyzes the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNA(Phe), tRNA(Trp) and, possibly, tRNA(Leu).
cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) + 2 S-adenosyl-L-homocysteine.
tRNA (cytidine(56)-2'-O)-methyltransferase
The archaeal enzyme specifically catalyzes the S-adenosyl-L-methionine dependent 2'-O-ribose methylation of cytidine at position 56 in tRNA transcripts.
cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine.
tRNA (cytidine(34)-2'-O)-methyltransferase
tRNA (cytidine(34)/5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase
The enzyme from Escherichia coli catalyzes the 2'-O-methylation of cytidine or 5-carboxymethylaminomethyluridine at the wobble position at nucleotide 34 in tRNA(Leu)CmAA and tRNA(Leu)cmnm(5)UmAA.
The enzyme is selective for the two tRNA(Leu) isoacceptors and only methylates these when they present the correct anticodon loop sequence and modification pattern.
Specifically, YibK requires a pyrimidine nucleoside at position 34, it has a clear preference for an adenosine at position 35, and it fails to methylate without prior addition of the N(6)-(isopentenyl)-2-methylthioadenosine modification at position 37.
cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine.
5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (uridine(2479)-2'-O)-methyltransferase
Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis.
To protect itself from the antibiotic, Streptomyces viridochromogenes utilizes two methyltransferases, 23S rRNA (uridine(2479)-2'-O)-methyltransferase and EC 2.1.1.209 whose actions confer avilamycin resistance to the RNA.
S-adenosyl-L-methionine + uridine(2479) in 23S rRNA = 2'-O-methyluridine(2479) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (guanine(2535)-N(1))-methyltransferase
To protect itself from the antibiotic, Streptomyces viridochromogenes utilizes two methyltransferases, 23S rRNA (guanine(2535)-N(1))-methyltransferase and EC 2.1.1.208 whose actions confer avilamycin resistance to the RNA.
guanosine(2535) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(2535) in 23S rRNA + S-adenosyl-L-homocysteine.
In Rhodopseudomonas capsulata and Rubrivivax gelatinosus the enzyme is involved in biosynthesis of spheroidene.
In Rubrivivax gelatinosus the enzyme also catalyzes the methylation of demethylspirilloxanthin to spirilloxanthin and the methylation of 3,4-didehydrorhodopin to anhydrorhodovibrin.
demethylspheroidene + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + spheroidene.
tRNA(Ser) (uridine(44)-2'-O)-methyltransferase
The 2'-O-methylation of uridine(44) contributes to stability of tRNA(Ser)(CGA).
S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine.
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
Specifically methylates 2,4',7-trihydroxyisoflavanone on the 4'-position.
The enzyme is involved in formononetin biosynthesis in legumes.
The protein from pea (Pisum sativum) also methylates (+)-6a-hydroxymaackiain at the 3-position (cf. EC 2.1.1.270).
(2R,3S)-2,4',7-trihydroxyisoflavanone + S-adenosyl-L-methionine = (2R,3S)-2,7-dihydroxy-4'-methoxyisoflavanone + H(+) + S-adenosyl-L-homocysteine.
tRNA (guanine(10)-N(2))-dimethyltransferase
N(2),N(2)-dimethylguanosine tRNA methyltransferase
guanosine(10) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(10) in tRNA + 2 S-adenosyl-L-homocysteine.
tRNA (guanine(10)-N(2))-methyltransferase
In contrast to the archaeal enzyme EC 2.1.1.213, tRNA (guanine(10)-N(2))-methyltransferase from yeast does not catalyze the methylation from N(2)-methylguanine(10) to N(2)-dimethylguanine(10) in tRNA.
guanosine(10) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(10) in tRNA + S-adenosyl-L-homocysteine.
tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferase
The enzyme from Aquifex aeolicus is similar to the TRM1 methyltransferases of archaea and eukarya (see EC 2.1.1.216).
However, it catalyzes the double methylation of guanines at both positions 26 and 27 of tRNA.
guanosine(26)/guanosine(27) in tRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(2)-dimethylguanosine(26)/N(2)-dimethylguanosine(27) in tRNA + 4 S-adenosyl-L-homocysteine.
tRNA (guanine(26)-N(2))-dimethyltransferase
The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions.
In contrast to EC 2.1.1.215, this enzyme does not catalyze the methylation of guanine(27) in tRNA.
guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine.
tRNA (adenine(22)-N(1))-methyltransferase
The enzyme specifically methylates adenine(22) in tRNA.
adenosine(22) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(22) in tRNA + S-adenosyl-L-homocysteine.
tRNA (adenine(9)-N(1))-methyltransferase
The enzyme from Sulfolobus acidocaldarius specifically methylates adenine(9) in tRNA.
The bifunctional enzyme from Thermococcus kodakaraensis also catalyzes the methylation of guanine(9) in tRNA (cf. EC 2.1.1.221).
adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine.
tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase
The enzyme catalyzes the formation of N(1)-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs (e.g. tRNA(Asp)).
Methyladenosine at position 57 is an obligatory intermediate for the synthesis of methylinosine, which is commonly found at position 57 of archaeal tRNAs.
adenosine(57)/adenosine(58) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(1)-methyladenosine(57)/N(1)-methyladenosine(58) in tRNA + 2 S-adenosyl-L-homocysteine.
tRNA (adenine(58)-N(1))-methyltransferase
The enzyme specifically methylates adenine(58) in tRNA.
The methylation of A(58) is critical for maintaining the stability of initiator tRNA(Met) in yeast.
adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine.
tRNA (guanine(9)-N(1))-methyltransferase
The enzyme from Saccharomyces cerevisiae specifically methylates guanine(9).
The bifunctional enzyme from Thermococcus kodakaraensis also catalyzes the methylation of adenine(9) in tRNA (cf. EC 2.1.1.218).
guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine.
UbiG catalyzes both methylation steps in ubiquinone biosynthesis in Escherichia coli.
The second methylation is classified as EC 2.1.1.64.
In eukaryotes Coq3 catalyzes the two methylation steps in ubiquinone biosynthesis.
However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114.
The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.
a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosyl-L-homocysteine.
3-(all-trans-octaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-octaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine.
3-(all-trans-heptaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-heptaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine.
3-(all-trans-nonaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-nonaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine.
3-(all-trans-decaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-decaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine.
3-(all-trans-hexaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = 2-methoxy-6-(all-trans-hexaprenyl)phenol + H(+) + S-adenosyl-L-homocysteine.
tRNA1(Val) (adenine(37)-N(6))-methyltransferase
The enzyme specifically methylates adenine(37) in tRNA1(Val) (anticodon cmo(5)UAC).
adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine.
23S rRNA (adenine(2503)-C(8))-methyltransferase
Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics.
The enzyme methylates adenosine at position 2503 of 23S rRNA by a radical mechanism, transferring a CH2 group from S-adenosyl-L-methionine while retaining the hydrogen at the C-8 position of the adenine.
Cfr first transfers an CH2 group to a conserved cysteine (Cys(338) in Staphylococcus aureus), the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen.
The enzyme will also methylate 2-methyladenine produced by the action of EC 2.1.1.192.
adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + 8-methyladenosine(2503) in 23S rRNA + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine.
The enzyme from Saccharomyces cerevisiae 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
cytidine(4) in tRNA(Pro) + S-adenosyl-L-methionine = 2'-O-methylcytidine(4) in tRNA(Pro) + H(+) + S-adenosyl-L-homocysteine.
cytidine(4) in tRNA(Gly)(GCC) + S-adenosyl-L-methionine = 2'-O-methylcytidine(4) in tRNA(Gly)(GCC) + H(+) + S-adenosyl-L-homocysteine.
adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine.
23S rRNA (cytidine(1920)-2'-O)-methyltransferase
The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine(1920) in helix 69 of 23S rRNA and cytidine(1409) in helix 44 of 16S rRNA (cf. EC 2.1.1.227).
These methylations result in increased susceptibility to the antibiotics capreomycin and viomycin.
cytidine(1920) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1920) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
16S rRNA (cytidine(1409)-2'-O)-methyltransferase
The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine(1409) in helix 44 of 16S rRNA and cytidine(1920) in helix 69 of 23S rRNA (cf. EC 2.1.1.226).
cytidine(1409) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1409) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine.
tRNA (guanine(37)-N(1))-methyltransferase
transfer RNA (m(1)G(37)) methyltransferase
This enzyme is important for the maintenance of the correct reading frame during translation.
Unlike TrmD from Escherichia coli, which recognizes the G(36)pG(37) motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37.
guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine.
tRNA (carboxymethyluridine(34)-5-O)-methyltransferase
The enzyme catalyzes the post-translational modification of uridine residues at the wobble position 34 of the anticodon loop of tRNA.
carboxymethyluridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine.
23S rRNA (adenosine(1067)-2'-O)-methyltransferase
nosiheptide-resistance methyltransferase
The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton.
adenosine(1067) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methyladenosine(1067) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine.
The enzyme catalyzes the 4'-methylation of naringenin.
In vitro it catalyzes the 4'-methylation of apigenin, quercetin, daidzein and genistein.
a 4'-hydroxyflavanone + S-adenosyl-L-methionine = a 4'-methoxyflavanone + H(+) + S-adenosyl-L-homocysteine.
The enzyme is involved in the biosynthesis of the sakuranetin, an inducible defense mechanism of Oryza sativa against pathogen attack.
(2S)-naringenin + S-adenosyl-L-methionine = (2S)-sakuranetin + H(+) + S-adenosyl-L-homocysteine.
[phosphatase 2A protein]-leucine-carboxy methyltransferase
Methylates the C-terminal leucine of phosphatase 2A.
A key regulator of protein phosphatase 2A.
The methyl ester is hydrolyzed by EC 3.1.1.89.
Occurs mainly in the cytoplasm, Golgi region and late endosomes.
[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine.
dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
The enzyme is involved in the biosynthesis of desosamine, a 3-(dimethylamino)-3,4,6-trideoxyhexose found in certain macrolide antibiotics such as erthyromycin, azithromycin, and clarithromycin.
dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-desosamine + 2 H(+) + 2 S-adenosyl-L-homocysteine.
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase
The enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin, which is produced by the bacterium Streptomyces fradiae.
dTDP-3-amino-3,6-dideoxy-alpha-D-glucose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-mycaminose + 2 H(+) + 2 S-adenosyl-L-homocysteine.
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose N,N-dimethyltransferase
The enzyme is involved in the synthesis of dTDP-D-ravidosamine, the amino sugar moiety of the antibiotic ravidomycin V, which is produced by the bacterium Streptomyces ravidus.
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose + 2 S-adenosyl-L-methionine = dTDP-D-ravidosamine + 2 H(+) + 2 S-adenosyl-L-homocysteine.
The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics.
mycinamicin III + S-adenosyl-L-methionine = H(+) + mycinamicin IV + S-adenosyl-L-homocysteine.
mycinamicin VI + S-adenosyl-L-methionine = H(+) + mycinamicin III + S-adenosyl-L-homocysteine.
L-olivosyl-oleandolide 3-O-methyltransferase
The enzyme is involved in the biosynthesis of the macrolide antibiotic oleandomycin in Streptomyces antibioticus.
It can also act on other monoglycosylated macrolactones, including L-rhamnosyl-erythronolide B and L-mycarosyl-erythronolide B.
L-olivosyl-oleandolide + S-adenosyl-L-methionine = H(+) + L-oleandrosyl-oleandolide + S-adenosyl-L-homocysteine.
trans-resveratrol di-O-methyltransferase
The enzyme catalyzes the biosynthesis of pterostilbene from resveratrol.
2 S-adenosyl-L-methionine + trans-resveratrol = 2 H(+) + pterostilbene + 2 S-adenosyl-L-homocysteine.
2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase
The enzyme is involved in the biosynthesis of the protective and allelophatic benzoxazinoid DIMBOA ((2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin) in some plants, most commonly from the family of Poacea (grasses).
S-adenosyl-L-methionine + TRIBOA beta-D-glucoside = DIMBOA beta-D-glucoside + H(+) + S-adenosyl-L-homocysteine.
16S rRNA (guanine(1516)-N(2))-methyltransferase
The enzyme specifically methylates guanine(1516) at N(2) in 16S rRNA.
guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine.
The enzyme is involved in production of the rare amino acid 3-methylarginine, which is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas syringae pv. glycinea.
5-guanidino-2-oxopentanoate + S-adenosyl-L-methionine = 5-guanidino-3-methyl-2-oxopentanoate + H(+) + S-adenosyl-L-homocysteine.
This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved.
When the terminal amino acid is L-proline, the enzyme catalyzes two successive methylations of its alpha-amino group.
When the first amino acid is either L-alanine or L-serine, the enzyme catalyzes three successive methylations.
The Pro-Lys in positions 2-3 cannot be exchanged for other amino acids.
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine.
N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine.
N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-homocysteine.
5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
Catalyzes the transfer of a methyl group from the cobamide cofactor of a corrinoid/Fe-S protein to the N5 group of tetrahydrosarcinapterin.
Forms, together with EC 1.2.7.4 and EC 2.3.1.169 the acetyl-CoA decarbonylase/synthase complex that catalyzes the demethylation of acetyl-CoA in a reaction that also forms CO2.
This reaction is a key step in methanogenesis from acetate.
5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid Fe-S protein] + H(+).
[methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from methanol, catalyzes the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.90), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, the enzyme that catalyzes the final step in methanogenesis.
Free methylcob(I)alamin can substitute for the corrinoid protein in vitro.
coenzyme M + methyl-Co(III)-[methanol-specific corrinoid protein] = Co(I)-[methanol-specific corrinoid protein] + H(+) + methyl-coenzyme M.
[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyzes the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, EC 2.1.1.249 and EC 2.1.1.250) to coenzyme M, forming the substrate for EC 2.8.4.1, the enzyme that catalyzes the final step in methanogenesis.
coenzyme M + methyl-Co(III)-[methylamine-specific corrinoid protein] = Co(I)-[methylamine-specific corrinoid protein] + H(+) + methyl-coenzyme M.
coenzyme M + methyl-Co(III)-[dimethylamine-specific corrinoid protein] = Co(I)-[dimethylamine-specific corrinoid protein] + H(+) + methyl-coenzyme M.
coenzyme M + methyl-Co(III)-[trimethylamine-specific corrinoid protein] = Co(I)-[trimethylamine-specific corrinoid protein] + H(+) + methyl-coenzyme M.
[methylamine--corrinoid protein] Co-methyltransferase
The enzyme, which catalyzes the transfer of a methyl group from methylamine to a methylamine-specific corrinoid protein (MtmC), is involved in methanogenesis from methylamine.
The enzyme contains the unusual amino acid pyrrolysine.
The methylated corrinoid protein is substrate for EC 2.1.1.247.
Co(I)-[methylamine-specific corrinoid protein] + H(+) + methylamine = methyl-Co(III)-[methylamine-specific corrinoid protein] + NH4(+).
[dimethylamine--corrinoid protein] Co-methyltransferase
The enzyme, which catalyzes the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine.
Co(I)-[dimethylamine-specific corrinoid protein] + dimethylamine + H(+) = methyl-Co(III)-[dimethylamine-specific corrinoid protein] + methylamine.
[trimethylamine--corrinoid protein] Co-methyltransferase
The enzyme, which catalyzes the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine.
Co(I)-[trimethylamine-specific corrinoid protein] + H(+) + trimethylamine = dimethylamine + methyl-Co(III)-[trimethylamine-specific corrinoid protein].
methylated-thiol--coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-(methylsulfanyl)propanoate, catalyzes two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to coenzyme M.
With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90 and EC 2.1.1.246).
The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation.
coenzyme M + methanethiol = H(+) + hydrogen sulfide + methyl-coenzyme M.
tetramethylammonium--corrinoid protein Co-methyltransferase
The enzyme, which catalyzes the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium.
The methylated corrinoid protein is substrate for EC 2.1.1.253.
Co(I)-[tetramethylammonium-specific corrinoid protein] + H(+) + tetramethylammonium = methyl-Co(III)-[tetramethylammonium-specific corrinoid protein] + trimethylamine.
[methyl-Co(III) tetramethylammonium-specific corrinoid protein]:coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyzes the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, the enzyme that catalyzes the final step in methanogenesis.
coenzyme M + methyl-Co(III)-[tetramethylammonium-specific corrinoid protein] = Co(I)-[tetramethylammonium-specific corrinoid protein] + H(+) + methyl-coenzyme M.
The enzyme methylates the 3 position of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A.
It can also methylate the precursor erythromycin D, forming erythromycin B, which is then converted to erythromycin A by EC 1.14.13.154.
erythromycin C + S-adenosyl-L-methionine = erythromycin A + H(+) + S-adenosyl-L-homocysteine.
erythromycin D + S-adenosyl-L-methionine = erythromycin B + H(+) + S-adenosyl-L-homocysteine.
geranyl diphosphate 2-C-methyltransferase
This enzyme, along with EC 4.2.3.118, produces 2-methylisoborneol, an odiferous compound produced by soil microorganisms with a strong earthy/musty odor.
(2E)-geranyl diphosphate + S-adenosyl-L-methionine = (E)-2-methylgeranyl diphosphate + H(+) + S-adenosyl-L-homocysteine.
tRNA (guanine(6)-N(2))-methyltransferase
The enzyme specifically methylates guanine(6) at N(2) in tRNA.
guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine.
tRNA (pseudouridine(54)-N(1))-methyltransferase
While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54.
pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine.
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
Catalyzes the transfer of a methyl group from the N(5) group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein.
Involved, together with EC 1.2.7.4 and EC 2.3.1.169, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
(6S)-5,6,7,8-tetrahydrofolate + methyl-Co(III)-[corrinoid Fe-S protein] = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + Co(I)-[corrinoid Fe-S protein] + H(+).
[fructose-bisphosphate aldolase]-lysine N-methyltransferase
S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase
The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13).
The enzyme from pea (Pisum sativum) also methylates Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39), but that from Arabidopsis thaliana does not.
[fructose-bisphosphate aldolase]-L-lysine + 3 S-adenosyl-L-methionine = [fructose-bisphosphate aldolase]-N(6),N(6),N(6)-trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-homocysteine.
rRNA small subunit pseudouridine methyltransferase Nep1
This enzyme, which occurs in both prokaryotes and eukaryotes, recognizes specific pseudouridine residues (Psi) in small subunits of ribosomal RNA based on the local RNA structure.
It recognizes Psi(914) in 16S rRNA from the archaeon Methanocaldococcus jannaschii, Psi(1191) in yeast 18S rRNA, and Psi(1248) in human 18S rRNA.
pseudouridine(1191) in yeast 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(1191) in yeast 18S rRNA + S-adenosyl-L-homocysteine.
a pseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = an N(1)-methylpseudouridine in 16S/18S rRNA + H(+) + S-adenosyl-L-homocysteine.
pseudouridine(914) in M. jannaschii 16S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(914) in M. jannaschii 16S rRNA + S-adenosyl-L-homocysteine.
pseudouridine(1248) in human 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl-L-homocysteine.
4-dimethylallyltryptophan N-methyltransferase
The enzyme catalyzes a step in the pathway leading to biosynthesis of ergot alkaloids in certain fungi.
4-(3-methylbut-2-enyl)-L-tryptophan + S-adenosyl-L-methionine = 4-(3-methylbut-2-enyl)-L-abrine + H(+) + S-adenosyl-L-homocysteine.
Two isoforms differing in their specificity were isolated from the green alga Botryococcus braunii BOT22.
TMT-1 gave more of the dimethylated form whereas TMT2 gave more of the monomethylated form.
2 S-adenosyl-L-methionine + squalene = 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene + 2 H(+) + 2 S-adenosyl-L-homocysteine.
Shows a very weak activity with squalene.
C30 botryococcene + 2 S-adenosyl-L-methionine = 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene + 2 H(+) + 2 S-adenosyl-L-homocysteine.
23S rRNA (guanine(2069)-N(7))-methyltransferase
The enzyme specifically methylates guanine(2069) at position N7 in 23S rRNA.
In gamma-proteobacteria the enzyme also catalyzes EC 2.1.1.173, while in beta-proteobacteria the activities are carried out by separate proteins.
The enzyme from the gamma-proteobacterium Escherichia coli has RNA unwinding activity as well.
guanosine(2069) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2069) in 23S rRNA + S-adenosyl-L-homocysteine.
The enzyme is involved in the detoxification of tellurite.
It can also methylate selenite and selenium dioxide.
S-adenosyl-L-methionine + tellurite = methanetellurite + S-adenosyl-L-homocysteine.
23S rRNA (adenine(2030)-N(6))-methyltransferase
The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits.
adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine.
Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside.
The enzyme from Catharanthus roseus was most active with myricetin.
S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid.
S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3',5'-dimethoxyflavonoid.
myricetin + S-adenosyl-L-methionine = H(+) + laricitrin + S-adenosyl-L-homocysteine.
laricitrin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + syringetin.
a 5'-hydroxy-3'-methoxyflavone + S-adenosyl-L-methionine = a 3',5'-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine.
tRNA(Thr) (cytosine(32)-N(3))-methyltransferase
The enzyme from Saccharomyces cerevisiae specifically methylates cytosine(32) in tRNA(Thr) and in tRNA(Ser).
cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine.
cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine.
dimethylsulfoniopropionate-dependent demethylase A
The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific toward S,S-dimethyl-beta-propiothetin.
They do not demethylate glycine-betaine.
(6S)-5,6,7,8-tetrahydrofolate + S,S-dimethyl-beta-propiothetin = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3-(methylsulfanyl)propanoate + H(+).
(+)-6a-hydroxymaackiain 3-O-methyltransferase
The protein from the plant Pisum sativum (garden pea) methylates (+)-6a-hydroxymaackiain at the 3-position.
It also methylates 2,7,4'-trihydroxyisoflavanone on the 4'-position (cf. EC 2.1.1.212).
(+)-6a-hydroxymaackiain + S-adenosyl-L-methionine = (+)-pisatin + H(+) + S-adenosyl-L-homocysteine.
This enzyme, which participates in the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway, catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A.
See EC 2.1.1.133 for the equivalent enzyme that participates in the aerobic cobalamin biosynthesis pathway.
Co-precorrin-4 + S-adenosyl-L-methionine = Co-precorrin-5A + H(+) + S-adenosyl-L-homocysteine.
Isolated from the bacterium Bacillus megaterium.
The enzyme, which participates in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, catalyzes a crucial reaction where the tetrapyrrole ring contracts as a result of methylation of C-17.
It can also convert cobalt-precorrin-3 to cobalt-precorrin-4.
See EC 2.1.1.131 for the corresponding enzyme that participates in the aerobic cobalamin biosynthesis pathway.
AH2 + Co(II)-factor III + S-adenosyl-L-methionine = A + Co-precorrin-4 + S-adenosyl-L-homocysteine.
While the enzyme from the plant Zea mays is specific for benzoate, the enzymes from Arabidopsis species and Clarkia breweri also catalyze the reaction of EC 2.1.1.274.
In snapdragon (Antirrhinum majus) two isoforms are found, one specific for benzoate and one that is also active toward salicylate.
The volatile product is an important scent compound in some flowering species.
benzoate + S-adenosyl-L-methionine = methyl benzoate + S-adenosyl-L-homocysteine.
The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.273.
S-adenosyl-L-methionine + salicylate = methyl salicylate + S-adenosyl-L-homocysteine.
The enzyme also methylates gibberellins A20 (95%), A3 (80%), A4 (69%) and A34 (46%) with significant activity.
gibberellin A9 + S-adenosyl-L-methionine = O-methyl gibberellin A9 + S-adenosyl-L-homocysteine.
gibberellin A20 + S-adenosyl-L-methionine = gibberellin A20 methyl ester + S-adenosyl-L-homocysteine.
gibberellin A3 + S-adenosyl-L-methionine = O-methyl gibberellin A3 + S-adenosyl-L-homocysteine.
gibberellin A4 + S-adenosyl-L-methionine = O-methyl gibberellin A4 + S-adenosyl-L-homocysteine.
gibberellin A34 + S-adenosyl-L-methionine = O-methyl gibberellin A34 + S-adenosyl-L-homocysteine.
gibberellin A4 carboxyl methyltransferase
The enzyme also methylates gibberellins A34 (80%), A9 (60%), and A3 (45%) with significant activity.
In the plant maize (Zea mays), the isoforms AAMT1 and AAMT2 are specific for anthranilate while AAMT3 also has the activity of EC 2.1.1.273.
anthranilate + S-adenosyl-L-methionine = O-methyl anthranilate + S-adenosyl-L-homocysteine.
The enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate.
The product, methyl (indol-3-yl)acetate is inactive as hormone.
(indol-3-yl)acetate + S-adenosyl-L-methionine = methyl (indol-3-yl)acetate + S-adenosyl-L-homocysteine.
The enzyme from anise (Pimpinella anisum) is highly specific for substrates in which the double bond in the propenyl side chain is located between C7 and C8, and, in contrast to EC 2.1.1.146, does not have activity with eugenol or chavicol.
S-adenosyl-L-methionine + trans-anol = H(+) + S-adenosyl-L-homocysteine + trans-anethole.
The enzyme from broccoli (Brassica oleracea var. italica) also has the activity of EC 2.1.1.10.
L-selenocysteine + S-methyl-L-methionine = H(+) + L-methionine + Se-methyl-L-selenocysteine.
The enzyme from the bacterium Streptomyces hygroscopicus NRRL3085 is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin.
3-phenylpyruvate + S-adenosyl-L-methionine = (3S)-2-oxo-3-phenylbutanoate + H(+) + S-adenosyl-L-homocysteine.
tRNA(Phe) 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4)]-methyltransferase
The enzyme is involved in the biosynthesis of hypermodified tricyclic bases found at position 37 of certain tRNAs.
These modifications are important for translational reading-frame maintenance.
The enzyme is found in all eukaryotes and in some archaea, but not in bacteria.
The eukaryotic enzyme is involved in the biosynthesis of wybutosine.
4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-homocysteine.
The enzyme is involved in biosynthesis of the seco-anthraquinone (+)-geodin.
emodin + S-adenosyl-L-methionine = H(+) + questin + S-adenosyl-L-homocysteine.
8-demethylnovobiocic acid C(8)-methyltransferase
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin.
8-desmethylnovobiocic acid + S-adenosyl-L-methionine = H(+) + novobiocic acid + S-adenosyl-L-homocysteine.
demethyldecarbamoylnovobiocin O-methyltransferase
desmethyldescarbamoylnovobiocin + S-adenosyl-L-methionine = descarbamoylnovobiocin + H(+) + S-adenosyl-L-homocysteine.
25S rRNA (adenine(2142)-N(1))-methyltransferase
In the yeast Saccharomyces cerevisiae this methylation is important for resistance toward hydrogen peroxide and the antibiotic anisomycin.
adenosine(2142) in 25S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(2142) in 25S rRNA + S-adenosyl-L-homocysteine.
25S rRNA (adenine(645)-N(1))-methyltransferase
The adenine position refers to tRNA the yeast Saccharomyces cerevisiae, in which the enzyme is important for ribosome biogenesis.
adenosine(645) in 25S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(645) in 25S rRNA + S-adenosyl-L-homocysteine.
The enzyme from the Gram-positive bacterium Streptomyces sp. C5 is involved in the biosynthesis of the anthracycline daunorubicin.
aklanonate + S-adenosyl-L-methionine = methyl aklanonate + S-adenosyl-L-homocysteine.
cobalt-precorrin-7 (C(5))-methyltransferase
This enzyme catalyzes the methylation at C-5 of cobalt-precorrin-7, a step in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway.
Co-precorrin-7 + S-adenosyl-L-methionine = Co-precorrin-8X + H(+) + S-adenosyl-L-homocysteine.
tRNA(Phe) [7-(3-amino-3-carboxypropyl)wyosine(37)-O]-methyltransferase
The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs.
The modification is important for translational reading-frame maintenance.
In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37) in tRNA(Phe) as substrate.
The enzyme also has the activity of EC 2.3.1.231.
7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-homocysteine.
The enzyme from the plant Papaver somniferum (opium poppy) methylates (S)- and (R)-reticuline with equal efficiency and is involved in the biosynthesis of tetrahydrobenzylisoquinoline alkaloids.
(S)-reticuline + S-adenosyl-L-methionine = (S)-laudanine + H(+) + S-adenosyl-L-homocysteine.
(R)-reticuline + S-adenosyl-L-methionine = (R)-laudanine + H(+) + S-adenosyl-L-homocysteine.
The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius are involved in the biosynthesis of the anthracycline daunorubicin.
In vitro the enzyme from Streptomyces sp. C5 also catalyzes the 4-O-methylation of 13-dihydrocarminomycin, rhodomycin D and 10-carboxy-13-deoxycarminomycin.
carminomycin + S-adenosyl-L-methionine = daunorubicin + H(+) + S-adenosyl-L-homocysteine.
6-hydroxytryprostatin B O-methyltransferase
6-hydroxytryprostatin B + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + tryprostatin A.
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a.
O-polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit.
The dual kinase/methylase WbdD also catalyzes the preceding phosphorylation of alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]N-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.7.1.181).
3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + S-adenosyl-L-methionine = 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + S-adenosyl-L-homocysteine.
2-methyl-6-phytyl-1,4-hydroquinone methyltransferase
2-methyl-6-solanyl-1,4-hydroquinone methyltransferase
Involved in the biosynthesis of plastoquinol, as well as vitamin E (tocopherols and tocotrienols).
2-methyl-6-phytyl-1,4-benzene-1,4-diol + S-adenosyl-L-methionine = 2,3-dimethyl-6-phytylbenzene-1,4-diol + H(+) + S-adenosyl-L-homocysteine.
2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + S-adenosyl-L-methionine = H(+) + plastoquinol-9 + S-adenosyl-L-homocysteine.
6-geranylgeranyl-2-methylbenzene-1,4-diol + S-adenosyl-L-methionine = 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol + H(+) + S-adenosyl-L-homocysteine.
The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the nucleoside at the second transcribed position of mRNAs and snRNAs.
The human enzyme can also methylate mRNA molecules where the upstream ribonucleotide is not methylated (see EC 2.1.1.57), but with lower efficiency.
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-adenosyl-L-homocysteine.
peptide chain release factor N(5)-glutamine methyltransferase
N(5)-glutamine S-adenosyl-L-methionine dependent methyltransferase
Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity.
L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine.
ribosomal protein L3 N(5)-glutamine methyltransferase
Modifies the glutamine residue in the glycylglycylglutamine (GGQ) motif of ribosomal protein L3 (Gln(150) in the protein from the bacterium Escherichia coli).
The enzyme does not act on peptide chain release factor 1 or 2.
L-glutaminyl-[ribosomal protein uL3] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[ribosomal protein uL3] + S-adenosyl-L-homocysteine.
protein N-terminal monomethyltransferase
In contrast to EC 2.1.1.244, the protein only adds one methyl group to the N-terminal.
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N-terminal N-methyl-L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine.
N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N-terminal N-methyl-L-prolyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine.
N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N-terminal N-methyl-L-seryl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine.
The enzyme, isolated from the plant Thalictrum flavum, also methylates (R,S)-stylopine and (S)-scoulerine (11%) with lower activity (14% and 11%, respectively).
(+-)-pavine + S-adenosyl-L-methionine = H(+) + N-methylpavine + S-adenosyl-L-homocysteine.
The enzyme, isolated from Streptomyces sp. OH-4156, can methylate a variety of oligopeptides, cyclic peptides such as nisin and haloduracin, and the epsilon-amino group of lysine.
Cypemycin is a peptide antibiotic, a member of the linaridins, a class of post-translationally modified ribosomally synthesized peptides.
N-terminal L-alanyl-[cypemycin] + 2 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N-dimethyl-L-alanyl-[cypemycin] + 2 S-adenosyl-L-homocysteine.
3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase
3-hydroxy-5-methyl-1-naphthoate + S-adenosyl-L-methionine = 3-methoxy-5-methyl-1-naphthoate + H(+) + S-adenosyl-L-homocysteine.
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate.
This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin.
In vivo the enzyme catalyzes the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1-naphthoate.
In vitro it also recognizes other dihydroxynaphthoic acids and catalyzes their regiospecific O-methylation.
2,7-dihydroxy-5-methyl-1-naphthoate + S-adenosyl-L-methionine = 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + H(+) + S-adenosyl-L-homocysteine.
The enzyme from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.
L-tyrosine + S-adenosyl-L-methionine = 3-methyl-L-tyrosine + H(+) + S-adenosyl-L-homocysteine.
8-demethyl-8-alpha-L-rhamnosyl tetracenomycin-C 2'-O-methyltransferase
The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.
8-demethyl-8-alpha-L-rhamnosyl-tetracenomycin C + S-adenosyl-L-methionine = 8-demethyl-8-(2-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + H(+) + S-adenosyl-L-homocysteine.
8-demethyl-8-(2-methoxy-alpha-L-rhamnosyl)-tetracenomycin-C 3'-O-methyltransferase
8-demethyl-8-(2-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + S-adenosyl-L-methionine = 8-demethyl-8-(2,3-di-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + H(+) + S-adenosyl-L-homocysteine.
8-demethyl-8-(2,3-dimethoxy-alpha-L-rhamnosyl)-tetracenomycin-C 4'-O-methyltransferase
8-demethyl-8-(2,3-di-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + S-adenosyl-L-methionine = 8-demethyl-8-(2,3,4-tri-O-methyl-alpha-L-rhamnosyl)-tetracenomycin C + H(+) + S-adenosyl-L-homocysteine.
cytidylyl-2-hydroxyethylphosphonate methyltransferase
The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis.
It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor.
The enzyme uses two molecues of SAM for the reaction.
One molecule forms a 5'-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor.
The 5'-deoxyadenosyl radical abstracts a hydrogen from the C2 position of cytidine 5'-{[(2-hydroxyethyl)phosphonoyl]phosphate} forming a free radical that reacts with the methyl group on methylcob(III)alamin at the opposite side from SAM and the [4Fe-4S] cluster to produce a racemic mix of methylated products and cob(II)alamin.
Both the [4Fe-4S] cluster and the cob(II)alamin need to be reduced by an unknown factor(s) before the enzyme could catalyze another cycle.
AH2 + cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + A + cytidine 5'-{[hydroxy(2-hydroxypropyl)phosphonoyl]phosphate} + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine.
18S rRNA (guanine(1575)-N(7))-methyltransferase
The enzyme, found in eukaryotes, is involved in pre-rRNA processing.
The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae.
guanosine(1575) in yeast 18S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(1575) in yeast 18S rRNA + S-adenosyl-L-homocysteine.
25S rRNA (cytosine(2870)-C(5))-methyltransferase
The enzyme, found in eukaryotes, is specific for cytosine(2870) of the 25S ribosomal RNA.
cytidine(2870) in 25S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(2870) in 25S rRNA + H(+) + S-adenosyl-L-homocysteine.
25S rRNA (cytosine(2278)-C(5))-methyltransferase
The enzyme, found in eukaryotes, is specific for 25S cytosine(2278).
cytidine(2278) in 25S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(2278) in 25S rRNA + H(+) + S-adenosyl-L-homocysteine.
25S rRNA (uracil(2843)-N(3))-methyltransferase
The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.
S-adenosyl-L-methionine + uridine(2843) in 25S rRNA = H(+) + N(3)-methyluridine(2843) in 25S rRNA + S-adenosyl-L-homocysteine.
25S rRNA (uracil(2634)-N(3))-methyltransferase
S-adenosyl-L-methionine + uridine(2634) in 25S rRNA = H(+) + N(3)-methyluridine(2634) in 25S rRNA + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + uridine in 25S rRNA = H(+) + N(3)-methyluridine in 25S rRNA + S-adenosyl-L-homocysteine.
This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide.
Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98).
The relevant histidine of elongation factor 2 is His(715) in mammals and His(699) in yeast.
2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-homocysteine.
27-O-demethylrifamycin SV methyltransferase
The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the antitubercular drug rifamycin B.
27-O-demethylrifamycin SV + S-adenosyl-L-methionine = H(+) + rifamycin SV + S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Streptomyces lavendulae, is involved in the biosynthesis of the quinone-containing antibiotics mitomycin A and mitomycin B.
6-demethylmitomycin A + S-adenosyl-L-methionine = mitomycin A + S-adenosyl-L-homocysteine.
6-demethylmitomycin B + S-adenosyl-L-methionine = mitomycin B + S-adenosyl-L-homocysteine.
The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.
a (4E,8E)-4-sphinga-4,8-dienine ceramide + S-adenosyl-L-methionine = a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide + H(+) + S-adenosyl-L-homocysteine.
[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase
The enzyme, characterized from the yeast Saccharomyces cerevisiae, enhances the activity of EC 2.4.1.15 resulting in elevating the levels of trehalose in the cell and contributing to stationary phase survival.
In vitro the enzyme performs S-methylation of L-cysteine residues of various protein substrates.
[trehalose-6-phosphate synthase]-L-cysteine + S-adenosyl-L-methionine = [trehalose-6-phosphate synthase]-S-methyl-L-cysteine + H(+) + S-adenosyl-L-homocysteine.
type I protein arginine methyltransferase
This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues.
Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific.
The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues.
PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells.
L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine.
type II protein arginine methyltransferase
The enzyme catalyzes the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine.
The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins.
L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine.
type III protein arginine methyltransferase
Type III protein arginine methyltransferases catalyze the single methylation of one of the terminal nitrogen atoms of the guanidino group in an L-arginine residue within a protein.
Unlike type I and type II protein arginine methyltransferases, which also catalyze this reaction, type III enzymes do not methylate the substrate any further.
L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine.
type IV protein arginine methyltransferase
This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the Delta-nitrogen atom of arginine residues within proteins.
Among its substrates are Arg(67) of the ribosomal protein L12.
L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine.
(-)-pluviatolide + S-adenosyl-L-methionine = (-)-bursehernin + H(+) + S-adenosyl-L-homocysteine.
dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase
TDP-4-amino-2,3,6-trideoxy-D-glucose N,N-dimethyltransferase
The enzyme was isolated from the bacterium Saccharopolyspora spinosa, where it is involved in the biosynthesis of spinosyn A, an active ingredient of several commercial insecticides.
dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-erythro-hexopyranose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-forosamine + 2 H(+) + 2 S-adenosyl-L-homocysteine.
The enzyme, found in insects, is involved in the synthesis of juvenile hormone III, a sesquiterpenoid that regulates several processes including embryonic development, metamorphosis, and reproduction, in many insect species.
(2E,6E)-farnesoate + S-adenosyl-L-methionine = methyl (2E,6E)-farnesoate + S-adenosyl-L-homocysteine.
juvenile hormone III carboxylate + S-adenosyl-L-methionine = juvenile hormone III + S-adenosyl-L-homocysteine.
N-acetyl-demethylphosphinothricin P-methyltransferase
The enzyme was originally characterized from bacteria that produce the tripeptides bialaphos and phosalacine, which inhibit plant and bacterial glutamine synthetases.
It is a radical S-adenosyl-L-methionine (SAM) enzyme.
According to the proposed mechanism, the reduced iron-sulfur center donates an electron to SAM, resulting in homolytic cleavage of the carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts the hydrogen atom from the P-H bond of the substrate, forming a phosphinate-centered radical.
This radical reacts with methylcob(III)alamin to produce the methylated product and cob(II)alamin, which is reduced by an unknown donor to cob(I)alamin.
A potential route for restoring the latter back to methylcob(III)alamin is a nucleophilic attack on a second SAM molecule.
The enzyme acts in vivo on N-acetyl-demethylphosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of bialaphos and phosalacine, respectively.
This transformation produces the only example of a carbon-phosphorus-carbon linkage known to occur in nature.
AH2 + N-acetyl-demethyl-L-phosphinothricin + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + A + 2 H(+) + L-methionine + N-acetyl-L-phosphinothricin + S-adenosyl-L-homocysteine.
phenazine-1-carboxylate N-methyltransferase
The enzyme is active in vitro only in the presence of EC 1.14.13.218.
phenazine-1-carboxylate + S-adenosyl-L-methionine = 5-methyl-phenazine-1-carboxylate + S-adenosyl-L-homocysteine.
N-demethylindolmycin N-methyltransferase
The enzyme, characterized from the bacterium Streptomyces griseus, catalyzes the ultimate reaction in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial EC 6.1.1.2.
N-demethylindolmycin + S-adenosyl-L-methionine = H(+) + indolmycin + S-adenosyl-L-homocysteine.
2-phytyl-1,4-naphthoquinol methyltransferase
The enzyme, found in plants and cyanobacteria, catalyzes the final step in the biosynthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I.
The enzyme is specific for the quinol form of the substrate, and does not act on the quinone form.
demethylphylloquinol + S-adenosyl-L-methionine = H(+) + phylloquinol + S-adenosyl-L-homocysteine.
5'-demethylyatein 5'-O-methyltransferase
(-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-homocysteine.
bacteriochlorophyllide d C-12(1)-methyltransferase
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme and contains a [4Fe-4S] cluster.
It adds a methyl group at the C-12(1) position of bacteriochlorophylls of the c, d and e types.
This methylation plays a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influences the chlorosomes absorption properties.
8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d + S-adenosyl-L-methionine = 8,12-diethyl-3-vinylbacteriochlorophyllide d + H(+) + S-adenosyl-L-homocysteine.
bacteriochlorophyllide d C-8(2)-methyltransferase
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme.
It adds one or two methyl groups at the C-8(2) position of bacteriochlorophylls of the c, d and e types.
These methylations play a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influence chlorosomal absorption properties.
8,12-diethyl-3-vinylbacteriochlorophyllide d + S-adenosyl-L-methionine = 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d + H(+) + S-adenosyl-L-homocysteine.
12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d + S-adenosyl-L-methionine = 12-ethyl-8-isobutyl-3-vinylbacteriochlorophyllide d + H(+) + S-adenosyl-L-homocysteine.
bacteriochlorophyllide d C-20 methyltransferase
The enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), catalyzes the methylation of the C-20 methine bridge position in bacteriochlorophyllide d, forming bacteriochlorophyllide c.
a bacteriochlorophyllide d + S-adenosyl-L-methionine = a bacteriochlorophyllide c + H(+) + S-adenosyl-L-homocysteine.
The enzyme, found in many bacterial taxa, is involved in a pathway that converts L-methionine to dimethyl sulfide.
methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine.
4-amino-anhydrotetracycline N(4)-methyltransferase
4-amino-4-dedimethylamino-anhydrotetracycline + S-adenosyl-L-methionine = 4-methylamino-4-dedimethylamino-anhydrotetracycline + H(+) + S-adenosyl-L-homocysteine.
4-methylamino-4-dedimethylamino-anhydrotetracycline + S-adenosyl-L-methionine = anhydrotetracycline + H(+) + S-adenosyl-L-homocysteine.
The enzyme, characterized from the plants Nerine bowdenii and Narcissus aff pseudonarcissus (daffodil), participates in the biosynthesis of alkaloids produced by plants that belong to the Amaryllidaceae family.
norbelladine + S-adenosyl-L-methionine = 4'-O-methylnorbelladine + H(+) + S-adenosyl-L-homocysteine.
The enzyme from opium poppy (Papaver somniferum) can also methylate (R)-reticuline, tetrahydropapaverine, (S)-glaucine and (S)-bulbocapnine.
It is involved in the biosynthesis of the quaternary benzylisoquinoline alkaloid magnoflorine.
(S)-reticuline + S-adenosyl-L-methionine = (S)-tembetarine + H(+) + S-adenosyl-L-homocysteine.
(S)-corytuberine + S-adenosyl-L-methionine = magnoflorine + S-adenosyl-L-homocysteine.
(R)-reticuline + S-adenosyl-L-methionine = (R)-tembetarine + H(+) + S-adenosyl-L-homocysteine.
(R)-tetrahydropapaverine + S-adenosyl-L-methionine = (R)-N-methyltetrahydropapaverine + H(+) + S-adenosyl-L-homocysteine.
(S)-glaucine + S-adenosyl-L-methionine = (S)-N-methylglaucine + H(+) + S-adenosyl-L-homocysteine.
(S)-bulbocapnine + S-adenosyl-L-methionine = (S)-N-methylbulbocapnine + H(+) + S-adenosyl-L-homocysteine.
desmethylxanthohumol 6'-O-methyltransferase
The enzyme can also methylate xanthogalenol.
desmethylxanthohumol + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + xanthohumol.
S-adenosyl-L-methionine + xanthogalenol = 4'-O-methylxanthohumol + H(+) + S-adenosyl-L-homocysteine.
The enzyme from hops (Humulus lupulus) has a broad substrate specificity.
The best substrates in vitro are resveratrol, desmethylxanthohumol, chalconaringenin and isoliquiritigenin.
S-adenosyl-L-methionine + xanthohumol = 4-O-methylxanthohumol + H(+) + S-adenosyl-L-homocysteine.
The enzyme, characterized from Hordeum vulgare (barley), catalyzes two successive N-methylation reactions during the biosynthesis of gramine, a toxic indole alkaloid.
3-(aminomethyl)indole + 2 S-adenosyl-L-methionine = gramine + 2 H(+) + 2 S-adenosyl-L-homocysteine.
vanillate/3-O-methylgallate O-demethylase
The enzyme, characterized from the bacterium Sphingomonas sp. SYK6, is involved in the degradation of lignin.
The enzyme has similar activities with vanillate and 3-O-methylgallate.
(6S)-5,6,7,8-tetrahydrofolate + vanillate = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3,4-dihydroxybenzoate.
(6S)-5,6,7,8-tetrahydrofolate + 3-O-methylgallate = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3,4,5-trihydroxybenzoate.
The enzyme, studied from the bacterium Escherichia coli O157:H7, is a radical SAM (AdoMet) enzyme that is involved in heme degradation and iron utilization under anaerobic conditions.
The enzyme uses two SAM molecules for the reaction.
The first molecule is used to generate a 5'-deoxyadenosyl radical, which abstracts a hydrogen atom from the methyl group of the second SAM molecule.
The newly formed methylene radical attacks the substrate, causing a rearrangement of the porphyrin ring that results in the liberation of iron.
heme b + 2 reduced [flavodoxin] + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + anaerobilin + Fe(2+) + L-methionine + 2 oxidized [flavodoxin] + S-adenosyl-L-homocysteine.
8-amino-8-demethylriboflavin N,N-dimethyltransferase
The enzyme, characterized from the soil bacterium Streptomyces davawensis, catalyzes the last two steps in the biosynthesis of the antibiotic roseoflavin.
8-amino-8-demethylriboflavin + 2 S-adenosyl-L-methionine = 2 H(+) + roseoflavin + 2 S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Singulisphaera acidiphila, catalyzes three successive methylations of the terminal delta-nitrogen in ornithine lipids.
an N(2)-[(3R)-3-(2-saturated-acyloxy)acyl]-L-ornithine lipid + 3 S-adenosyl-L-methionine = an N,N,N-trimethylornithine lipid + 3 H(+) + 3 S-adenosyl-L-homocysteine.
The product, psilocybin, is a psychoactive compound.
4-hydoxytryptamine 4-phosphate + 2 S-adenosyl-L-methionine = 2 H(+) + psilocybin + 2 S-adenosyl-L-homocysteine.
This enzyme, found in vertebrates, methylates a specific adenine in a hairpin structure of snRNA.
The effects of the binding of the methyltransferase to its substrate is important for the regulation of the activity of an isoform of EC 2.5.1.6, that produces S-adenosyl-L-methionine.
The enzyme also binds (and maybe methylates) the lncRNAs XIST and MALAT1 as well as a number of pre-mRNAs at specific positions often found in the intronic regions.
adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine.
Isolated from the bacterium Herpetosiphon aurantiacus.
(+)-kolavelool + S-adenosyl-L-methionine = (+)-O-methylkolavelool + H(+) + S-adenosyl-L-homocysteine.
This enzyme, found in eukaryotes, methylates adenines in mRNA with the consensus sequence RRACH.
an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine.
The enzyme is a dual-specificity methyltransferase that catalyzes the last two steps of toxoflavin biosynthesis.
Toxoflavin is a major virulence factor of several bacterial crop pathogens.
1,6-didemethyltoxoflavin + S-adenosyl-L-methionine = H(+) + reumycin + S-adenosyl-L-homocysteine.
reumycin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + toxoflavin.
The enzyme, found in a wide range of bacteria and archaea, is a radical SAM (AdoMet) enzyme that utilizes two molecules of S-adenosyl-L-methionine, one as the methyl group donor, and one for the creation of a 5'-deoxyadenosine radical that drives the reaction forward.
a menaquinone + reduced [flavodoxin] + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + an 8-methylmenaquinone + 3 H(+) + L-methionine + oxidized [flavodoxin] + S-adenosyl-L-homocysteine.
a 2-demethylmenaquinone + reduced [flavodoxin] + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + a 2-demethyl-8-methylmenaquinone + 3 H(+) + L-methionine + oxidized [flavodoxin] + S-adenosyl-L-homocysteine.
The enzyme, isolated from the bacterium Saccharothrix syringae, is involved in the biosynthesis of nocamycin I and nocamycin II.
nocamycin E + S-adenosyl-L-methionine = nocamycin I + S-adenosyl-L-homocysteine.
3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase
This activity is part of the noscapine biosynthesis pathway, as characterized in the plant Papaver somniferum (opium poppy).
It is catalyzed by heterodimeric complexes of the OMT2 gene product and the product of either OMT3 or 6OMT.
OMT2 is the catalytic subunit in both complexes.
(S)-S-adenosyl-L-methionine + 3-O-acetyl-4'-O-demethylpapaveroxine = 3-O-acetylpapaveroxine + H(+) + S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Streptomyces thioluteus, participates in the biosynthesis of the antibiotic aureothin.
An orthologous enzyme in the bacteria Streptomyces orinoci and Streptomyces spectabilis catalyzes a similar reaction in the biosynthesis of spectinabilin.
demethylluteothin + S-adenosyl-L-methionine = luteothin + S-adenosyl-L-homocysteine.
demethyldeoxyspectinabilin + S-adenosyl-L-methionine = deoxyspectinabilin + S-adenosyl-L-homocysteine.
[histone H3]-lysine(4) N-trimethyltransferase
This entry describes several enzymes that successively methylate the L-lysine(4) residue of histone H3 (H3K4), ultimately generating a trimethylated form.
These modifications influence the binding of chromatin-associated proteins.
In most cases the trimethylation of this position is associated with gene activation.
EC 2.1.1.364 describes enzymes that can catalyze only monomethylation of this substrate (the first sub-reaction of this entry).
L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-homocysteine.
[histone H3]-lysine(9) N-trimethyltransferase
This entry describes several enzymes that successively methylate the L-lysine(9) residue of histone H3 (H3K9), ultimately generating a trimethylated form.
In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes.
L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine.
[histone H3]-lysine(27) N-trimethyltransferase
This entry describes enzymes that successively methylate the L-lysine(27) residue of histone H3 (H3K27), ultimately generating a trimethylated form.
The methylation of lysine(27) leads to transcriptional repression of the affected target genes.
The enzyme associates with other proteins to form a complex that is essential for activity.
The enzyme can also methylate some non-histone proteins.
L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine.
[histone H3]-lysine(36) N-dimethyltransferase
This entry describes a group of metazoan enzymes that catalyze two successive methylations of lysine(36) of histone H3 (H3K36), forming mono- and dimethylated forms.
The product can be further methylated to the trimethyl form by EC 2.1.1.358.
The yeast SET2 enzyme can catalyze all three methylations (see EC 2.1.1.359).
L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-homocysteine.
[histone H3]-lysine(36) N-trimethyltransferase
The enzyme, characterized from yeast, catalyzes the successive methylation of lysine(36) of histone H3 (H3K36), forming the trimethylated form.
The enzyme couples the methylation reactions with transcriptional elongation through an interaction with the large subunit of RNA polymerase II.
In mammals this activity is catalyzed by two different enzymes, EC 2.1.1.357 and EC 2.1.1.358.
L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-homocysteine.
[histone H3]-lysine(79) N-trimethyltransferase
The enzyme successively methylates the L-lysine(79) residue of histone H3 (H3K79), ultimately generating a trimethylated form.
This is the only known methylation event of a lysine residue within the core region of a histone, as all other such modifications occur at the tail.
L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-homocysteine.
[histone H4]-lysine(20) N-methyltransferase
The enzyme catalyzes the monomethylation of the L-lysine(20) residue of histone H4 (H4K20).
This event is usually followed by further methylation by EC 2.1.1.362, [histone H4]-N-methyl-L-lysine(20) N-methyltransferase.
This enzyme plays a pivotal role in DNA replication.
Activity is high during the G2 and M phases, but declines significantly during G1 and S phases.
Mutations in the enzyme have severe consequences, including DNA double-strand breaks, activation of DNA damage checkpoints, defective cell cycle progression, and reduced cell proliferation.
L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine.
[histone H4]-N-methyl-L-lysine(20) N-methyltransferase
This entry describes a group of enzymes that catalyze a single methylation of monomethylated lysine(20) of histone H4 (H4K20m1, generated by EC 2.1.1.361), forming the dimethylated form.
This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes.
The double-methylated form of lysine(20) in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules.
Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.
N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Serratia plymuthica, participates in biosynthesis of sodorifen.
(2E,6E)-farnesyl diphosphate + S-adenosyl-L-methionine = H(+) + pre-sodorifen diphosphate + S-adenosyl-L-homocysteine.
[histone H3]-lysine(4) N-methyltransferase
This entry describes enzymes that catalyze a single methylation of the L-lysine(4) residue of histone H3 (H3K4), generating a monomethylated form.
This modifications influence the binding of chromatin-associated proteins and result in gene activation or suppression.
Some enzymes that catalyze this reaction continue to generate a trimethylated form; these enzymes are classified under EC 2.1.1.354.
L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine.
3-O-methylmannose polysaccharide 1-O-methyltransferase
The enzyme, characterized from the bacterium Mycolicibacterium hassiacum, participates in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria.
The methylation catalyzed by this enzyme was shown to block the reducing end of 3,3'-di-O-methyl-alpha-mannobiose, a probable early precursor of the 3-O-methylmannose polysaccharides.
3,3'-di-O-methyl-4alpha-mannobiose + S-adenosyl-L-methionine = 1,3,3'-tri-O-methyl-4alpha-mannobiose + H(+) + S-adenosyl-L-homocysteine.
[histone H3]-N(6),N(6)-dimethyl-lysine(9) N-methyltransferase
The enzyme methylates only dimethylated lysine(9) of histone H3 (H3K9), forming the trimethylated form.
This modification influences the binding of chromatin-associated proteins.
The enzyme is highly up-regulated in Huntington disease patients.
N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine.
[histone H3]-lysine(9) N-methyltransferase
This entry describes several enzymes that methylate the L-lysine-9 residue of histone H3 (H3K9) only once, generating a monomethylated form.
L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine.
[histone H3]-lysine(9) N-dimethyltransferase
This entry describes several enzymes, characterized from plants, that successively methylate the L-lysine-9 residue of histone H3 (H3K9) twice, ultimately generating a dimethylated form.
L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-homocysteine.
[histone H3]-lysine(27) N-methyltransferase
This entry describes enzymes that methylate the L-lysine-27 residue of histone H3 only once, generating a monomethylated form.
The methylation of lysine-27 leads to transcriptional repression of the affected target genes.
L-lysyl(27)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(27)-[histone H3] + S-adenosyl-L-homocysteine.
[histone H3]-lysine(4) N-dimethyltransferase
This entry describes enzymes that successively methylate the L-lysine(4) residue of histone H3 (H3K4) twice, ultimately generating a dimethylated form.
These modifications influence the binding of chromatin-associated proteins.The human NSD3 protein also catalyzes the activity of EC 2.1.1.371.
L-lysyl(4)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + 2 S-adenosyl-L-homocysteine.
[histone H3]-lysine(27) N-dimethyltransferase
This entry describes enzymes that successively methylate the L-lysine(27) residue of histone H3 (H3K27) twice, ultimately generating a dimethylated form.
The human NSD3 protein also catalyzes the activity of EC 2.1.1.370.
L-lysyl(27)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + 2 S-adenosyl-L-homocysteine.
[histone H4]-lysine(20) N-trimethyltransferase
The enzyme, characterized from the fission yeast Schizosaccharomyces pombe, catalyzes three successive methylations of the L-lysine-20 residue of histone H4 (H4K20), forming the trimethylated form.
The methylation of this site is apparently not involved in the regulation of gene expression or heterochromatin function but participates in DNA damage response.
L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-homocysteine.
2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase
methylthiohydroxybutyrate methyltransferase
The enzyme, characterized from the marine bacterium Labrenzia aggregata, participates in the biosynthesis of dimethylsulfoniopropanoate (DMSP).
A eukaryotic enzyme that shares little sequence similarity with the bacterial enzyme was identified in many marine phytoplankton species.
(2R)-2-hydroxy-4-(methylsulfanyl)butanoate + S-adenosyl-L-methionine = (2R)-4-(dimethylsulfaniumyl)-2-hydroxybutanoate + S-adenosyl-L-homocysteine.
2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
The enzyme, found in mycobacteria, is a member of a family of heterocyclic toxin methyltransferases.
It is involved in defense against several antimicrobial natural compounds and drugs.
4-Hydroxyquinolin-2(1H)-one, 2-heptylquinolin-4(1H)-one, 2-heptyl-3-hydroxyquinolin-4(1H)-one (the "Pseudomonas quinolone signal", PQS) and the flavonol quercetin are also O-methylated, albeit with lower activity.
The enzyme also N-methylates the bactericidal compound 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile.
2-heptyl-1-hydroxy-4(1H)-quinolinone + S-adenosyl-L-methionine = 2-heptyl-1-methoxy-4(1H)-quinolinone + H(+) + S-adenosyl-L-homocysteine.
3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone + S-adenosyl-L-methionine = 3-bromo-2-heptyl-1-methoxy-4(1H)-quinolinone + H(+) + S-adenosyl-L-homocysteine.
3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile + S-adenosyl-L-methionine = 3,5-dimethyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile + H(+) + S-adenosyl-L-homocysteine.
The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses) catalyzes two successive methylations.
In higher eukaryotes the two methylations occur in the reverse order and are catalyzed by two different enzymes (cf. EC 2.1.1.56 and EC 2.1.1.57) that do not required a specific motif.
a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine.
glycine betaine--corrinoid protein Co-methyltransferase
The enzyme, which catalyzes the transfer of a methyl group from glycine betaine to a glycine betaine-specific corrinoid protein (MtgC), is involved in methanogenesis from glycine betaine in some methanogenic archaea, and in glycine betaine degradation in some bacteria.
Unlike similar enzymes involved in methanogenesis from methylated C1 compounds, this enzyme does not contain the unusual amino acid L-pyrrolysine.
Co(I)-[glycine betaine-specific corrinoid protein] + glycine betaine + H(+) = methyl-Co(III)-[glycine betaine-specific corrinoid protein] + N,N-dimethylglycine.
[methyl-Co(III) glycine betaine-specific corrinoid protein]--coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from glycine betaine, catalyzes the transfer of a methyl group bound to the cobalt cofactor of glycine betaine-specific corrinoid protein to coenzyme M, forming the substrate for EC 2.8.4.1, which catalyzes the final step in methanogenesis.
The enzyme from the methanogenic archaeon Methanolobus vulcani B1d can also catalyze the activity of EC 2.1.1.246.
coenzyme M + methyl-Co(III)-[glycine betaine-specific corrinoid protein] = Co(I)-[glycine betaine-specific corrinoid protein] + H(+) + methyl-coenzyme M.
[methyl-Co(III) glycine betaine-specific corrinoid protein]--tetrahydrofolate methyltransferase
This enzyme, characterized from the anaerobic bacterium Desulfitobacterium hafniense Y51, catalyzes a similar reaction to that of EC 2.1.1.258, but in the opposite direction, transferring a methyl group from a methylated corrinoid protein to tetrahydrofolate.
The corrinoid protein is specifically methylated by EC 2.1.1.376.
(6S)-5,6,7,8-tetrahydrofolate + methyl-Co(III)-[glycine betaine-specific corrinoid protein] = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + Co(I)-[glycine betaine-specific corrinoid protein] + H(+).
[methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
The enzyme, present in methanogenic archaea, catalyzes a modification of an L-arginine residue at the active site of EC 2.8.4.1, which catalyzes the last and methane-releasing step of methanogenesis.
The enzyme is a radical AdoMet (radical SAM) enzyme and contains an [4Fe-4S] cluster and a Coalpha-[alpha-(5-hydroxybenzimidazolyl)]-cobamide cofactor.
The methyl group, which is derived from S-adenosyl-L-methionine, is transferred to the cob(I)amide cofactor, forming methylcob(III)amide as an intermediate carrier, before being transferred to the arginine residue.
AH2 + L-arginyl-[methyl-coenzyme M reductase] + 2 S-adenosyl-L-methionine = (5S)-C-methyl-L-arginyl-[methyl-coenzyme M reductase] + 5'-deoxyadenosine + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine.
3-amino-4-hydroxybenzoate 4-O-methyltransferase
The enzyme, characterized from the bacterium Streptomyces cremeus, is involved in cremeomycin biosynthesis.
3-amino-2,4-dihydroxybenzoate + S-adenosyl-L-methionine = 3-amino-2-hydroxy-4-methoxybenzoate + H(+) + S-adenosyl-L-homocysteine.
The enzyme, characterized from the bacterium Streptomyces achromogenes subsp. streptozoticus, participates in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin.
L-arginine + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginine + S-adenosyl-L-homocysteine.
methoxylated aromatic compound--corrinoid protein Co-methyltransferase
This entry stands for a family of enzymes that have been characterized from acetogenic bacteria and archaeal species.
Different members of this family have different substrate specificity.
In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in acetogenic bacteria and in non-methanogenic archaea it participates in methoxydotrophic growth.
Most of the enzymes have a wide specificity and were shown to act on a large number of methoxylated aromatic compounds, carrying a methoxy group at positions 2, 3 or 4 of the aromatic ring.
Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state; during methylation the cobalt is oxidized to the Co(III) state.
a methoxylated aromatic compound + Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) = a phenol + methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein].
Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) + vanillate = 3,4-dihydroxybenzoate + methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein].
3-hydroxy-4-methoxybenzoate + Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) = 3,4-dihydroxybenzoate + methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein].
Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) + syringate = 3-O-methylgallate + methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein].
Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + guaiacol + H(+) = catechol + methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein].
3-methoxyphenol + Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) = methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein] + resorcinol.
Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) + veratrole = 3-methoxyphenol + methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein].
2-methoxybenzoate + Co(I)-[methoxylated-aromatic-compound-specific corrinoid protein] + H(+) = methyl-Co(III)-[methoxylated-aromatic-compound-specific corrinoid protein] + salicylate.
L-carnitine--corrinoid protein Co-methyltransferase
The enzyme, characterized from the bacterium Eubacterium limosum, is a component of a system that transfers a methyl group from L-carnitine to tetrahydrofolate, as part of an L-carnitine degradation pathway.
The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood--Ljungdahl pathway.
(R)-carnitine + Co(I)-[quaternary-amine-specific corrinoid protein] + H(+) = (3R)-4-(dimethylamino)-3-hydroxybutanoate + methyl-Co(III)-[quaternary-amine-specific corrinoid protein].
The enzyme from Dictyostelium discoideum is involed in modifying the resorcinolic back-bone of the differentiation regulating factor 4-methyl-5-pentylbenzene-1,3-diol.
It also shows activity toward 5-pentylbenzene-1,3-diol.
resorcinol + S-adenosyl-L-methionine = 3-methoxyphenol + H(+) + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + thiocyanate = methyl thiocyanate + S-adenosyl-L-homocysteine.
5-pentadecatrienyl resorcinol O-methyltransferase
In Sorghum, this enzyme is part of the biosynthetic pathway of the phytotoxin sorgoleone.
(8Z,11Z)-5-(pentadeca-8,11,14-trien-1-yl)resorcinol + S-adenosyl-L-methionine = (8Z,11Z)-5-(pentadeca- 8,11,14-trien-1-yl)resorcinol-3-methyl ether + H(+) + S-adenosyl-L-homocysteine.
Adds a methyl group to the ribose of the last nucleotide of small RNAs (sRNAs).
This protects the 3'-end of sRNAs from uridylation activity and subsequent degradation.
Can methylates 3'-end of microRNAs (miRNAs), small interfering RNAs (siRNas) and trans-acting small interfering RNAs (ta-siRNAs).
S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide.
methylphosphotriester-DNA--[protein]-cysteine S-methyltransferase
This protein is involved in the repair of Sp diastereomers of DNA methylphosphotriester lesions.
This enzyme catalyzes only one turnover and therefore is not strictly catalytic.
The enzyme from the bacterium Escherichia coli also has the activity of EC 2.1.1.63 while the enzyme from Bacillus subtilis does not.
(2'-deoxyribonucleoside 5'-methylphosphotriester)-DNA + L-cysteinyl-[protein] = 2'-deoxyribonucleotide-DNA + H(+) + S-methyl-L-cysteinyl-[protein].
Hydroxymethyl-, formyl- and related transferases
Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine.
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine.
phosphoribosylglycinamide formyltransferase 1
2-amino-N-ribosylacetamide 5'-phosphate transformylase
5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase
5'-phosphoribosylglycinamide transformylase
glycinamide ribonucleotide transformylase
Two enzymes are known to catalyze the third step in de novo purine biosynthesis.
This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC 6.3.1.21, utilizes formate.
In vertebrates this activity is catalyzed by a trifunctional enzyme that also catalyzes the activities of EC 6.3.4.13 and EC 6.3.3.1.
(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide.
phosphoribosylaminoimidazolecarboxamide formyltransferase
10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase
5-amino-4-imidazolecarboxamide ribonucleotide transformylase
5-amino-4-imidazolecarboxamide ribotide transformylase
aminoimidazolecarboxamide ribonucleotide transformylase
(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
5-formimidoyltetrahydrofolate + glycine = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoylglycine.
The enzymes also catalyzes formyl transfer from 5-formyltetrahydrofolate to L-glutamate.
In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
5-formimidoyltetrahydrofolate + L-glutamate = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoyl-L-glutamate.
(6S)-5-formyl-5,6,7,8-tetrahydrofolate + L-glutamate = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-glutamate.
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine.
deoxycytidylate 5-hydroxymethyltransferase
Deoxycytidylate hydroxymethyltransferase
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dCMP + H2O = (6S)-5,6,7,8-tetrahydrofolate + 5-hydroxymethyl-dCMP.
formylmethionyl-transfer ribonucleic synthetase
methionyl-transfer ribonucleate methyltransferase
methionyl-transfer ribonucleic transformylase
N(10)-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase
(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet).
A component, with EC 1.4.4.2 and EC 1.8.1.4, of the glycine cleavage system, formerly known as glycine synthase.
(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+).
3-methyl-2-oxobutanoate hydroxymethyltransferase
alpha-ketoisovalerate hydroxymethyltransferase
dehydropantoate hydroxymethyltransferase
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate.
UDP-4-amino-4-deoxy-L-arabinose formyltransferase
The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305.
(6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose.
The enzyme, characterized from the bacterium Brucella melitensis, synthesizes a building block of the O antigen produced by Brucella species.
(6S)-10-formyltetrahydrofolate + GDP-alpha-D-perosamine = (6S)-5,6,7,8-tetrahydrofolate + GDP-N-formyl-alpha-D-perosamine + H(+).
A biotinyl-protein, containing cobalt and zinc.
The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyzes carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains.
The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.
(S)-methylmalonyl-CoA + pyruvate = oxaloacetate + propanoyl-CoA.
carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate.
The plant enzyme also catalyzes the reactions of EC 2.1.3.6, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, converting agmatine and ornithine into putrescine and citrulline respectively.
carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate.
carbamoyl phosphate + oxamate = N-carbamoyl-2-oxoglycine + phosphate.
The plant enzyme also catalyzes the reactions of EC 2.1.3.3, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, converting agmatine and ornithine into putrescine and citrulline respectively.
carbamoyl phosphate + putrescine = H(+) + N-carbamoylputrescine + phosphate.
3-hydroxymethylcephem carbamoyltransferase
Acts on a wide range of 3-hydroxymethylcephems (a subclass of the cephalosporin antibiotics).
carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate = phosphate + a 3-carbamoyloxymethylcephem.
carbamoyl phosphate + L-lysine = H(+) + L-homocitrulline + phosphate.
This enzyme replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of several eubacteria and has no catalytic activity with L-ornithine as substrate.
carbamoyl phosphate + N(2)-acetyl-L-ornithine = H(+) + N(2)-acetyl-L-citrulline + phosphate.
malonyl-S-ACP:biotin-protein carboxyltransferase
Derived from the components MadC and MadD of the anaerobic bacterium Malonomonas rubra, this enzyme is a component of EC 7.2.4.4.
The carboxy group is transferred from malonate to the prosthetic group of the biotin protein (MadF) with retention of configuration.
Similar to EC 4.1.1.87, which forms part of the biotin-independent EC 4.1.1.88, this enzyme also follows on from EC 2.3.1.187, and results in the regeneration of the acetyl-[acyl-carrier protein].
malonyl-[ACP] + N(6)-biotinyl-L-lysyl-[protein] = acetyl-[ACP] + N(6)-carboxybiotinyl-L-lysyl-[protein].
N-succinylornithine carbamoyltransferase
Specific for N-succinyl-L-ornithine and cannot use either L-ornithine (see EC 2.1.3.3) or N-acetyl-L-ornithine (see EC 2.1.3.9) as substrate.
However, a single amino-acid substitution (Pro90Glu) is sufficient to switch the enzyme to one that uses N-acetyl-L-ornithine as substrate.
It is essential for de novo arginine biosynthesis in the obligate anaerobe Bacteroides fragilis, suggesting that this organism uses an alternative pathway for synthesizing arginine.
carbamoyl phosphate + N(2)-succinyl-L-ornithine = H(+) + N(2)-succinyl-L-citrulline + phosphate.
decarbamoylnovobiocin carbamoyltransferase
The enzyme catalyzes the last step in the biosynthesis of the aminocoumarin antibiotic novobiocin.
carbamoyl phosphate + descarbamoylnovobiocin = novobiocin + phosphate.
The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA.
In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2).
Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3).
acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein].
The enzyme, characterized from the bacterium Rubrobacter xylanophilus, is involved in a purine degradation pathway.
(S)-2-ureidoglycine + carbamoyl phosphate = allantoate + H(+) + phosphate.
glycine + L-arginine = guanidinoacetate + L-ornithine.
scyllo-inosamine-4-phosphate amidinotransferase
L-arginine:inosamine phosphate amidinotransferase
1D-1-Guanidino-3-amino-1,3-dideoxy-scyllo-inositol 6-phosphate, streptamine phosphate and 2-deoxystreptamine phosphate can also act as acceptors.
1-amino-1-deoxy-scyllo-inositol 4-phosphate + L-arginine = 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + L-ornithine.
The enzyme, characterized from the bacterium Pseudomonas savastanoi pv. phaseolicola, is involved in the biosynthesis of the toxin phaseolotoxin, a modified tripeptide that causes the 'halo blight' disease of beans.
L-arginine + L-lysine = L-homoarginine + L-ornithine.
L-canavanine + L-ornithine = H(+) + L-arginine + L-canaline.
(+)-sesamin + (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) = (+)-sesamin monocatechol + (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n).
(+)-sesamin monocatechol + (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) = (+)-sesamin dicatechol + (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n).
Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH.
The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate.
D-erythrose 4-phosphate + D-xylulose 5-phosphate = beta-D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate.
D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate.
Also converts hydroxypyruvate and formaldehyde into glycerone and CO2.
D-xylulose 5-phosphate + formaldehyde = D-glyceraldehyde 3-phosphate + dihydroxyacetone.
acetoin--ribose-5-phosphate transaldolase
1-deoxy-D-altro-heptulose-7-phosphate synthetase
acetoin + aldehydo-D-ribose 5-phosphate = 1-deoxy-D-altro-heptulose 7-phosphate + acetaldehyde.
2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating)
alpha-ketoglutaric-glyoxylic carboligase
The product decarboxylates to 5-hydroxy-4-oxopentanoate.
The enzyme can decarboxylate 2-oxoglutarate.
2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2.
acetolactate pyruvate-lyase (carboxylating)
The reaction shown is in the pathway of biosynthesis of valine.
The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2.
2-oxobutanoate + H(+) + pyruvate = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + CO2.
1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating)
The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.
D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2.
Can also convert chloroacetaldehyde into 4-chloro-L-threonine.
Unlike EC 2.1.2.1 does not use glycine as a substrate.
fluoroacetaldehyde + L-threonine = 4-fluoro-L-threonine + acetaldehyde.
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase
Involved in the biosynthesis of vitamin K2 (menaquinone).
In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival.
It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO2 but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20.
Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC.
2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2.
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
The enzyme can also catalyze the cleavage of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4-semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate.
6-deoxy-5-ketofructose 1-phosphate synthase
The enzyme can also catalyze the reaction of EC 4.1.2.13.
beta-D-fructose 1,6-bisphosphate + methylglyoxal = 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + D-glyceraldehyde 3-phosphate.
beta-D-fructose 1-phosphate + methylglyoxal = 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + D-glyceraldehyde.
The enzyme, characterized from the bacterium Serratia marcescens, participates in the biosynthesis of the antibiotic prodigiosin.
The enzyme decarboxylates pyruvate, followed by attack of the resulting two-carbon fragment on (E)-oct-2-enal, resulting in a Stetter reaction.
In vitro the enzyme can act on a number of alpha,beta-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyze both 1-2 and 1-4 carboligations depending on the substrate.
(2E)-octenal + H(+) + pyruvate = (S)-3-acetyloctanal + CO2.
apulose 4-phosphate + D-glyceraldehyde 3-phosphate = D-xylulose 5-phosphate + dihydroxyacetone phosphate.
6-deoxy-6-sulfo-D-fructose transaldolase
The enzyme, characterized from the bacterium Bacillus aryabhattai SOS1, is involved in a degradation pathway for 6-sulfo-D-quinovose.
The enzyme can also use D-erythrose 4-phosphate as the acceptor, forming D-sedoheptulose 7-phosphate.
6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde 3-phosphate = (2S)-3-sulfolactaldehyde + D-fructose 6-phosphate.
6-deoxy-6-sulfo-D-fructose + D-erythrose 4-phosphate = (2S)-3-sulfolactaldehyde + D-sedoheptulose 7-phosphate.
Transferring groups other than amino-acyl groups
Also acts with L-aspartate and, more slowly, with some other amino acids.
acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate.
1H-imidazole + acetyl-CoA = CoA + N-acetylimidazole.
acetyl-CoA + D-glucosamine = CoA + H(+) + N-acetyl-D-glucosamine.
glucosamine-phosphate N-acetyltransferase
aminodeoxyglucosephosphate acetyltransferase
glucosamine 6-phosphate N-acetyltransferase
N-acetylglucosamine-6-phosphate synthase
acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate.
Wide specificity for aromatic amines, including serotonin; also catalyzes acetyl-transfer between arylamines without CoA.
acetyl-CoA + an arylamine = an N-acetylarylamine + CoA.
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
acetyl-CoA + choline = acetylcholine + CoA.
Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 and EC 2.3.1.137).
(R)-carnitine + acetyl-CoA = CoA + O-acetyl-(R)-carnitine.
Also acts with other short-chain acyl-CoAs.
acetyl-CoA + phosphate = acetyl phosphate + CoA.
The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms.
The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA.
In the second step the acyl group is transferred to an acetyl-CoA molecule.
acetyl-CoA + hydrogen sulfide = CoA + thioacetate.
2-sulfanylethan-1-ol (2-mercaptoethanol) can act as a substrate.
acetyl-CoA + cysteamine = CoA + S-acetylcysteamine.
dihydrolipoyllysine-residue acetyltransferase
acetyl-CoA:dihydrolipoamide S-acetyltransferase
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4.
The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA.
(R)-dihydrolipoamide + acetyl-CoA = (R)-S(6)-acetyldihydrolipoamide + CoA.
The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor.
Not identical with EC 2.3.1.68 or EC 2.3.1.71.
an acyl-CoA + glycine = an N-acylglycine + CoA + H(+).
L-glutamine + phenylacetyl-CoA = CoA + H(+) + N(2)-phenylacetyl-L-glutamine.
glycerol-3-phosphate 1-O-acyltransferase
Acyl-[acyl-carrier-protein] can also act as acyl donor.
Acts only with derivatives of fatty acids of chain length above C10.
an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA.
The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation.
The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl-CoA shortened by two carbon atoms.
The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA.
In the second step the acyl group is transferred to CoA.
Most enzymes have a broad substrate range for the 3-oxoacyl-CoA.
acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA.
acetyl-CoA + L-aspartate = CoA + H(+) + N-acetyl-L-aspartate.
Acts on thiogalactosides and phenylgalactoside.
a beta-D-galactoside + acetyl-CoA = a 6-acetyl-beta-D-galactoside + CoA.
butanoyl-CoA + phosphate = butanoyl phosphate + CoA.
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA.
Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA (cf. EC 2.3.1.7 and EC 2.3.1.137).
(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine.
Various 2-acylglycerols can act as acceptor.
The sn-1 position and the sn-3 position are both acylated, at about the same rate.
a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol + CoA.
1-acylglycerophosphocholine O-acyltransferase
Acts preferentially with unsaturated acyl-CoA derivatives.
1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA.
a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine + CoA + H(+).
1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + an acyl-CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CoA.
The enzyme catalyzes the formation of sterol esters from a sterol and long-chain fatty acyl-coenzyme A.
The enzyme from yeast, but not from mammals, prefers monounsaturated acyl-CoA.
In mammals the enzyme acts mainly on cholesterol and forms cholesterol esters that are stored in cytosolic droplets, which may serve to protect cells from the toxicity of free cholesterol.
In macrophages, the accumulation of cytosolic droplets of cholesterol esters results in the formation of 'foam cells', a hallmark of early atherosclerotic lesions.
In hepatocytes and enterocytes, cholesterol esters can be incorporated into apolipoprotein B-containing lipoproteins for secretion from the cell.
a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA.
an acyl-CoA + cholesterol = a cholesterol ester + CoA.
acetyl-CoA + cortisol = CoA + cortisol 21-acetate.
acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA.
2-amino-3-ketobutyrate coenzyme A ligase
Acts in concert with EC 1.1.1.103 in the degradation of threonine to form glycine.
This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex.
acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA.
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.
acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine.
acetyl phosphate + L-lysine = H(+) + N(6)-acetyl-L-lysine + phosphate.
acetyl-CoA + L-histidine = CoA + H(+) + N(alpha)-acetyl-L-histidine.
acetyl-CoA + D-tryptophan = CoA + H(+) + N-acetyl-D-tryptophan.
acetylglutamate-acetylornithine transacetylase
acetylglutamic-acetylornithine transacetylase
acetylornithine glutamate acetyltransferase
Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate.
a D-alpha-amino acid + acetyl-CoA = an N-acetyl-D-amino acid + CoA + H(+).
glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA.
[acyl-carrier-protein] S-acetyltransferase
acetyl coenzyme A-acyl-carrier-protein transacylase
Essential, along with EC 2.3.1.39, for the initiation of fatty-acid biosynthesis in bacteria.
The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide.
This is one of the activities associated with EC 2.3.1.180.
acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA.
[acyl-carrier-protein] S-malonyltransferase
malonyl-CoA/dephospho-CoA acyltransferase
malonyl-CoA-acyl carrier protein transacylase
malonyl coenzyme A-acyl carrier protein transacylase
Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria.
Also provides the malonyl groups for polyketide biosynthesis.
The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis.
In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate.
This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89.
Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase.
In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates.
The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP].
acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP].
beta-ketoacyl-[acyl-carrier-protein] synthase I
3-ketoacyl-acyl carrier protein synthase
3-oxoacyl-[acyl-carrier-protein] synthase
acyl-malonyl(acyl-carrier-protein)-condensing enzyme
acyl-malonyl acyl carrier protein-condensing enzyme
beta-ketoacyl-[acyl carrier protein] synthase
beta-ketoacyl acyl carrier protein synthase
beta-ketoacyl-acyl carrier protein synthetase
Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain.
Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids.
Can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16).
The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP].
dihydroxyacetone phosphate acyltransferase
Uses CoA derivatives of palmitate, stearate, and oleate, with highest activity on palmitoyl-CoA.
an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone 3-phosphate + CoA.
phosphatidylcholine--sterol O-acyltransferase
phospholipid--cholesterol acyltransferase
Palmitoyl, oleoyl, and linoleoyl can be transferred; a number of sterols, including cholesterol, can act as acceptors.
The bacterial enzyme also catalyzes the reactions of EC 3.1.1.4 and EC 3.1.1.5.
a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-acyl-sn-glycero-3-phosphocholine + a sterol ester.
N-acetylneuraminate 4-O-acetyltransferase
Both free and glycosidically bound N-acetyl- and N-glycolyl- neuraminates can act as O-acetyl acceptors.
acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-4-O-acetylneuraminate.
N-acetylneuraminate 7-O(or 9-O)-acetyltransferase
Both free and glycosidically bound N-acetyl- and N-glycolylneuraminates can act as O-acetyl acceptors.
acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O-acetylneuraminate.
acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-9-O-acetylneuraminate.
L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine.
7-keto-8-aminopelargonic acid synthetase
The enzyme catalyzes the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis.
Pimeloyl-CoA can be used with lower efficiency.
6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP].
6-carboxyhexanoyl-CoA + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + CoA.
A group of enzymes acetylating histones.
Several of the enzymes can also acetylate lysines in other proteins.
acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein].
acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone].
deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase
Both this enzyme and EC 6.2.1.22 acetylate and activate EC 4.1.3.6.
holo-[citrate lyase ACP] + S-acetylphosphopantotheine = (R)-4'-phosphopantetheine + acetyl-[citrate lyase ACP].
H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA.
1-acylglycerol-3-phosphate O-acyltransferase
The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA.
2-acylglycerol-3-phosphate O-acyltransferase
Saturated acyl-CoA thioesters are the most effective acyl donors.
a 2-acyl-sn-glycerol 3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA.
Also acts, more slowly, on L-histidine and L-alanine.
acetyl-CoA + L-phenylalanine = CoA + H(+) + N-acetyl-L-phenylalanine.
aromatic-hydroxylamine O-acetyltransferase
Transfers the N-acetyl group of some aromatic acethydroxamates to the O-position of some aromatic hydroxylamines.
N-hydroxy-4-acetylaminobiphenyl = N-acetoxy-4-aminobiphenyl.
acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase
Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine.
acetyl-CoA + an alkane-alpha,omega-diamine = an N-acetylalkane-alpha,omega-diamine + CoA + H(+).
acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine.
acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine.
acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine.
2,3-diaminopropionate N-oxalyltransferase
(S)-2,3-diaminopropanoate + oxalyl-CoA = CoA + N(3)-oxalyl-L-2,3-diaminopropanoate.
The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, neomycin B, kanamycin B and kanamycin C can also act as acceptors.
acetyl-CoA + gentamicin C1a = CoA + H(+) + N(2')-acetylgentamicin C1a.
aminoglycoside acetyltransferase AAC(3)-1
acetyl-CoA + gentamicin C = CoA + H(+) + N(3)-acetylgentamycin C.
dihydrolipoyllysine-residue succinyltransferase
succinyl-CoA:dihydrolipoamide S-succinyltransferase
succinyl-CoA:dihydrolipoate S-succinyltransferase
A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4.
The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA.
2-acylglycerophosphocholine O-acyltransferase
a 2-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA.
1-alkylglycerophosphocholine O-acyltransferase
1-O-alkyl-sn-glycero-3-phosphocholine + an acyl-CoA = 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + CoA.
p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase
4-coumaroyl-CoA + agmatine = CoA + H(+) + N-(4-guanidinobutyl)-4-hydroxycinnamamide.
bile acid-CoA:amino acid N-acyltransferase
cholyl-CoA glycine-taurine N-acyltransferase
Also acts on CoA derivatives of other bile acids.
Taurine and 2-fluoro-beta-alanine can act as substrates, but more slowly.
Can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase.
Bile-acid--amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol.
This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalyzed by EC 6.2.1.7.
choloyl-CoA + glycine = CoA + glycocholate + H(+).
Propanoyl-CoA can act, more slowly, as donor.
L-arginine, L-valine, L-phenylalanine and peptides containing L-leucine can act as acceptor.
acetyl-CoA + L-leucine = CoA + H(+) + N-acetyl-L-leucine.
1-alkylglycerophosphocholine O-acetyltransferase
1-alkyl-2-lysolecithin acetyltransferase
1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase
acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine 2-O-acetyltransferase
acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase
blood platelet-activating factor acetyltransferase
lyso-platelet activating factor:acetyl-CoA acetyltransferase
lyso-platelet-activating factor:acetyl-CoA acetyltransferase
platelet-activating factor acylhydrolase
platelet-activating factor-synthesizing enzyme
1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA.
Phenylacetyl-CoA and (indol-3-yl)acetyl-CoA, but not benzoyl-CoA, can act as acyl donor.
Not identical with EC 2.3.1.13 or EC 2.3.1.71.
an acyl-CoA + L-glutamine = an N(2)-acyl-L-glutamine + CoA + H(+).
(-)-menthol, (+)-neomenthol, borneol, cyclohexanol and N-decanol can be acetylated.
acetyl-CoA + a monoterpenol = CoA + a monoterpenol acetate ester.
Not identical with EC 2.3.1.13 or EC 2.3.1.68.
benzoyl-CoA + glycine = CoA + H(+) + N-benzoylglycine.
indoleacetylglucose--inositol O-acyltransferase
The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups.
1-O-(indol-3-ylacetyl)-beta-D-glucose + myo-inositol = D-glucose + indole-3-acetyl-1D-myo-inositol.
diacylglycerol--sterol O-acyltransferase
Cholesterol, sitosterol, campesterol and diacylglycerol can act as acceptors.
Transfers a number of long-chain fatty acyl groups.
a 1,2-diacyl-sn-glycerol + a sterol = a 1-acyl-sn-glycerol + a sterol ester.
The enzyme catalyzes the first committed step in the biosynthesis of flavonoids.
It can also act on dihydro-4-coumaroyl-CoA, forming phloretin.
4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA.
long-chain-alcohol O-fatty-acyltransferase
Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes.
The best acceptor is cis-icos-11-en-1-ol.
a fatty acyl-CoA + a long chain fatty alcohol = a wax ester + CoA.
Acts on palmitoyl-CoA and other long-chain fatty-acyl derivatives of CoA.
all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA.
triacylglycerol--sterol O-acyltransferase
Tripalmitoylglycerol can act as donor, and, more slowly, other triacylglycerols containing C6 to C22 fatty acids.
The best acceptors are 3beta-hydroxysteroids with a planar ring system.
a 3beta-hydroxysteroid + a triacylglycerol = a 3beta-hydroxysteroid ester + a diacylglycerol.
heparan-alpha-glucosaminide N-acetyltransferase
Brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed.
Not identical with EC 2.3.1.3 or EC 2.3.1.4.
acetyl-CoA + alpha-D-glucosaminyl-[heparan sulfate](n) = CoA + H(+) + N-acetyl-alpha-D-glucosaminyl-[heparan sulfate](n).
acetyl-CoA + D-maltose = 1-O-acetylmaltose + CoA.
cysteine-S-conjugate N-acetyltransferase
S-benzyl-L-cysteine and, in decreasing order of activity, S-butyl-L-cysteine, S-propyl-L-cysteine, O-benzyl-L-serine and S-ethyl-L-cysteine, can act as acceptor.
acetyl-CoA + an S-substituted L-cysteine = an N-acetyl-L-cysteine-S-conjugate + CoA + H(+).
A wide range of antibiotics containing the 2-deoxystreptamine ring can act as acceptor, including gentamicin, kanamycin, tobramycin, neomycin and apramycin.
a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-acetyl-2-deoxystreptamine antibiotic + CoA + H(+).
The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, gentamicin C2, sisomicin and tobramycin are substrates.
The antibiotic paromomycin is not a substrate.
The 6-amino group of the purpurosamine ring is acetylated.
acetyl-CoA + kanamycin B = CoA + H(+) + N(6')-acetylkanamycin B.
phosphatidylcholine--dolichol O-acyltransferase
a 1,2-diacyl-sn-glycero-3-phosphocholine + di-trans,poly-cis-dolichol = a 1-acyl-sn-glycero-3-phosphocholine + acyldolichol.
Acts on a range of short-chain aliphatic alcohols, including methanol and ethanol.
acetyl-CoA + an aliphatic alcohol = an acetyl ester + CoA.
The animal enzyme is a multifunctional protein catalyzing the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, EC 4.2.1.59, EC 1.3.1.39 and EC 3.1.2.14.
acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+).
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits.
One subunit catalyzes the reactions EC 1.1.1.100 and EC 2.3.1.41, while the other subunit catalyzes the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 4.2.1.59, EC 1.3.1.10 and EC 1.1.1.279.
The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+).
Narrow specificity toward 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine.
This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4).
2-arylethylamine + acetyl-CoA = CoA + H(+) + N-acetyl-2-arylethylamine.
acetyl-CoA + serotonin = CoA + H(+) + N-acetylserotonin.
tetrahydrodipicolinate N-acetyltransferase
(S)-2,3,4,5-tetrahydrodipicolinate + acetyl-CoA + H2O = CoA + L-2-acetamido-6-oxoheptanedioate.
beta-Glucogallin can act as donor and as acceptor.
Digalloylglucose can also act as acceptor, with the formation of 1-O,2-O,6-O-trigalloylglucose.
2 1-O-galloyl-beta-D-glucose = 1,6-bis-O-galloyl-beta-D-glucose + D-glucose.
sinapoylglucose--choline O-sinapoyltransferase
1-O-(trans-sinapoyl)-beta-D-glucose + choline = D-glucose + O-sinapoylcholine.
sinapoylglucose--malate O-sinapoyltransferase
(S)-malate + 1-O-(trans-sinapoyl)-beta-D-glucose = D-glucose + sinapoyl (S)-malate.
Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA and butanoyl-CoA can act as acyl donors.
Involved in the synthesis of lupanine alkaloids.
(2E)-2-methylbut-2-enoyl-CoA + 13-hydroxylupanine = 13-(2-methylcrotonoyloxy)lupanine + CoA.
The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics.
Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3.
The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain.
Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP).
The KS domain both accepts the growing polyketide chain from the previous module and catalyzes the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain.
This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms.
6 (S)-methylmalonyl-CoA + 12 H(+) + 6 NADPH + propanoyl-CoA = 6-deoxyerythronolide B + 6 CO2 + 7 CoA + H2O + 6 NADP(+).
Not identical with EC 2.3.1.74 or EC 2.3.1.146.
4-coumaroyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA + trans-resveratrol.
glycylpeptide N-tetradecanoyltransferase
The enzyme catalyzes the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins.
It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide.
The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein].
chlorogenate--glucarate O-hydroxycinnamoyltransferase
Galactarate can act as acceptor, more slowly.
Involved with EC 2.3.1.99 in the formation of caffeoylglucarate in tomato.
chlorogenate + D-glucarate = 2-O-caffeoylglucarate + L-quinate.
hydroxycinnamoyl coenzyme A-quinate transferase
Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, more slowly.
Involved in the biosynthesis of chlorogenic acid in sweet potato and, with EC 2.3.1.98 in the formation of caffeoyl-CoA in tomato.
(E)-feruloyl-CoA + L-quinate = 4-O-feruloyl-D-quinate + CoA.
[myelin-proteolipid] O-palmitoyltransferase
The enzyme in brain transfers long-chain acyl residues to the endogenous myelin proteolipid.
palmitoyl-CoA + [myelin proteolipid] = CoA + O-palmitoyl-[myelin proteolipid].
formylmethanofuran--tetrahydromethanopterin N-formyltransferase
Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin.
Involved in the synthesis of aerobactin from lysine in a strain of Escherichia coli.
acetyl-CoA + N(6)-hydroxy-L-lysine = CoA + N(6)-acetyl-N(6)-hydroxy-L-lysine.
sinapoylglucose--sinapoylglucose O-sinapoyltransferase
2 1-O-(trans-sinapoyl)-beta-D-glucose = 1,2-di-O-sinapoyl beta-D-glucose + D-glucose.
alkylglycerophosphate 2-O-acetyltransferase
Involved in the biosynthesis of thrombocyte activating factor in animal tissues.
1-O-alkyl-sn-glycero-3-phosphate + acetyl-CoA = 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphate + CoA.
tartronate O-hydroxycinnamoyltransferase
hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase
4-Coumaroyl-CoA (4-hydroxycinnamoyl-CoA), caffeoyl-CoA (3,4-dihydroxycinnamoyl-CoA) and feruloyl-CoA (4-hydroxy-3-methoxycinnamoyl-CoA) can also act as donors for the enzyme from the mung bean (Vigna radiata).
(E)-sinapoyl-CoA + hydroxymalonate = (E)-sinapoyltartronate + CoA.
17-O-deacetylvindoline O-acetyltransferase
acetyl-CoA:17-O-deacetylvindoline 17-O-acetyltransferase
acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase
acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase
acetylcoenzyme A:deacetylvindoline O-acetyltransferase
acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase
Catalyzes the final step in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.
4-O-deacetylvindoline + acetyl-CoA = CoA + vindoline.
The enzyme is conserved from protists to mammals and is present in flowering plants.
In most organisms it acetylates L-lysine at position 40 of alpha-tubulin.
acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-acetyl-L-lysyl-[alpha-tubulin].
arginine and ornithine N(2)-succinyltransferase
This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine.
The five enzymes involved in this pathway are EC 2.3.1.109, EC 3.5.3.23, EC 2.6.1.81, EC 1.2.1.71 and EC 3.5.1.96.
L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine.
L-ornithine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-ornithine.
Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as donors.
Some aromatic amines can act as acceptors.
(E)-feruloyl-CoA + tyramine = CoA + H(+) + N-[(E)-feruloyl]tyramine.
The enzyme, characterized from mycobacteria, is loaded with a long-chain acyl moiety by EC 6.2.1.49 and elongates it by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8-tetramethyloctacosanoate (C32-mycocerosate).
Since the enzyme lacks a thioesterase domain, the product remains bound and requires additional enzyme(s) for removal.
Even though the enzyme can accept C6 to C20 substrates in vitro, it prefers to act on C14-C20 substrates in vivo.
3 (R)-methylmalonyl-CoA + 9 H(+) + long-chain fatty acyl-[mycocerosate synthase] + 6 NADPH = 3 CO2 + 3 CoA + 3 H2O + 6 NADP(+) + trimethylated-mycocerosoyl-[mycocerosate synthase].
4 (R)-methylmalonyl-CoA + 12 H(+) + long-chain fatty acyl-[mycocerosate synthase] + 8 NADPH = 4 CO2 + 4 CoA + 4 H2O + 8 NADP(+) + tetramethylated-mycocerosoyl-[mycocerosate synthase].
1-Aminocyclopropane-1-carboxylate can act instead of malonyl-CoA.
D-tryptophan + malonyl-CoA = CoA + H(+) + N(2)-malonyl-D-tryptophan.
anthranilate + malonyl-CoA = CoA + N-malonylanthranilate.
3,4-dichloroaniline N-malonyltransferase
3,4-dichloroaniline + malonyl-CoA = CoA + N-(3,4-dichlorophenyl)malonamate.
isoflavone-7-O-beta-glucoside 6''-O-malonyltransferase
flavone/flavonol 7-O-beta-D-glucoside malonyltransferase
The 6-position of the glucose residue of formononetin can also act as acceptor; some other 7-O-glucosides of isoflavones, flavones and flavonols can also act, but more slowly.
biochanin A 7-O-beta-D-glucoside + malonyl-CoA = biochanin A 7-O-beta-D-glucoside 6''-O-malonate + CoA.
flavonol-3-O-beta-glucoside O-malonyltransferase
a flavonol 3-O-beta-D-glucoside + malonyl-CoA = a flavonol 3-O-(6-O-malonyl-beta-D-glucoside) + CoA.
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase
tetrahydrodipicolinate N-succinyltransferase
tetrahydrodipicolinate succinyltransferase
Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants.
Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase.
(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-2-succinylamino-6-oxoheptanedioate + CoA.
The enzyme from liver, but not that from bacteria, can also catalyze N-acetylation of arylamines and N,O-acetylation of arylhydroxamates.
acetyl-CoA + an N-hydroxyarylamine = an N-acetoxyarylamine + CoA.
1-alkenylglycerophosphoethanolamine O-acyltransferase
Long-chain unsaturated acyl-CoAs are the best substrates.
1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + an acyl-CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + CoA.
Catalyzes the exchange of mycolic acid between trehalose, trehalose mycolate and trehalose bismycolate.
Trehalose 6-palmitate can also act as donor.
2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose.
Alpha-saturated dolichols are acylated more rapidly than the alpha-unsaturated analogs.
di-trans,poly-cis-dolichol + hexadecanoyl-CoA = a dolichyl hexadecanoate + CoA.
1-alkyl-2-acetylglycerol O-acyltransferase
1-hexadecyl-2-acetylglycerol acyltransferase
A number of acyl-CoAs can act as acyl donor; maximum activity is obtained with linoleoyl-CoA.
a 1-O-alkyl-2-acetyl-sn-glycerol + an acyl-CoA = a 1-O-alkyl-2-acetyl-3-acyl-sn-glycerol + CoA.
isocitrate O-dihydroxycinnamoyltransferase
Feruloyl-CoA and 4-coumaroyl-CoA can also act as donors.
(E)-caffeoyl-CoA + D-threo-isocitrate = 2-[(E)-caffeoyl]-D-threo-isocitrate(3-) + CoA.
2 benzoyl-CoA + L-ornithine = 2 CoA + 2 H(+) + N(2),N(5)-dibenzoyl-L-ornithine.
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase
Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.
a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP].
galactarate O-hydroxycinnamoyltransferase
Sinapoyl-CoA and 4-coumaroyl-CoA can also act as donors.
(E)-feruloyl-CoA + galactarate = 2-O-[(E)-feruloyl]-D-galactarate + CoA.
4-coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as donors, more slowly.
(E)-sinapoyl-CoA + D-glucarate = 2-O-[(E)-sinapoyl]-D-glucarate + CoA.
glucarolactone O-hydroxycinnamoyltransferase
(E)-sinapoyl-CoA + D-glucono-1,5-lactone = 6-O-[(E)-sinapoyl]-D-glucono-1,5-lactone + CoA.
Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors, more slowly.
4-coumaroyl-CoA + shikimate = CoA + trans-4-coumaroylshikimate.
galactolipid:galactolipid acyltransferase
Di-D-galactosyldiacylglycerol can also act as acceptor.
2 mono-beta-D-galactosyldiacylglycerol = acylmono-beta-D-galactosyldiacylglycerol + mono-beta-D-galactosylacylglycerol.
phosphatidylcholine--retinol O-acyltransferase
A key enzyme in retinoid metabolism, catalyzing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored.
Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form.
a 1,2-diacyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = a 2-acyl-sn-glycero-3-phosphocholine + an all-trans-retinyl ester + apo--[retinol-binding protein].
Acts only on substrates containing more than 14 sialosyl residues.
Catalyzes the modification of capsular polysaccharides in some strains of Escherichia coli.
[(2->8)-N-acetyl-alpha-D-neuraminosyl](n) + n acetyl-CoA = [(2->8)-O(7),N-diacetyl-alpha-D-neuraminosyl](n) + n CoA.
[(2->8)-N-acetyl-alpha-D-neuraminosyl](n) + n acetyl-CoA = [(2->8)-N,O(9)-diacetyl-alpha-D-neuraminosyl](n) + n CoA.
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups.
(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine.
putrescine N-hydroxycinnamoyltransferase
Feruloyl-CoA, cinnamoyl-CoA and sinapoyl-CoA can also act as donors, more slowly.
(E)-caffeoyl-CoA + putrescine = CoA + H(+) + N-caffeoylputrescine.
ecdysone + hexadecanoyl-CoA = CoA + ecdysone hexadecanoate.
Involved with EC 1.1.1.237 in the biosynthesis of rosmarinic acid.
Characterized from the plant Melissa officinalis L. (lemon balm).
(2R)-3-(3,4-dihydroxyphenyl)lactate + (E)-caffeoyl-CoA = (R)-rosmarinate + CoA.
galactosylacylglycerol O-acyltransferase
Transfers long-chain acyl groups to the sn-1 position of the glycerol residues.
a 2-acyl-3-O-(beta-D-galactosyl)-sn-glycerol + a fatty acyl-[ACP] = a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + holo-[ACP].
palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein.
beta-glucogallin--tetrakisgalloylglucose O-galloyltransferase
1,2,3,6-tetrakis-O-galloyl-beta-D-glucose + 1-O-galloyl-beta-D-glucose = 1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose + D-glucose + H(+).
Cinnamoyl-CoA, 4-coumaroyl-CoA and salicyloyl-CoA can act as donors, more slowly.
anthranilate + benzoyl-CoA = CoA + N-benzoylanthranilate.
Pyrrolidine and 3-pyrroline can also act as acceptors, more slowly.
(E,E)-piperoyl-CoA + piperidine = CoA + H(+) + N-[(E,E)-piperoyl]piperidine.
Not identical with EC 2.3.1.74 or EC 2.3.1.95.
(E)-cinnamoyl-CoA + 3 H(+) + 3 malonyl-CoA = (E)-pinosylvin + 4 CO2 + 4 CoA.
glycerophospholipid arachidonoyl-transferase (CoA-independent)
Catalyzes the transfer of arachidonate and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid.
The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl.
The term 'radyl' has sometimes been used to refer to such substituting groups.
Differs from EC 2.3.1.148 in not requiring CoA and in its specificity for poly-unsaturated acyl groups.
1-alkyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + 1-O-alkyl-sn-glycero-3-phosphoethanolamine = 1-O-alkyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + 1-O-alkyl-sn-glycero-3-phosphocholine.
glycerophospholipid acyltransferase (CoA-dependent)
Catalyzes the transfer of fatty acids from intact choline- or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid.
Differs from EC 2.3.1.147 in requiring CoA and not favoring the transfer of polyunsaturated acyl groups.
1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + 1-O-alkyl-sn-glycero-3-phosphoethanolamine = 1-O-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + 1-O-alkyl-sn-glycero-3-phosphocholine.
platelet-activating factor acetyltransferase
Catalyzes the transfer of the acetyl group from 1-alkyl-2-acyl-sn-glycero-3-phosphocholine (platelet-activating factor) to the sn-2 position of lyso-glycerophospholipids containing ethanolamine, choline, serine, inositol or phosphate groups at the sn-3 position as well as to sphingosine and long-chain fatty alcohols.
The organyl group can be alkyl, acyl or alk-1-enyl (sometimes also collectively referred to as 'radyl').
1-organyl-2-lyso-sn-glycero-3-phospholipid + a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-alkyl-sn-glycero-3-phosphocholine + 1-organyl-2-acetyl-sn-glycero-3-phospholipid.
At higher pH values the product, 7-O-acetylsalutaridinol, spontaneously closes the 4->5 oxide bridge by allylic elimination to form the morphine precursor thebaine.
From the opium poppy plant, Papaver somniferum.
(7S)-salutaridinol + acetyl-CoA = (7S)-O-acetylsalutaridinol + CoA.
2,3',4,6-tetrahydroxybenzophenone synthase
Involved in the biosynthesis of plant xanthones.
Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA (cf. EC 2.3.1.220).
3-hydroxybenzoyl-CoA + 2 H(+) + 3 malonyl-CoA = 2,3',4,6-tetrahydroxybenzophenone + 3 CO2 + 4 CoA.
acceptor alcohols (ROH) include methanol, ethanol and propanol.
No cofactors are required as 1-O-trans-cinnamoyl-beta-D-glucopyranose itself is an 'energy-rich' (activated) acyl-donor, comparable to CoA-thioesters.
1-O-trans-Cinnamoyl-beta-D-gentobiose can also act as the acyl donor, but with much less affinity.
1-O-(trans-cinnamoyl)-beta-D-glucose + an alcohol = an alkyl cinnamate + beta-D-glucose.
anthocyanin 5-(6'''-hydroxycinnamoyltransferase)
Isolated from the plant Gentiana triflora.
Transfers the hydroxycinnamoyl group only to the C-5 glucoside of anthocyanin.
Caffeoyl-CoA, but not malonyl-CoA, can substitute as an acyl donor.
(E)-4-coumaroyl-CoA + an anthocyanidin 3,5-di-O-beta-D-glucoside = an anthocyanidin 3-O-beta-D-glucoside 5-O-beta-D-[(6-O-(E)-4-coumaroyl)glucoside] + CoA.
3-oxopalmitoyl-CoA-CoA acetyltransferase
A peroxisomal enzyme involved in branched chain fatty acid beta-oxidation in peroxisomes.
It differs from EC 2.3.1.154 in not being active toward 3-oxopristanoyl-CoA.
acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA.
3-methyl-1-(trihydroxyphenyl)butan-1-one synthase
Also acts on isobutyryl-CoA as substrate to give phlorisobutyrophenone.
The products are intermediates in the biosynthesis of the bitter acids in hops (Humulus lupulus) and glucosides in strawberry (Fragaria X ananassa).
It is also able to generate naringenin chalcone from 4-coumaroyl-CoA.
3-methylbutanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + phlorisovalerophenone.
2-methylpropanoyl-CoA + 3 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + phlorisobutanophenone.
glucosamine-1-phosphate N-acetyltransferase
The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23.
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate.
phospholipid:diacylglycerol acyltransferase
This enzyme differs from EC 2.3.1.20 by synthesizing triacylglycerol using an acyl-CoA-independent mechanism.
The specificity of the enzyme for the acyl group in the phospholipid varies with species, e.g., the enzyme from castor bean (Ricinus communis) preferentially incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas that from the hawk's beard (Crepis palaestina) incorporates both ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups.
The enzyme from the yeast Saccharomyces cerevisiae specifically transfers acyl groups from the sn-2 position of the phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid.
a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a monoacylglycerophospholipid + a triacyl-sn-glycerol.
3 H(+) + 3 malonyl-CoA + N-methylanthraniloyl-CoA = 1,3-dihydroxy-N-methylacridone + 3 CO2 + 4 CoA + H2O.
The indole nitrogen of 16-epivellosimine interacts with its aldehyde group giving an hydroxy-substituted new ring.
Also acts on gardneral (11-methoxy-16-epivellosimine).
Generates the ajmalan skeleton, which forms part of the route to ajmaline.
16-epivellosimine + acetyl-CoA = CoA + vinorine.
This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase.
The PKS catalyzes many of the chain building reactions of EC 2.3.1.85, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
19 H(+) + holo-[lovastatin nonaketide synthase] + 9 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine = 9 CO2 + 9 CoA + dihydromonacolin L-[lovastatin nonaketide synthase] + 6 H2O + 11 NADP(+) + S-adenosyl-L-homocysteine.
taxa-4(20),11(12)-dien-5alpha-ol O-acetyltransferase
This is the third enzyme in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel), which is widely used in the treatment of carcinomas, sarcomas and melanomas.
acetyl-CoA + taxa-4(20),11-dien-5alpha-ol = CoA + taxa-4(20),11-dien-5alpha-yl acetate.
acetyl coenzyme A:10-hydroxytaxane O-acetyltransferase
Acts on a number of related taxane diterpenoids with a free 10-beta-hydroxy group.
10-deacetyltaxuyunnanin C + acetyl-CoA = CoA + taxuyunnanin C.
acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase
acyl-coenzyme A:isopenicillin N acyltransferase
isopenicillin N:acyl-CoA acyltransferase
Proceeds by a two stage mechanism via 6-aminopenicillanic acid.
H2O + isopenicillin N + phenylacetyl-CoA = CoA + H(+) + L-2-aminoadipate + penicillin G.
A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein.
It has a similar sequence to vertebrate type I fatty acid synthase.
Acetoacetyl-CoA can also act as a starter molecule.
acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+).
2alpha-hydroxytaxane 2-O-benzoyltransferase
2-debenzoyl-7,13-diacetylbaccatin III-2-O-benzoyl transferase
benzoyl-CoA:taxane 2alpha-O-benzoyltransferase
The enzyme was studied using the semisynthetic substrate 2-debenzoyl-7,13-diacetylbaccatin III.
It will not acylate the hydroxy group at 1beta, 7beta, 10beta or 13alpha of 10-deacetylbaccatin III, or at 2alpha or 5alpha of taxa-4(20),11-diene-2alpha,5alpha-diol.
10-deacetyl-2-debenzoylbaccatin III + benzoyl-CoA = 10-deacetylbaccatin III + CoA.
10-deacetylbaccatin III 10-O-acetyltransferase
The enzyme will not acylate the hydroxy group at 1beta, 7beta, 13alpha of 10-deacetylbaccatin III, or at 5alpha of taxa-4(20), 11-dien-5alpha-ol.
10-deacetylbaccatin III + acetyl-CoA = baccatin III + CoA.
dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4.
The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A.
In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[protein] + CoA.
Involved, together with EC 1.2.7.4 in the synthesis of acetyl-CoA from CO2 and H2.
acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA + methyl-Co(III)-[corrinoid Fe-S protein].
Isoliquiritigenin is the precursor of liquiritigenin, a 5-deoxyflavanone.
4-coumaroyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 3 CO2 + 4 CoA + H2O + isoliquiritigenin + NADP(+).
Acts on pelargonidin 3-O-glucoside in dahlia (Dahlia variabilis), delphinidin 3-O-glucoside, and on cyanidin 3-O-glucoside in transgenic petunia (Petunia hybrida).
an anthocyanidin 3-O-beta-D-glucoside + malonyl-CoA = an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside) + CoA.
anthocyanin 5-O-glucoside 6'''-O-malonyltransferase
Specific for the penultimate step in salvianin biosynthesis.
The enzyme also catalyzes the malonylation of shisonin to malonylshisonin [cyanidin 3-O-(6''-O-p-coumaryl-beta-D-glucoside)-5-(6'''-O-malonyl-beta-D-glucoside)].
The compounds 4'''-demalonylsalvianin, salvianin, pelargonidin 3,5-diglucoside and delphinidin 3,5-diglucoside cannot act as substrates.
malonyl-CoA + pelargonidin 3-O-(6-O-[(E)-caffeoyl]-beta-D-glucoside) 5-O-beta-D-glucoside = 4'''-demalonylsalvianin + CoA.
flavonol-3-O-triglucoside O-coumaroyltransferase
Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit, almost certainly at C-6.
4-coumaroyl-CoA + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside = a flavonol 3-O-[6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside] + CoA.
The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223.
acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA.
deacetylcephalosporin-C acetyltransferase
deacetylcephalosporin C acetyltransferase
This enzyme catalyzes the final step in the biosynthesis of cephalosporin C.
acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
propionyl-CoA C(2)-trimethyltridecanoyltransferase
Also acts on dihydroxy-5beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives.
Catalyzes the penultimate step in the formation of bile acids.
The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65.
choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA.
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CoA.
A polyketide synthase that is involved in the production of the phytoalexin aucuparin.
2-hydroxybenzoyl-CoA can also act as substrate but it leads to the derailment product 4-hydroxycoumarin (cf. EC 2.3.1.208).
This enzyme uses the same starter substrate as EC 2.3.1.151.
benzoyl-CoA + 3 H(+) + 3 malonyl-CoA = biphenyl-3,5-diol + 4 CO2 + 4 CoA.
L-2,4-diaminobutanoate acetyltransferase
Ornithine, lysine, aspartate, and alpha-, beta- and gamma-aminobutanoate cannot act as substrates.
However, acetyl-CoA can be replaced by propanoyl-CoA, although the reaction proceeds more slowly.
Forms part of the ectoine biosynthesis pathway.
acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoate + CoA + H(+).
beta-ketoacyl-[acyl-carrier-protein] synthase II
3-oxoacyl-acyl carrier protein synthase I
Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria.
While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme.
The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature.
Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures.
(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-octadecenoyl-[ACP] + CO2 + holo-[ACP].
beta-ketoacyl-[acyl-carrier-protein] synthase III
3-ketoacyl-acyl carrier protein synthase III
beta-ketoacyl (acyl carrier protein) synthase III
beta-ketoacyl-acyl carrier protein synthase III
The enzyme is responsible for initiating straight-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria.
In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses short-chain acyl-CoA thioesters (preferably acetyl-CoA) rather than acyl-[acp] as its substrate.
The enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent.
The enzymes from some organisms (e.g. the Gram-positive bacterium Streptococcus pneumoniae) can accept branched-chain acyl-CoAs in addition to acetyl-CoA (cf. EC 2.3.1.300).
acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA.
lipoyl (octanoyl)-[acyl-carrier-protein]-protein N-lipoyltransferase
octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
The first committed step in the biosynthesis of lipoyl cofactor.
The lipoyl cofactor is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein.
Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate.
The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8.
An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs).
L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein].
The substrate phosphinothricin is used as a nonselective herbicide and is a potent inhibitor of EC 6.3.1.2, a key enzyme of nitrogen metabolism in plants.
acetyl-CoA + phosphinothricin = CoA + H(+) + N-acetylphosphinothricin.
Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing.
Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signaling which, in turn, initiates the expression of particular virulence genes.
N-(3-oxohexanoyl)-[acyl-carrier-protein] and hexanoyl-[acyl-carrier-protein] are the best substrates.
The fatty-acyl substrate is derived from fatty-acid biosynthesis through acyl-[acyl-carrier-protein] rather than from fatty-acid degradation through acyl-CoA.
S-Adenosyl-L-methionine cannot be replaced by methionine, S-adenosylhomocysteine, homoserine or homoserine lactone.
a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine.
Exhibits absolute specificity for the endo/3alpha configuration found in tropine as pseudotropine (tropan-3beta-ol; see EC 2.3.1.186) is not a substrate.
Acts on a wide range of aliphatic acyl-CoA derivatives, with tigloyl-CoA and acetyl-CoA being the best substrates.
It is probably involved in the formation of the tropane alkaloid littorine, which is a precursor of hyoscyamine.
an acyl-CoA + tropine = CoA + H(+) + O-acyltropine.
Exhibits absolute specificity for the exo/3beta configuration found in pseudotropine as tropine (tropan-3alpha-ol; see EC 2.3.1.185) and nortropine are not substrates.
Acts on a wide range of aliphatic acyl-CoA derivatives, including acetyl-CoA, beta-methylcrotonyl-CoA and tigloyl-CoA.
an acyl-CoA + pseudotropine = CoA + H(+) + O-acylpseudotropine.
This is the first step in the catalysis of malonate decarboxylation and involves the exchange of an acetyl thioester residue bound to the activated acyl-carrier protein (ACP) subunit of the malonate decarboxylase complex for a malonyl thioester residue.
This enzyme forms the alpha subunit of the multienzyme complexes EC 4.1.1.88 and EC 7.2.4.4.
Can also use acetyl-CoA as a substrate but more slowly.
acetyl-[ACP] + malonate = acetate + malonyl-[ACP].
omega-hydroxypalmitate O-feruloyl transferase
hydroxycinnamoyl-CoA omega-hydroxypalmitic acid O-hydroxycinnamoyltransferase
p-Coumaroyl-CoA and sinapoyl-CoA also act as substrates.
The enzyme is widely distributed in roots of higher plants.
(E)-feruloyl-CoA + 16-hydroxyhexadecanoate = 16-feruloyloxyhexadecanoate + CoA.
This enzyme catalyzes the last step in the biosynthesis of mycothiol, the major thiol in most actinomycetes, including Mycobacterium.
The enzyme is a member of a large family of GCN5-related N-acetyltransferases (GNATs).
The enzyme has been purified from Mycobacterium tuberculosis H37Rv.
Acetyl-CoA is the preferred CoA thioester but propionyl-CoA is also a substrate.
1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol.
It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, EC 1.2.1.105, EC 1.2.1.25 and EC 1.4.1.27.
acetoin + CoA + NAD(+) = acetaldehyde + acetyl-CoA + H(+) + NADH.
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
UDP-3-O-[3-hydroxymyristoyl]-D-glucosamine N-acyltransferase
UDP-3-O-acyl-glucosamine N-acyltransferase
The enzyme catalyzes a step of lipid A biosynthesis.
LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein], but it does not an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism.
a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP].
This enzyme was purified from bovine liver mitochondria.
L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values.
glycine + phenylacetyl-CoA = CoA + H(+) + phenylacetylglycine.
The enzyme acetylates the wobble base C34 of the CAU anticodon of elongation-specific tRNA(Met).
Escherichia coli TmcA strictly discriminates elongator tRNA(Met) from tRNA(Ile), which is structurally similar and has the same anticodon loop, mainly by recognizing the C27-G43 pair in the anticodon stem.
The enzyme can use GTP in place of ATP for formation of N(4)-acetylcytidine.
acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate.
The enzyme from the soil bacterium Streptomyces sp. CL190 produces acetoacetyl-CoA to be used for mevalonate production via the mevalonate pathway.
Unlike the homologous EC 2.3.1.180 this enzyme does not accept malonyl-[acyl-carrier-protein] as a substrate.
acetyl-CoA + H(+) + malonyl-CoA = acetoacetyl-CoA + CO2 + CoA.
The enzyme is resonsible for the production of (3Z)-hex-3-en-1-yl acetate, the major volatile compound released upon mechanical wounding of the leaves of Arabidopsis thaliana.
(3Z)-hex-3-en-1-ol + acetyl-CoA = (3Z)-hex-3-en-1-yl acetate + CoA.
The enzyme is involved in volatile benzenoid and benzoic acid biosynthesis.
The enzyme from Petunia hybrida also catalyzes the formation of 2-phenylethyl benzoate from benzoyl-CoA and 2-phenylethanol.
The apparent catalytic efficiency of the enzyme from Petunia hybrida with benzoyl-CoA is almost 6-fold higher than with acetyl-CoA.
benzoyl-CoA + benzyl alcohol = benzyl benzoate + CoA.
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase
The product, dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose, is a component of the glycan chain of the of the crystalline bacterial cell surface layer protein (S-layer glycoprotein) of Aneurinibacillus thermoaerophilus.
acetyl-CoA + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose = CoA + dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactopyranose + H(+).
glycerol-3-phosphate 2-O-acyltransferase
sn-2-glycerol-3-phosphate O-acyltransferase
A membrane-associated enzyme required for suberin or cutin synthesis in plants.
Active with a wide range of acyl-CoA substrates (C16:0-C24:0).
The enzyme from some sources has much higher activity with omega-oxidized acyl-CoAs.
Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols.
an acyl-CoA + sn-glycerol 3-phosphate = a 2-acyl-sn-glycerol 3-phosphate + CoA.
very-long-chain beta-ketoacyl-CoA synthase
This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs.
Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids.
For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate, while CER6 from the same plant prefers substrates with chain length of C22 to C32.
a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA.
In the bacterium Listeria monocytogenes the enzyme takes part in a pathway for scavenging of lipoic acid.
The enzyme is bound to 2-oxo-acid dehydrogenases such as the pyruvate dehydrogenase complex, where it transfers the lipoyl moiety from lipoyl-[glycine cleavage system H] to the E2 subunits of the complexes.
(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + L-lysyl-[glycine-cleavage complex H protein].
UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase
acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate = CoA + H(+) + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate.
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase
The enzyme is involved in the biosynthesis of pseudaminic acid.
acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine = CoA + H(+) + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose.
UDP-N-acetylbacillosamine N-acetyltransferase
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase
The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species and O-linked glycosylation of certain L-serine residues in Neisseria species.
acetyl-CoA + UDP-N-acetylbacillosamine = CoA + H(+) + UDP-N,N'-diacetylbacillosamine.
octanoyl-[GcvH]:protein N-octanoyltransferase
In the bacterium Bacillus subtilis it has been shown that the enzyme catalyzes the amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N(6)-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein].
acetyl-CoA + fumigaclavine B = CoA + fumigaclavine A.
A polyketide synthase catalyzing the first committed step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa.
The enzyme was previously thought to also function as a cyclase, but the cyclization is now known to be catalyzed by EC 4.4.1.26.
3 H(+) + hexanoyl-CoA + 3 malonyl-CoA = 3,5,7-trioxododecanoyl-CoA + 3 CO2 + 3 CoA.
beta-ketodecanoyl-[acyl-carrier-protein] synthase
This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyzes the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via beta-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle.
The enzyme provides a shunt for beta-oxidation degradation intermediates into de novo fatty acid biosynthesis.
H(+) + malonyl-[ACP] + octanoyl-CoA = 3-oxodecanoyl-[ACP] + CO2 + CoA.
The enzyme, a polyketide synthase, can also accept benzoyl-CoA as substrate, which it condenses with 3 malonyl-CoA molecules to form 3,5-dihydroxybiphenyl (cf. EC 2.3.1.177).
2-hydroxybenzoyl-CoA + malonyl-CoA = 4-hydroxycoumarin + CO2 + 2 CoA.
dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
The non-activated product, 4-acetamido-4,6-dideoxy-alpha-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose = CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose + H(+).
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
The product, TDP-4-acetamido-4,6-dideoxy-D-galactose, is utilized in the biosynthesis of Enterobacterial Common Antigen (ECA).
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose + H(+).
A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyzes the formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin.
Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes, the diketide intermediate formed by this enzyme remains within the enzyme's cavity and is not released to the environment.
2 4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA = bisdemethoxycurcumin + 2 CO2 + 3 CoA.
A polyketide synthase that catalyzes the C6-C4 skeleton of phenylbutanoids in higher plants.
4-coumaroyl-CoA + H(+) + H2O + malonyl-CoA = 4-hydroxybenzalacetone + 2 CO2 + 2 CoA.
cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6'''-O-hydroxycinnamoyltransferase
Isolated from the plant Daucus carota (Afghan cultivar carrot).
In addition to 1-O-(4-hydroxycinnamoyl)-beta-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of beta-D-glucose.
1-O-(trans-4-coumaroyl)-beta-D-glucose + cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) betaine = beta-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-beta-D-glucosyl)-2-O-beta-D-xylosyl-beta-D-galactoside] + H(+).
pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4'''-malonyltransferase
Isolated from the plant Salvia splendens (scarlet sage).
4'''-demalonylsalvianin + malonyl-CoA = CoA + salvianin.
anthocyanidin 3-O-glucoside 6''-O-acyltransferase
Isolated from the plants Perilla frutescens and Gentiana triflora (clustered gentian).
Acts on a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside.
It did not act on delphinidin 3,3',7-tri-O-glucoside.
Recombinant Perilla frutescens enzyme could utilize caffeoyl-CoA but not malonyl-CoA as alternative acyl donor.
(E)-4-coumaroyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = an anthocyanidin 3-O-[6-O-(4-hydroxycinnamoyl)-beta-D-glucoside] + CoA + H(+).
A polyketide synthase from the plant Aloe arborescens (aloe).
4 H(+) + 5 malonyl-CoA = 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + 5 CoA + H2O.
A polyketide synthase from the plant Curcuma longa (turmeric).
Three isoforms exist, CURS1, CURS2 and CURS3.
While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well (see EC 2.3.1.219).
(E)-feruloyl-CoA + (E)-feruloylacetyl-CoA + H2O = CO2 + 2 CoA + curcumin.
The enzyme has been characterized from the plant Curcuma longa (turmeric).
It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.
(E)-feruloyl-CoA + H(+) + malonyl-CoA = (E)-feruloylacetyl-CoA + CO2 + CoA.
4-coumaroyl-CoA + H(+) + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO2 + CoA.
While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate (cf. EC 2.3.1.217), CURS3 can accept 4-coumaroyl-CoA equally well.
(E)-4-coumaroyl-CoA + (E)-feruloylacetyl-CoA + H2O = CO2 + 2 CoA + demethoxycurcumin.
(4-coumaroyl)acetyl-CoA + 4-coumaroyl-CoA + H2O = bisdemethoxycurcumin + CO2 + 2 CoA.
The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151).
benzoyl-CoA + 2 H(+) + 3 malonyl-CoA = 2,4,6-trihydroxybenzophenone + 3 CO2 + 4 CoA.
A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.
The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase.
6 H(+) + hexanoyl-[ACP] + 7 malonyl-CoA = 7 CO2 + 7 CoA + 2 H2O + holo-[ACP] + noranthrone.
Part of the degradation pathway for 1,2-propanediol.
phosphate + propanoyl-CoA = CoA + propanoyl phosphate.
The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174.
2,3-didehydroadipoyl-CoA + acetyl-CoA = 3-oxo-5,6-didehydrosuberyl-CoA + CoA.
acetyl-CoA-benzylalcohol acetyltransferase
The enzyme is found in flowers like Clarkia breweri, where it is important for floral scent production.
Unlike EC 2.3.1.84 this enzyme is active with alcohols that contain a benzyl ring.
acetyl-CoA + benzyl alcohol = benzyl acetate + CoA.
(E)-cinnamyl alcohol + acetyl-CoA = (E)-cinnamyl acetate + CoA.
The enzyme catalyzes the post-translational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity.
Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein].
(S)-1-pyrroline-5-carboxylate + H(+) + H2O + malonyl-CoA = (2S,5S)-5-carboxymethylproline + CO2 + CoA.
GDP-alpha-D-perosamine N-acetyltransferase
D-Perosamine is one of several dideoxy sugars found in the O-antigen component of the outer membrane lipopolysaccharides of Gram-negative bacteria.
acetyl-CoA + GDP-alpha-D-perosamine = CoA + GDP-N-acetyl-alpha-D-perosamine + H(+).
The enzyme, found in the bacterium Bradyrhizobium japonicum, does not accept isovaleryl-[acyl-carrier protein] as acyl donor (cf. EC 2.3.1.184).
3-methylbutanoyl-CoA + S-adenosyl-L-methionine = CoA + H(+) + N-isovaleryl-L-homoserine lactone + S-methyl-5'-thioadenosine.
The enzyme is found in the bacterium Rhodopseudomonas palustris, which produces N-(4-coumaroyl)-L-homoserine lactone as a quorum-sensing signal.
4-coumaroyl-CoA + S-adenosyl-L-methionine = CoA + H(+) + N-(4-coumaroyl)-L-homoserine lactone + S-methyl-5'-thioadenosine.
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex.
The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue.
Together with the PqsB subunit, the proteins catalyze the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
(2-aminobenzoyl)acetate + H(+) + octanoyl-CoA = 2-heptyl-4(1H)-quinolone + CO2 + CoA + H2O.
tRNA(Phe) {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine(37)-N}-methoxycarbonyltransferase
In some species that produce hydroxywybutosine the enzyme uses 7-[2-hydroxy-3-amino-3-(methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) as substrate.
The enzyme also has the activity of EC 2.1.1.290.
7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + CO2 + S-adenosyl-L-methionine = 2 H(+) + S-adenosyl-L-homocysteine + wybutosine(37) in tRNA(Phe).
The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape.
The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol.
It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency.
In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes.
anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate.
1,3,6,8-tetrahydroxynaphthalene synthase
Isolated from the fungus Colletotrichum lagenarium, and the bacteria Streptomyces coelicolor and Streptomyces peucetius.
It only uses malonyl-CoA, without invovement of acetyl-CoA.
5 H(+) + 5 malonyl-CoA = 5 CO2 + 5 CoA + H2O + naphthalene-1,3,6,8-tetrol.
N(6)-L-threonylcarbamoyladenine synthase
The enzyme is involved in the synthesis of N(6)-threonylcarbamoyladenosine(37) in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNA(Ile), tRNA(Thr), tRNA(Asn), tRNA(Lys), tRNA(Ser) and tRNA(Arg).
adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA.
A multi-domain polyketide synthase involved in the synthesis of tetracenomycin in the bacterium Streptomyces glaucescens.
It involves a ketosynthase complex, an acyl carrier protein, a malonyl CoA:ACP acyltransferase, and a cyclase.
A malonyl-CoA molecule is initially bound to the acyl carrier protein and decarboxylated to form an acetyl starter unit.
Additional two-carbon units are added from nine more malonyl-CoA molecules.
8 H(+) + 10 malonyl-CoA = 10 CO2 + 10 CoA + 2 H2O + tetracenomycin F2.
A multi-domain polyketide synthase involved in the synthesis of azinomycin B in the bacterium Streptomyces griseofuscus.
acetyl-CoA + 7 H(+) + 5 malonyl-CoA + 3 NADPH = 5-methyl-1-naphthoate + 5 CO2 + 6 CoA + 4 H2O + 3 NADP(+).
A multi-domain polyketide synthase involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
acetyl-CoA + 6 H(+) + 5 malonyl-CoA + 2 NADPH = 2-hydroxy-5-methyl-1-naphthoate + 5 CO2 + 6 CoA + 3 H2O + 2 NADP(+).
monacolin J acid methylbutanoate transferase
The enzyme catalyzes the ultimate reaction in the lovastatin biosynthesis pathway of the filamentous fungus Aspergillus terreus.
(S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + monacolin J carboxylate = holo-[2-methylbutanoate polyketide synthase] + lovastatin carboxylate.
(2S)-methylmalonyl-CoA:malonyl-CoA malonyltransferase (10-deoxymethynolide forming)
The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae.
The enzyme also produces narbonolide (see EC 2.3.1.240).
The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain.
Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP).
Not all active sites are used in the biosynthesis.
5 (S)-methylmalonyl-CoA + 11 H(+) + malonyl-CoA + 5 NADPH = 10-deoxymethynolide + 6 CO2 + 6 CoA + 2 H2O + 5 NADP(+).
The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae.
The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239).
6 (S)-methylmalonyl-CoA + 12 H(+) + malonyl-CoA + 5 NADPH = 7 CO2 + 7 CoA + 2 H2O + 5 NADP(+) + narbonolide.
alpha-Kdo-(2->4)-alpha-(2->6)-lipid IVA lauroyltransferase
The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.
It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule.
The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) acyl groups, giving the enzyme its previous accepted name.
However, enzymes from different species accept highly variable substrates.
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + dodecanoyl-[ACP] = dodecanoyl-(Kdo)2-lipid IVA + holo-[ACP].
a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA = an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)-lipid IVA + holo-[ACP].
(Kdo)2-lipid IVA palmitoleoyltransferase
alpha-Kdo-(2->4)-alpha-(2->6)-lipid IVA palmitoleoyltransferase
palmitoleoyl-acyl carrier protein-dependent acyltransferase
The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
(9Z)-hexadecenoyl-[ACP] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA = (9Z)-hexadecenoyl-(Kdo)2-lipid IVA + holo-[ACP].
acyl-Kdo2-lipid IVA myristoyltransferase
myristoyl-[acyl-carrier protein]:alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached at the 2-O position of the non-reducing glucosamine molecule.
The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) acyl groups, giving the enzyme its previous accepted name.
dodecanoyl-(Kdo)2-lipid IVA + tetradecanoyl-[ACP] = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + holo-[ACP].
a fatty acyl-[ACP] + an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)-lipid IVA = an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(acyl)2-lipid A + holo-[ACP].
This polyketide synthase enzyme forms the (S)-2-methylbutanoate side chain during lovastatin biosynthesis by the filamentous fungus Aspergillus terreus.
The overall reaction comprises a single condensation reaction followed by alpha-methylation, beta-ketoreduction, dehydration, and alpha,beta enoyl reduction.
3 H(+) + holo-[2-methylbutanoate polyketide synthase] + 2 malonyl-CoA + 2 NADPH + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CO2 + 2 CoA + H2O + 2 NADP(+) + S-adenosyl-L-homocysteine.
3-hydroxy-5-phosphooxypentane-2,4-dione thiolase
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
acetyl-CoA + dihydroxyacetone phosphate = 3-hydroxy-2,4-dioxopentyl phosphate + CoA.
The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the nonproteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin.
4 H(+) + 4 malonyl-CoA = (3,5-dihydroxyphenyl)acetyl-CoA + 4 CO2 + 3 CoA + H2O.
The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.
(5S)-5-amino-3-oxohexanoate + acetyl-CoA = (3S)-3-aminobutanoyl-CoA + acetoacetate.
The enzyme from the plant Arabidopsis thaliana has no activity with 4-coumaroyl-CoA (cf. EC 2.3.1.249).
2 (E)-sinapoyl-CoA + spermidine = 2 CoA + 2 H(+) + N(1),N(8)-bis[(E)-sinapoyl]-spermidine.
The enzyme from the plant Arabidopsis thaliana has no activity with sinapoyl-CoA (cf. EC 2.3.1.248).
2 (E)-4-coumaroyl-CoA + spermidine = 2 CoA + 2 H(+) + N(1),N(8)-bis(coumaroyl)-spermidine.
[Wnt protein] O-palmitoleoyl transferase
The enzyme, found in animals, modifies a specific serine residue in Wnt proteins, e.g. Ser(209) in human Wnt3a and Ser(224) in chicken WNT1.
The enzyme can accept C13 to C16 fatty acids in vitro, but only (9Z)-hexadecenoate modification is observed in vivo.
(9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + CoA.
Isolated from the bacteria Escherichia coli and Salmonella typhimurium.
The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position.
There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds.
The enzyme also acts on Kdo-(2->4)-Kdo-(2->6)-lipid IVA.
1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid A (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A.
1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = a 2-acyl-sn-glycero-3-phosphocholine + lipid IIB.
1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA (E. coli) = a 2-acyl-sn-glycero-3-phosphocholine + lipid IVB.
This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyl-tetracosanoate (C27-mycolipanoate).
Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.
3 (S)-methylmalonyl-CoA + a long-chain fatty acyl-CoA + 9 H(+) + holo-[mycolipanoate synthase] + 6 NADPH = 3 CO2 + 4 CoA + 3 H2O + long-chain mycolipanoyl-[mycolipanoate synthase] + 6 NADP(+).
The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a type III polyketide synthase.
The mechanism involves the cyclization of an activated 3,5-dioxoheptanedioate intermediate.
The enzyme exhibits broad substrate specificity, and can accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoA as the starter molecules, forming C(6)-polyoxoalkylated alpha-pyrones by sequential condensation with malonyl-CoA.
3 H(+) + 3 malonyl-CoA = 1,3,5-trihydroxybenzene + 3 CO2 + 3 CoA.
N-terminal methionine N(alpha)-acetyltransferase NatB
N-terminal acetylases (NATs) catalyze the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein.
This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing.
The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein].
N-terminal amino-acid N(alpha)-acetyltransferase NatA
N-terminal-acetylases (NATs) catalyze the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein.
This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic.
The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine.
acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein].
acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein].
acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein].
acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein].
acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein].
acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[protein].
N-terminal methionine N(alpha)-acetyltransferase NatC
The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein].
N-terminal L-serine N(alpha)-acetyltransferase NatD
NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4.
Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.
acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H4].
acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A].
N-terminal methionine N(alpha)-acetyltransferase NatE
This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis.
It may also play a role in membrane targeting and gene silencing.
NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation.
It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr.
There is some substrate overlap with EC 2.3.1.256.
In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18.
The enzyme also has the activity of EC 2.3.1.48 and autoacetylates several of its own lysine residues.
acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein].
acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein].
N-terminal methionine N(alpha)-acetyltransferase NatF
NatF is found only in higher eukaryotes, and is absent from yeast.
Unlike other Nat systems the enzyme is located in the Golgi apparatus.
It faces the cytosolic side of intracellular membranes, and specifically acetylates transmembrane proteins whose N termini face the cytosol.
NatF targets N-terminal L-methionine residues attached to Lys, Ser, Val, Leu, Gln, Ile, Tyr and Thr residues.
acetyl-CoA + N-terminal L-methionyl-[transmembrane protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane protein].
The synthesis, in the bacterium Streptomyces rimosus of the tetracycline antibiotics core skeleton requires a minimal polyketide synthase (PKS) consisting of a ketosynthase (KS), a chain length factor (CLF), and an acyl-carrier protein (ACP).
Initiation involves an amide-containing starter unit that becomes the C-2 amide that is present in the tetracycline compounds.
Following the initiation, the PKS catalyzes the iterative condensation of 8 malonyl-CoA molecules to yield the polyketide backbone of tetracycline.
Throughout the proccess, the nascent chain is attached to the OxyC acyl-carrier protein.
8 H(+) + malonamoyl-[OxyC ACP] + 8 malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC ACP] + 8 CO2 + 8 CoA.
The enzyme is part of the biosynthetic pathway of phenolphthiocerol, a lipid that serves as a virulence factor of pathogenic mycobacteria.
It catalyzes the elongation of 4-hydroxybenzoate that is loaded on its acyl-carrier domain to form (4-hydroxyphenyl)alkanoate intermediates.
The enzyme adds either 8 or 9 malonyl-CoA units, resulting in formation of 17-(4-hydroxyphenyl)heptadecanoate or 19-(4-hydroxyphenyl)nonadecanoate, respectively.
As the enzyme lacks a thioesterase domain, the product remains loaded on the acyl-carrier domain at the end of catalysis, and has to be hydrolyzed by an as-yet unknown mechanism.
4-hydroxyphenyl-[4-hydroxyphenylalkanoate synthase] + 24 H(+) + 8 malonyl-CoA + 16 NADPH = 17-(4-hydroxyphenyl)heptadecanoyl-[4-hydroxyphenylalkanoate synthase] + 8 CO2 + 8 CoA + 8 H2O + 16 NADP(+).
4-hydroxyphenyl-[4-hydroxyphenylalkanoate synthase] + 27 H(+) + 9 malonyl-CoA + 18 NADPH = 19-(4-hydroxyphenyl)nonadecanoyl-[4-hydroxyphenylalkanoate synthase] + 9 CO2 + 9 CoA + 9 H2O + 18 NADP(+).
anthraniloyl-CoA anthraniloyltransferase
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone.
The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone.
However, when EC 3.1.2.32 is present, it removes the CoA moiety from the product, forming the stable 2-aminobenzoylacetate.
anthraniloyl-CoA + H(+) + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CO2 + CoA.
The enzyme, characterized from the bacterium Clostridium sticklandii, is part of a degradation pathway of ornithine.
It is specific for acetyl-CoA and D-alanine.
acetyl-CoA + D-alanine = (2R)-2-amino-4-oxopentanoate + CoA.
The enzyme is found in some methanogenic archaea and bacteria.
In archaea it is induced under salt stress.
The product, N(6)-acetyl-beta-L-lysine, serves as a compatible solute, conferring high salt resistance on the producing organisms.
(3S)-3,6-diaminohexanoate + acetyl-CoA = (3S)-6-acetamido-3-aminohexanoate + CoA + H(+).
phosphatidylinositol dimannoside acyltransferase
The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).
a 2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + an acyl-CoA = 2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA.
a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D-myo-inositol] + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-6-acyl-mannopyranosyl-(1<->6)-D-myo-inositol] + CoA.
[ribosomal protein S18]-alanine N-acetyltransferase
The enzyme, characterized from bacteria, is specific for protein S18, a component of the 30S ribosomal subunit.
acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18].
[ribosomal protein S5]-alanine N-acetyltransferase
The enzyme, characterized from bacteria, is specific for protein S5, a component of the 30S ribosomal subunit.
It also plays a role in maturation of the 30S ribosomal subunit.
acetyl-CoA + N-terminal L-alanyl-[ribosomal protein uS5] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein uS5].
The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts.
It is only distantly related to enzymes classified as EC 2.3.1.84.
The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.
acetyl-CoA + ethanol = CoA + ethyl acetate.
This bacterial enzyme transfers a fatty acid from a membrane phospholipid to form an amide linkage with the N-terminal cysteine residue of apolipoproteins, generating a triacylated molecule.
a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein].
This bacterial enzyme catalyzes the second step in the formation of ornithine lipids.
a fatty acyl-[ACP] + a lyso-ornithine lipid = an N(2)-[(3R)-3-(acyloxy)acyl]-L-ornithine lipid + holo-[ACP].
L-glutamate-5-semialdehyde N-acetyltransferase
The enzyme, characterized from the yeast Saccharomyces cerevisiae Sigma1278b, N-acetylates L-glutamate-5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions.
Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress.
The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.
acetyl-CoA + L-glutamate 5-semialdehyde = CoA + H(+) + N-acetyl-L-glutamate 5-semialdehyde.
2-acetylphloroglucinol acetyltransferase
The enzyme from the bacterium Pseudomonas sp. YGJ3 is composed of three subunits named PhlA, PhlB and PhlC.
Production of 2,4-diacetylphloroglucinol, which has antibiotic activity, is strongly inhibited by chloride ions.
2 2-acetylphloroglucinol = 1,3,5-trihydroxybenzene + 2,4-diacetylphloroglucinol + H(+).
The enzyme, characterized from mycobacteria, is involved in the biosynthesis of methylglucose lipopolysaccharide (MGLP).
The enzyme can also act on 2-O-(alpha-D-glucopyranosyl)-D-glycerate, but with lower activity.
(2R)-2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-glycerate + octanoyl-CoA = (2R)-2-O-[6-O-octanoyl-alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-glycerate + CoA.
acyl-[acyl-carrier-protein]--phosphate acyltransferase
The enzyme, found in bacteria, catalyzes the synthesis of fatty acyl-phosphate from acyl-[acyl carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation.
While the activity is modestly enhanced by Mg(2+), the enzyme does not require a divalent cation.
a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP].
acyl phosphate:glycerol-3-phosphate acyltransferase
acyl-phosphate--glycerol-3-phosphate acyltransferase
glycerol-3-phosphate acyltransferase (acyl-phosphate transferring)
The enzyme, found in bacteria, catalyzes a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation.
an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate.
galactosamine-1-phosphate N-acetyltransferase
The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward alpha-D-glucosamine 1-phosphate (cf. EC 2.3.1.157).
In addition, that enzyme contains a second domain that catalyzes the activities of EC 2.7.7.23, EC 2.7.7.24, and EC 2.7.7.83.
acetyl-CoA + alpha-D-galactosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate.
2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase
The enzyme catalyzes the first committed step in the biosynthesis of gamma-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.
a medium-chain 3-oxoacyl-[ACP] + dihydroxyacetone phosphate = a 2-oxo-3-(phosphooxy)propyl medium-chain 3-oxoalkanoate + holo-[ACP].
mycolipenoyl-CoA--2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains.
The enzyme catalyzes two successive activities - it first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279), followed by the transfer of a mycolipenyl group to position 3.
2-O-(long-chain fatty acyl)-alpha,alpha-trehalose + a mycolipenoyl-CoA = 2-O-(long-chain fatty acyl)-3-O-mycolipenoyl-trehalose + CoA.
long-chain-acyl-CoA--trehalose acyltransferase
The enzyme catalyzes two successive activities - it first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278).
a long-chain fatty acyl-CoA + alpha,alpha-trehalose = 2-O-(long-chain fatty acyl)-alpha,alpha-trehalose + CoA.
(aminoalkyl)phosphonate N-acetyltransferase
The enzyme, characterized from the bacterium Escherichia coli, is able to acetylate a range of (aminoalkyl)phosphonic acids.
Requires a divalent metal ion for activity.
acetyl-CoA + aminomethylphosphonate = 2-N-acetamidomethylphosphonate + CoA.
(2-aminoethyl)phosphonate + acetyl-CoA = (2-acetamidoethyl)phosphonate + CoA + H(+).
This polyketide synthase enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), catalyzes the first reaction in the biosynthesis of coelimycin P1.
The enzyme is made of three proteins which together comprise six modules that contain a total of 28 domains.
An NADH-dependent terminal reductase domain at the C-terminus of the enzyme catalyzes the reductive release of the product.
12 H(+) + 6 malonyl-CoA + NADH + 5 NADPH = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CO2 + 6 CoA + 4 H2O + NAD(+) + 5 NADP(+).
phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase
The enzyme, present in certain pathogenic species of mycobacteria, catalyzes the transfer of mycocerosic acids to the two hydroxyl groups at the common lipid core of phthiocerol, phthiodiolone, and phenolphthiocerol, forming dimycocerosate esters.
The fatty acid precursors of mycocerosic acids are activated by EC 6.2.1.49, which loads them onto EC 2.3.1.111.
That enzyme extends the precursors to form mycocerosic acids that remain attached until transferred by EC 2.3.1.282.
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol = a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase].
2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid synthase].
2 a mycocerosyl-[mycocerosic acid synthase] + a phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-[mycocerosic acid synthase].
2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
This mycobacterial enzyme catalyzes the acylation of 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose at the 3' position by a (hydroxy)phthioceranoyl group during the biosynthesis of mycobacterial sulfolipids.
a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose = a 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase].
3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase
The enzyme, present in mycobacteria, catalyzes the ultimate step in the biosynthesis of mycobacterial sulfolipids.
It catalyzes two successive transfers of a (hydroxy)phthioceranyl group from two diacylated intermediates to third diacylated intermediate, generating the tetraacylated sulfolipid.
3 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-alpha,alpha-trehalose = 3,6,6'-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2'-sulfo-alpha-alpha-trehalose + 2 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose.
(13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase
(13S,14R)-1,13-dihydroxy-N-methylcanadine + acetyl-CoA = (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine + CoA.
protein acetyllysine N-acetyltransferase
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins.
Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide.
phthioceranic/hydroxyphthioceranic acid synthase
This mycobacterial polyketide enzyme produces the hepta- and octa-methylated fatty acids known as phthioceranic acids, and presumably their hydroxylated versions.
Formation of hepta- and octamethylated products depends on whether the enzyme incorporates seven or eight methylmalonyl-CoA extender units, respectively.
Formation of hydroxylated products may result from the enzyme skipping the dehydratase (DH) and enoylreductase (ER) domains during the first cycle of condensation.
8 (S)-methylmalonyl-CoA + 24 H(+) + hexadecanoyl-[(hydroxy)phthioceranic acid synthase] + 16 NADPH = C40-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 8 CO2 + 8 CoA + 8 H2O + 16 NADP(+).
7 (S)-methylmalonyl-CoA + 21 H(+) + hexadecanoyl-[(hydroxy)phthioceranic acid synthase] + 14 NADPH = C37-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 7 CO2 + 7 CoA + 7 H2O + 14 NADP(+).
2-O-sulfo trehalose long-chain-acyltransferase
This mycobacterial enzyme catalyzes the acylation of 2-O-sulfo-alpha,alpha-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
2-O-sulfo-alpha,alpha-trehalose + octadecanoyl-CoA = 2-O-sulfo-2'-O-octadecanoyl-alpha,alpha-trehalose + CoA.
2-O-sulfo-alpha,alpha-trehalose + hexadecanoyl-CoA = 2-O-sulfo-2'-O-hexadecanoyl-alpha,alpha-trehalose + CoA.
This polyketide synthase, characterized from the bacterium Streptomyces thioluteus, generates the backbone of the antibiotic aureothin.
It is composed of 4 modules that total 18 domains and is encoded by three genes.
The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 4 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.
The first module (encoded by aurA) is used twice in an iterative fashion, so that the five Claisen condensation reactions are catalyzed by only four modules.
The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric).
4 (S)-methylmalonyl-CoA + 4-nitrobenzoyl-CoA + 8 H(+) + malonyl-CoA + 4 NADPH = 5 CO2 + 6 CoA + demethylluteothin + 3 H2O + 4 NADP(+).
spectinabilin polyketide synthase system
spectinabilin polyketide synthase complex
This polyketide synthase, characterized from the bacteria Streptomyces orinoci and Streptomyces spectabilis, generates the backbone of the antibiotic spectinabilin.
It is composed of 6 modules that total 28 domains and is encoded by four genes.
The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.
The first module (encoded by norA) is used twice in an iterative fashion, so that the seven Claisen condensation reactions are catalyzed by only six modules.
6 (S)-methylmalonyl-CoA + 4-nitrobenzoyl-CoA + 12 H(+) + malonyl-CoA + 6 NADPH = 7 CO2 + 8 CoA + demethyldeoxyspectinabilin + 5 H2O + 6 NADP(+).
Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates.
Ceramide synthase 5 (CERS5) is specific for palmitoyl-CoA as the acyl donor.
It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
a sphingoid base + hexadecanoyl-CoA = an N-hexadecanoyl-sphingoid base + CoA + H(+).
The enzyme, which is a complex of five polyketide synthase proteins, is involved in the synthesis of the lipid core common to phthiocerols and phenolphthiocerols.
The first protein, PpsA, can accept either a C18 or C20 long-chain fatty acyl, or a (4-hydroxyphenyl)-C17 or C19 fatty acyl.
The substrates must first be adenylated by EC 6.2.1.59, which also loads them onto PpsA.
PpsA then extends them using a malonyl-CoA extender unit.
The PpsB protein adds the next malonyl-CoA extender unit.
The absence of a dehydratase and an enoyl reductase domains in the PpsA and PpsB modules results in the formation of the diol portion of the phthiocerol moiety.
PpsC adds a third malonyl unit (releasing a water molecule due to its dehydratase domain), PpsD adds an (R)-methylmalonyl unit, releasing a water molecule, and PpsE adds a second (R)-methylmalonyl unit, without releasing a water molecule.
The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product.
The enzyme does not contain a thioesterase domain, and release of the products requires the tesA-encoded type II thioesterase.
2 (S)-methylmalonyl-CoA + 10 H(+) + icosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 3 malonyl-CoA + 5 NADPH = C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+).
2 (S)-methylmalonyl-CoA + docosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA + 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+).
2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA + 5 NADPH = C37-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+).
2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA + 5 NADPH = C35-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+).
meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I
beta-ketoacyl-acyl carrier protein synthase KasA
The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids.
Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes.
The two enzymes share some sequence identity but function independently on separate sets of substrates.
KasA differs from KasB (EC 2.3.1.294), by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
an ultra-long-chain mono-unsaturated fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxo-ultra-long-chain mono-unsaturated fatty acyl-[ACP] + CO2 + holo-[ACP].
meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II
beta-ketoacyl-acyl carrier protein synthase KasB
KasB differs from KasA (EC 2.3.1.293), by preferring longer substrates (closer to the upper limit), which also contain two double bonds.
an ultra-long-chain di-unsaturated fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxo-ultra-long-chain di-unsaturated fatty acyl-[ACP] + CO2 + holo-[ACP].
The enzyme, found in mycobacteria, is involved in the synthesis of beta-D-mannosyl phosphomycoketides.
It is a very large polyketide synthase that contains two complete sets of FAS-like fatty acid synthase modules.
It binds an acyl-CoA with 5-9 carbons as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units.
Depending on the starter unit, the enzyme forms mycoketide-CoAs of different lengths.
5 (S)-methylmalonyl-CoA + a medium-chain fatty acyl-CoA + 32 H(+) + 5 malonyl-CoA + 22 NADPH = a mycoketide-CoA + 10 CO2 + 10 CoA + 11 H2O + 22 NADP(+).
The enzyme participates in the production of acylceramides in the stratum corneum, the outermost layer of the epidermis.
Acylceramides are crucial components of the skin permeability barrier.
a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(omega-hydroxy-ultra-long chain fatty acyl)-sphingoid base = a diacylglycerol + an N-[omega-(9Z,12Z-octadecadienoyloxy)-O-ultra-long chain fatty acyl]-sphingoid base.
a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(omega-hydroxy-ultra-long chain fatty acyl)-sphing-4-enine = a diacylglycerol + an N-(omega-(9Z,12Z-octadecadienoyloxy)-ultra-long chain fatty acyl)-sphing-4-enine.
sphingoid base N-very-long-chain fatty acyl-CoA transferase
This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates.
The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base.
The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated.
The mammalian CERS3 isoform catalyzes this activity, but has a broader substrate range and also catalyzes the activity of EC 2.3.1.298.
Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
a sphingoid base + a very long-chain fatty acyl-CoA = an N-(very-long-chain fatty acyl)-sphingoid base + CoA + H(+).
sphingoid base N-ultra-long-chain fatty acyl-CoA transferase
Ceramide synthase 3 (CERS3) is the only enzyme that is active with ultra-long-chain acyl-CoA donors (C28 or longer).
It is active in the epidermis, where its products are incorporated into acylceramides.
CERS3 also accepts (2R)-2-hydroxy fatty acids and omega-hydroxy fatty acids, and can accept very-long-chain acyl-CoA substrates (see EC 2.3.1.297).
It can use multiple sphingoid bases including sphinganine, sphingosine, phytosphingosine, and (6R)-6-hydroxysphingosine.
a sphingoid base + an ultra-long-chain fatty acyl-CoA = an N-(ultra-long-chain-acyl)-sphingoid base + CoA + H(+).
Ceramide synthase 1 (CERS1) is structurally and functionally distinctive from all other CERS enzymes, and is specific for stearoyl-CoA as the acyl donor.
a sphingoid base + octadecanoyl-CoA = an N-octadecanoyl-sphingoid base + CoA + H(+).
branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase
The enzyme is responsible for initiating branched-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system (FAS-II) in some bacteria, using molecules derived from degradation of the branched-chain amino acids L-leucine, L-valine, and L-isoleucine to form the starting molecules for elongation by the FAS-II system.
In some organisms the enzyme is also able to use acetyl-CoA, leading to production of a mix of branched-chain and straight-chain fatty acids (cf. EC 2.3.1.180).
3-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = 5-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA.
2-methylpropanoyl-CoA + H(+) + malonyl-[ACP] = 4-methyl-3-oxopentanoyl-[ACP] + CO2 + CoA.
(2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = (4S)-4-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA.
mycobacterial beta-ketoacyl-[acyl carrier protein] synthase III
mycobacterial 3-oxoacyl-[acyl carrier protein] synthase III
The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms.
The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids.
The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300.
dodecanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + CoA.
hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-hydroxycinnamoyltransferase
The enzyme participates in the biosynthesis of avenanthramides, phenolic alkaloids found mainly in oats (Avena sativa).
The enzyme from oat does not accept feruloyl-CoA as a substrate.
(E)-4-coumaroyl-CoA + 5-hydroxyanthranilate = avenanthramide A + CoA.
(E)-caffeoyl-CoA + 5-hydroxyanthranilate = avenanthramide C + CoA.
alpha-L-Rha-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-PP-Und 2(IV)-O-acetyltransferase
The enzyme, present in Salmonella strains that belong to group C2, participates in the biosynthesis of the repeat unit of O antigens produced by these strains.
acetyl-CoA + alpha-L-Rha-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate = alpha-L-2OAcRha-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CoA.
This is the key enzyme in the biosynthesis of polyhydroxyalkanoates (PHA), linear polyesters produced by bacteria as a means of carbon and energy storage.
The enzyme catalyzes the stereoselective, covalent linkage of (3R)-3-hydroxyacyl-CoA thioesters in a transesterification reaction with concomitant release of coenzyme A.
The growing polymer is attached to a conserved active site L-cysteine residue.
Three types of PHA synthases have been proposed based on their substrate specificity and enzyme structure.
Type I and type III synthases preferentially polymerize short chain hydroxyalkanoate monomers containing 3-5 carbon atoms.
The difference between these two types is that type I synthases are composed of only a single subunit (PhaC), whereas type III synthases are composed of two different subunits, PhaC and PhaE. Type II synthases are also composed of a single subunit (PhaC), but preferentially polymerize monomers containing more than 5 carbon atoms.
[(R)-3-hydroxyalkanoate](n) + a (3R)-3-hydroxyacyl-CoA = [(R)-3-hydroxyalkanoate](n+1) + CoA.
(3R)-3-hydroxybutanoyl-CoA + [(3R)-hydroxybutanoate](n) = [(3R)-hydroxybutanoate](n+1) + CoA.
acyl-[acyl-carrier protein]--UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose N-acyltransferase
The enzyme is found in bacterial species whose lipid A contains 2,3-diamino-2,3-dideoxy-D-glucopyranose.
Some enzymes, such as that from Leptospira interrogans, are highly specific for 2,3-diamino-2,3-dideoxy-D-glucopyranose, while others, such as the enzyme from Acidithiobacillus ferrooxidans, are also able to accept UDP-N-acetyl-alpha-D-glucosamine (cf. EC 2.3.1.129).
The enzymes from different organisms also differ in their specificity for the acyl donor. The enzyme from L. interrogans is highly specific for (3R)-3-hydroxydodecanoyl-[acyl-carrier protein], while that from Mesorhizobium loti functions almost equally well with 10-, 12-, and 14-carbon 3-hydroxyacyl-[acyl-carrier protein]s.
a (3R)-hydroxyacyl-[ACP] + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose = a UDP-2-acetamido-3-{[(3R)-3-hydroxyacyl]amino}-2,3-dideoxy-alpha-D-glucopyranose + H(+) + holo-[ACP].
acetyl-CoA:lysine N(6)-acetyltransferase
The enzyme catalyzes the first step of an L-lysine degradation pathway found in many fungal species.
The enzyme is specific for acetyl-CoA as the acetyl donor. cf. EC 2.3.1.32.
acetyl-CoA + L-lysine = CoA + H(+) + N(6)-acetyl-L-lysine.
6-diazo-5-oxo-L-norleucine N(alpha)-acetyltranferase
The enzyme, characterized from the bacterium Streptacidiphilus griseoplanus, participates in the biosynthesis of the tripeptide alazopeptin.
6-diazo-5-oxo-L-norleucine + acetyl-CoA = CoA + H(+) + N(alpha)-acetyl-6-diazo-5-oxo-L-norleucine.
tubulin N-terminal N-acetyltransferase NAT9
microtubule-associated N-acetyltransferase NAT9
The enzyme, characterized from the fruit fly (Drosophila melanogaster), acetylates the N-terminal of both alpha- and beta-tubulin.
The enzyme acts cotranslationally, and can't act on a preformed tubulin alpha/beta heterodimer.
acetyl-CoA + N-terminal L-methionyl-[tubulin] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-[tubulin].
1-acyl-sn-glycerol-3-phosphate acyltransferase
a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphate + holo-[ACP].
glycerol-3-phosphate acyltransferase (acyl-[acyl-carrier-protein]-transferring)
a fatty acyl-[ACP] + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + holo-[ACP].
1-acylglycerophosphoserine O-acyltransferase
Acyltransferase which mediates the conversion of lysophosphatidylserine into phosphatidylserine.
The enzyme also catalyzes the acylation of lysophosphatidylethanolamine into phosphatidylethanolamine (cf. EC 2.3.1.n7).
a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CoA.
1-acylglycerophosphoethanolamine O-acyltransferase
lysophosphatidylethanolamine acyltransferase
The enzyme mediates the conversion of lysophosphatidylethanolamine into phosphatidylethanolamine.
The enzyme also catalyzes the acylation of lysophosphatidylserine into phosphatidylserine (cf. EC 2.3.1.n6).
a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA.
sinapoyl-beta-D-glucose:anthocyanin sinapoyltransferase
The product is the most abundant anthocyanin in the plant Arabidopsis thaliana.
The enzyme likely sinapoylates other anthocyanins in the plant.
1-O-(trans-sinapoyl)-beta-D-glucose + anthocyanin A8 = anthocyanin A11 + D-glucose.
The enzyme catalyzes two reactions; the first is the transfer of a glutamyl residue from L- or D-glutamine to D-glutamate via a gamma linkage, forming gamma-glutamyl-D-glutamate, and the second is the transfer of additional glutamyl residues to the peptide, extending the polypeptide chain.
D-glutamate + D-glutamine = gamma-D-glutamyl-D-glutamate + NH4(+).
L(or D)-glutamine + (gamma-D-glutamyl)n-[peptide] = NH3 + (gamma-D-glutamyl)n+1-[peptide].
The mammlian enzyme is part of the cell antioxidant defense mechanism.
It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels.
The protein also has EC 3.4.19.13 activity.
The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide.
The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions.
an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide].
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys).
Involved in the formation of thyrotropin-releasing hormone and other biologically active peptides containing N-terminal pyroglutamyl residues.
The enzyme from papaya also acts on glutaminyl-tRNA.
N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl-[peptide] + NH4(+).
leucyl/phenylalanyl-tRNA--protein transferase
Participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue.
Once modified, the proteins are recognized by EC 3.4.21.92.
The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo.
L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu).
L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = H(+) + N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu).
an N-terminal L-alpha-aminoacyl-[protein] + L-phenylalanyl-tRNA(Phe) = an N-terminal L-phenylalanyl-L-alpha-aminoacyl-[protein] + tRNA(Phe).
H(+) + hydroxylamine + L-asparagine = beta-L-aspartylhydroxamate + NH4(+).
Requires 2-sulfanylethan-1-ol (2-mercaptoethanol) and a univalent cation.
Peptides and proteins containing an N-terminal glutamate, aspartate or cystine residue can act as acceptors.
an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg).
4-hydroxyaniline, cyclohexylamine, 1-naphthylhydrazine and similar compounds can act as acceptors.
Also catalyzes the hydrolysis of agaritine.
agaritine + acceptor = 4-hydroxymethylphenylhydrazine + gamma-L-glutamyl-acceptor.
UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase
alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase
UDP-N-acetylmuramoylpentapeptide lysine N(6)-alanyltransferase
uridine diphosphoacetylmuramoylpentapeptide lysine N(6)-alanyltransferase
L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = H(+) + tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine.
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-alanyl-tRNA(Ala) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-alanyl)-sn-glycerol + tRNA(Ala).
Two non-equivlant ribonucleoprotein subunits operate in non-concerted fashion in peptide elongation.
The small subunit forms the mRNA-binding machinery and decoding center, the large subunit performs the main ribosomal catalytic function in the peptidyl-transferase center.
peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2).
protein-glutamine gamma-glutamyltransferase
glutaminylpeptide gamma-glutamyltransferase
The gamma-carboxymide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N(6)-(5-glutamyl)lysine cross-links.
L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+).
D-phenylalanine and D-2-aminobutyrate can also act as acceptors, more slowly.
Also catalyzes some of the reactions of EC 2.3.2.2.
D-alanine + L-glutamine = gamma-L-glutamyl-D-alanine + NH4(+).
glutathione gamma-glutamylcysteinyltransferase
[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine.
This enzyme from Staphylococcus aureus catalyzes the transfer of glycine from a charged tRNA to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc (lipid II), attaching it to the N(6) of the L-lysine at position 3 of the pentapeptide.
This is the first step in the synthesis of the pentaglycine interpeptide bridge that is used in S.aureus for the cross-linking of different glycan strands to each other.
Four additional glycine residues are subsequently attached by EC 2.3.2.17 (FemA) and EC 2.3.2.18 (FemB).
beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + glycyl-tRNA(Gly) = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + tRNA(Gly).
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N(6)-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
This enzyme catalyzes the successive transfer of two glycine moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to a glycine residue previously attached by EC 2.3.2.16 (FemX) to the N(6) of the L-lysine at position 3 of the pentapeptide.
This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the cross-linking of different glycan strands to each other.
The next step is catalyzed by EC 2.3.2.18 (FemB).
This enzyme is essential for methicillin resistance.
beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + 2 glycyl-tRNA(Gly) = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-GlcNAc + 2 tRNA(Gly).
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N(6)-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
This Staphylococcus aureus enzyme catalyzes the successive transfer of two glycine moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to the three glycine molecules that were previously attached to the N(6) of the L-lysine at position 3 of the pentapeptide by EC 2.3.2.16 (FemX) and EC 2.3.2.17 (FemA).
This is the last step in the synthesis of the pentaglycine interpeptide bridge that is used in this organism for the cross-linking of different glycan strands to each other.
2 glycyl-tRNA(Gly) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-GlcNAc = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N(6)-penta-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-GlcNAc + 2 tRNA(Gly).
ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoate transferase
The enzyme attaches the side chain of the aminoglycoside antibiotics of the butirosin family.
The side chain confers resistance against several aminoglycoside-modifying enzymes.
4-(gamma-L-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI ACP] + ribostamycin = gamma-L-glutamyl-butirosin B + H(+) + holo-[BtrI ACP].
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the L-phenylalanine residue.
The protein, found in the bacterium Streptomyces noursei, also forms cyclo(L-phenylalanyl-L-phenylalanyl), cyclo(L-methionyl-L-phenylalanyl), cyclo(L-phenylalanyl-L-tyrosyl) and cyclo(L-methionyl-L-tyrosyl).
L-leucyl-tRNA(Leu) + L-phenylalanyl-tRNA(Phe) = cyclo(L-phenylalanyl-L-leucyl) + H(+) + tRNA(Leu) + tRNA(Phe).
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-tyrosine residue.
The protein, from the bacterium Mycobacterium tuberculosis, also forms small amounts of cyclo(L-tyrosyl-L-phenylalanyl).
2 L-tyrosyl-tRNA(Tyr) = cyclo(L-tyrosyl-L-tyrosyl) + 2 tRNA(Tyr).
The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-leucine residue.
The proteins from bacteria of the genus Bacillus also form small amounts of cyclo(L-phenylalanyl-L-leucyl) and cyclo(L-leucyl-L-methionyl).
2 L-leucyl-tRNA(Leu) = cyclo(L-leucyl-L-leucyl) + 2 H(+) + 2 tRNA(Leu).
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself.
In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
(E3-independent) E2 ubiquitin-conjugating enzyme
E3-independent ubiquitin-conjugating enzyme E2
The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27).
It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg(2+)-ATP and catalyzes the conjugation of ubiquitin to protein substrates, independently of E3.
This transfer has only been observed with small proteins.
In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed.
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.
N-terminal E2 ubiquitin-conjugating enzyme
N-terminal ubiquitin-conjugating enzyme E2
The enzyme ubiquitinylates the N-terminus of the acceptor protein.
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].
In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond.
In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein.
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein.
Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin.
Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase).
In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32).
The enzyme, characterized from the bacterium Pseudomonas syringae, is involved in the biosynthesis of the toxin coronatine.
holo-[CmaD peptidyl-carrier protein] + L-alloisoleucyl-[CmaA peptidyl-carrier protein] = holo-[CmaA peptidyl-carrier protein] + L-alloisoleucyl-[CmaD peptidyl-carrier protein].
The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-aspartate or L-glutamate residue.
L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu).
L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu).
The enzyme, found in bacteria, catalyzes the first step in the biosynthesis of ornithine lipids.
a (3R)-hydroxyacyl-[ACP] + L-ornithine = a lyso-ornithine lipid + H(+) + holo-[ACP].
RBR-type E3 ubiquitin transferases have two RING fingers separated by an internal motif (IBR, for In Between RING).
The enzyme interacts with the CRL (Cullin-RING ubiquitin Ligase) complexes formed by certain RING-type E3 ubiquitin transferase (see EC 2.3.2.27), which include a neddylated cullin scaffold protein and a substrate recognition module.
The RING1 domain binds an EC 2.3.2.23, and transfers the ubiquitin that is bound to it to an internal cysteine residue in the RING2 domain, followed by the transfer of the ubiquitin from RING2 to the substrate.
Once the substrate has been ubiquitinated by the RBR-type ligase, it can be ubiqutylated further using ubiquitin carried directly on E2 enzymes, in a reaction catalyzed by EC 2.3.2.27.
Activity of the RBR-type enzyme is dependent on neddylation of the cullin protein in the CRL complex.
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Some RING-type E3 ubiquitin transferase (EC 2.3.2.27) are not able to bind a substrate protein directly.
Instead, they form a complex with a cullin scaffold protein and a substrate recognition module, which is named CRL for Cullin-RING-Ligase.
The cullin protein needs to be activated by the ubiquitin-like protein NEDD8 in a process known as neddylation.
The transfer of NEDD8 from a NEDD8-specific E2 enzyme onto the cullin protein is a secondary function of the RING-type E3 ubiquitin transferase in the CRL complex.
The process requires auxiliary factors that belong to the DCN1 (defective in cullin neddylation 1) family.
S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.
RCR-type E3 ubiquitin transferases is a class of RING-type E3 ubiquitin transferase (see EC 2.3.2.27) that mediates ubiquitination of acceptor proteins via an internal cysteine residue.
The RING1 domain binds an EC 2.3.2.23 and transfers the ubiquitin that is bound to it to an internal cysteine residue on a mediator loop of the RCR-type ligase.
The ubiquitin may be transferred to a second internal cysteine before the transfer of the ubiquitin from the RCR-type ligase to the substrate.
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.
Some RING-type E3 ubiquitin transferases (EC 2.3.2.27) are not able to bind a substrate protein directly.
Instead, they form complexes with a cullin scaffold protein and a substrate recognition module, which are known as CRL (Cullin-RING-Ligase) complexes.
Like ubiquitin, the NEDD8 protein ends with two glycine residues.
EC 6.2.1.64 activates NEDD8 in an ATP-dependent reaction by forming a high-energy thioester intermediate between NEDD8 and one of its cysteine residues.
The activated NEDD8 is subsequently transferred to a cysteine residue of an E2 NEDD8-conjugating enzyme, and is eventually conjugated to a lysine residue of specific substrates in the presence of the appropriate E3 transferase (EC 2.3.2.32).
[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine.
The enzyme, found only in plants that belong to the Capsicum genus, catalyzes the last step in the biosynthesis of capsaicinoids.
The enzyme catalyzes the acylation of vanillylamine by a branched-chain fatty acid.
The exact structure of the fatty acid determines the type of capsaicinoid formed.
(6E)-8-methylnon-6-enoyl-CoA + vanillylamine = capsaicin + CoA + H(+).
RING-type E3 ubiquitin transferase (cysteine targeting)
This relatively rare subpopulation of RING-type E3 ubiquitin transferases (cf. EC 2.3.2.27), found in mammals and herpes viruses, can transfer ubiquitin to a cysteine residue in target proteins.
Additional ubiquitin molecules are polymerized on top of the initial ubiquitin molecule by formation of an isopeptide linkage with lysine(48) in the pre-attached ubiquitin.
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.
Acyl groups converted into alkyl groups on transfer
citrate oxaloacetate-lyase [(pro-3S)-CH2COO->acetyl-CoA]
The stereospecificity of this enzyme is opposite to that of EC 2.3.3.3, which is found in some anaerobes.
Citrate synthase for which the stereospecificity with respect to C2 of oxaloacetate has not been established are included in EC 2.3.3.16.
acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+).
(2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating)
dodecanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA + H(+).
citrate oxaloacetate-lyase [(pro-3R)-CH2COO(-)->acetyl-CoA]
This enzyme is inactivated by oxygen and is found in some anaerobes.
Its stereospecificity is opposite to that of EC 2.3.3.1.
3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating)
Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate.
2-oxoglutarate + dodecanoyl-CoA + H2O = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA + H(+).
The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA.
The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1.
Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate.
H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate + CoA + H(+).
(R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating)
2-ethylmalate-3-hydroxybutanedioate synthase
2-oxobutanoate + acetyl-CoA + H2O = (R)-2-ethylmalate + CoA + H(+).
3-ethylmalate glyoxylate-lyase (CoA-butanoylating)
butanoyl-CoA + glyoxylate + H2O = 3-ethylmalate + CoA + H(+).
acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating)
ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO(-)->acetyl-CoA] (ATP-dephosphorylating)
The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 and EC 6.2.1.18.
acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA.
L-malate glyoxylate-lyase (CoA-acetylating)
The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate.
Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO2.
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+).
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA-acetylating)
3-hydroxy-3-methylglutaryl CoA synthetase
3-hydroxy-3-methylglutaryl coenzyme A synthase
3-hydroxy-3-methylglutaryl-coenzyme A synthase
3-hydroxy-3-methylglutaryl coenzyme A synthetase
beta-hydroxy-beta-methylglutaryl-CoA synthase
hydroxymethylglutaryl coenzyme alpha-condensing enzyme
hydroxymethylglutaryl coenzyme A synthase
acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+).
2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating)
glyoxylate + H2O + propanoyl-CoA = 2-hydroxyglutarate + CoA + H(+).
3-propylmalate glyoxylate-lyase (CoA-pentanoylating)
glyoxylate + H2O + pentanoyl-CoA = 3-propylmalate + CoA + H(+).
3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating)
3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+).
2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating)
acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase
Belongs in the alpha-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36.
Also acts with oxaloacetate as substrate, but more slowly.
2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+).
acetyl phosphate + H(+) + sulfite = phosphate + sulfoacetaldehyde.
citrate synthase (unknown stereospecificity)
CoA-acetylating citrate oxaloacetate-lyase
This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C2 of oxaloacetate has not been established (cf. EC 2.3.3.1 and EC 2.3.3.3).
The enzyme, characterized from the plant Arabidopsis thaliana, is involved in the L-methionine side-chain elongation pathway, forming substrates for the biosynthesis of aliphatic glucosinolates.
Two forms are known - MAM1 catalyzes only only the first two rounds of methionine chain elongation, while MAM3 catalyzes all six cycles, up to formation of L-hexahomomethionine.
acetyl-CoA + an omega-(methylsulfanyl)-2-oxoalkanoate + H2O = a 2-(omega-methylsulfanyl)alkylmalate + CoA + H(+).
4-methylsulfanyl-2-oxobutanoate + acetyl-CoA + H2O = 2-(2-methylsulfanyl)ethylmalate + CoA + H(+).
2-(5-methylsulfanyl)oxopentanoate + acetyl-CoA + H2O = 2-(3-methylsulfanyl)propylmalate + CoA + H(+).
The enzyme, characterized from the bacterium Streptomyces hygroscopicus, participates in the pathway for bialaphos biosynthesis.
It requires a divalent metal ion and can also act on oxaloacetate.
3-(hydrohydroxyphosphoryl)pyruvate + acetyl-CoA + H2O = CoA + H(+) + phosphinomethylmalate.
The enzyme, isolated from several Streptomyces species, participates in the biosynthesis of certain phosphonate antibiotics.
3-phosphonopyruvate + acetyl-CoA + H2O = (R)-2-(phosphonomethyl)malate + CoA + H(+).
The enzyme, found in certain bacterial species, catalyzes a head-to-head non-decarboxylative Claisen condensation of two acyl-CoA molecules, resulting in formation of a 2-alkyl-3-oxoalkanoic acid.
It is part of a pathway for the production of olefins.
a 1,2-saturated acyl-CoA + an acyl-CoA + H2O = an (R)-2-alkyl-3-oxoalkanoate + 2 CoA + H(+).
One of the enzymes involved in a pyruvate-derived pathway for isoleucine biosynthesis that is found in some bacterial and archaeal species.
The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine.
The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate.
acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+).
This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans.
Some of these enzymes catalyze the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers.
The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin.
The description (accepted name) of the enzyme should be modified for each specific instance by substituting 'glycogen' with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.
[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.
[(1->4)-alpha-D-glucosyl](n) + [(1->6)-alpha-D-glucosyl](n+1) = [(1->4)-alpha-D-glucosyl](n+1) + [(1->6)-alpha-D-glucosyl](n).
The glucansucrases transfer a D-glusosyl residue from sucrose to a glucan chain.
They are classified based on the linkage by which they attach the transferred residue.
In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated.
This enzyme extends the glucan chain by an alpha(1->4) linkage.
[(1->4)-alpha-D-glucosyl](n) + sucrose = [(1->4)-alpha-D-glucosyl](n+1) + D-fructose.
This enzyme extends the glucan chain by an alpha(1->6) linkage.
[(1->6)-alpha-D-glucosyl](n) + sucrose = [(1->6)-alpha-D-glucosyl](n+1) + D-fructose.
In the forward reaction, arsenate may replace phosphate.
In the reverse reaction, various ketoses and L-arabinose may replace D-fructose.
phosphate + sucrose = alpha-D-glucose 1-phosphate + D-fructose.
D-maltose + phosphate = beta-D-glucose 1-phosphate + D-glucose.
Converts sucrose into inulin and D-glucose.
Some other sugars can act as D-fructosyl acceptors.
[(2->1)-beta-D-fructosyl](n) + sucrose = [(2->1)-beta-D-fructosyl](n+1) + D-glucose.
[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose.
UDP-glucose--glycogen glucosyltransferase
The description (official name) varies according to the source of the enzyme and the nature of its synthetic product.
Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin.
The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186.
A similar enzyme utilizes ADP-glucose (cf. EC 2.4.1.21).
[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP.
UDP-glucose-beta-D-glucan glucosyltransferase
UDP-glucose--beta-glucan glucosyltransferase
UDP-glucose-cellulose glucosyltransferase
A similar enzyme utilizes GDP-glucose (cf. EC 2.4.1.29).
[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP.
sucrose-uridine diphosphate glucosyltransferase
UDP-glucose-fructose glucosyltransferase
uridine diphosphoglucose-fructose glucosyltransferase
Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose.
Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP-glucose (necessary for starch biosynthesis).
an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-diphosphate + H(+) + sucrose.
D-fructose + UDP-alpha-D-glucose = H(+) + sucrose + UDP.
ADP-alpha-D-glucose + D-fructose = ADP + H(+) + sucrose.
sucrosephosphate--UDP glucosyltransferase
UDP-glucose-fructose-phosphate glucosyltransferase
The enzyme from Synechocystis sp. strain PCC 6803 is not specific for UDP-glucose as it can use ADP-glucose and, to a lesser extent, GDP-glucose as substrates.
The enzyme from rice leaves is activated by glucose 6-phosphate but that from cyanobacterial species is not.
While the reaction catalyzed by this enzyme is reversible, the enzyme usually works in concert with EC 3.1.3.24 to form sucrose, making the above reaction essentially irreversible.
The F in sucrose 6(F)-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) + sucrose 6(F)-phosphate + UDP.
alpha,alpha-trehalose-phosphate synthase (UDP-forming)
trehalosephosphate-UDP glucosyltransferase
UDP-glucose--glucose-phosphate glucosyltransferase
D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP.
chitin-UDP acetyl-glucosaminyl transferase
Converts UDP-N-acetyl-D-glucosamine into chitin and UDP.
[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP.
17beta-hydroxysteroid UDP-glucuronosyltransferase
3alpha-hydroxysteroid UDP-glucuronosyltransferase
4-hydroxybiphenyl UDP-glucuronosyltransferase
4-methylumbelliferone UDP-glucuronosyltransferase
bilirubin monoglucuronide glucuronyltransferase
bilirubin uridine diphosphoglucuronyltransferase
p-hydroxybiphenyl UDP glucuronyltransferase
p-nitrophenol UDP-glucuronosyltransferase
UDP-glucuronate-4-hydroxybiphenyl glucuronosyltransferase
UDPglucuronate beta-D-glucuronosyltransferase (acceptor-unspecific)
UDP-glucuronate-bilirubin glucuronyltransferase
UDP glucuronate-estradiol-glucuronosyltransferase
UDP glucuronate-estriol glucuronosyltransferase
uridine 5'-diphosphoglucuronyltransferase
uridine diphosphate glucuronyltransferase
uridine diphosphoglucuronate-1,2-diacylglycerol glucuronosyltransferase
uridine diphosphoglucuronate-4-hydroxybiphenyl glucuronosyltransferase
uridine diphosphoglucuronate-bilirubin glucuronoside glucuronosyltransferase
uridine diphosphoglucuronate-bilirubin glucuronosyltransferase
uridine diphosphoglucuronate-estradiol glucuronosyltransferase
uridine diphosphoglucuronate-estriol 16alpha-glucuronosyltransferase
uridine diphosphoglucuronate-estriol glucuronosyltransferase
uridine diphosphoglucuronosyltransferase
Family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines and fatty acids.
glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP.
The description (official name) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme.
The latter has frequently been termed Q-enzyme.
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Cyclomaltodextrins (Schardinger dextrins) of various sizes (6, 7, 8, etc. glucose units) are formed reversibly from starch and similar substrates.
Also disproportionates linear maltodextrins without cyclizing (cf. EC 2.4.1.25).
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.
D-cellobiose + phosphate = alpha-D-glucose 1-phosphate + D-glucose.
The description (accepted name) varies according to the source of the enzyme and the nature of its synthetic product, e.g. starch synthase, bacterial glycogen synthase.
A similar enzyme utilizes UDP-alpha-D-glucose (cf. EC 2.4.1.11).
[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+).
UDP-galactose--glucose galactosyltransferase
The enzyme is a complex of 2 proteins A and B.
In the absence of the B protein (alpha-lactalbumin) the enzyme catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine (cf. EC 2.4.1.90).
D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP.
sphing-4-enine + UDP-alpha-D-galactose = beta-D-galactosyl-(1<->1)-sphing-4-enine + H(+) + UDP.
1,4-alpha-glucan 6-alpha-glucosyltransferase
oligoglucan-branching glycosyltransferase
Transfers an alpha-D-glucosyl residue in a (1->4)-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a (1->4)-alpha-D-glucan.
An enzymic activity of this nature forms part of the mammalian and Saccharomyces cerevisiae glycogen branching system (see EC 3.2.1.33).
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.
Transfers an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Transfers a beta-D-glucosyl residue from UDP-alpha-D-glucose to a hydroxymethylcytosine residue in DNA.
Transfers a beta-D-glucosyl residue from UDP-alpha-D-glucose to a glucosylhydroxymethylcytosine residue in DNA.
GDP-glucose-beta-D-glucan glucosyltransferase
GDP-glucose-cellulose glucosyltransferase
A similar enzyme utilizes UDP-alpha-D-glucose (cf. EC 2.4.1.12).
[(1->4)-beta-D-glucosyl](n) + GDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + GDP + H(+).
beta-1,3-oligoglucan:orthophosphate glucosyltransferase II
Differs in specificity from EC 2.4.1.31 and EC 2.4.1.97.
[(1->3)-beta-D-glucosyl](n) + phosphate = [(1->3)-beta-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.
Differs in specificity from EC 2.4.1.30 and EC 2.4.1.97.
beta-D-glucosyl-(1->3)-D-glucose + phosphate = alpha-D-glucose 1-phosphate + D-glucose.
GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1.
The enzyme catalyzes the polymerization of beta-D-mannuronate residues into a mannuronan polymer, an intermediate in the biosynthesis of alginate.
It is found in brown algae and in alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.
[(1->4)-beta-D-mannuronosyl](n) + GDP-alpha-D-mannuronate = [(1->4)-beta-D-mannuronosyl](n+1) + GDP + H(+).
1,3-beta-D-glucan-UDP glucosyltransferase
1,3-beta-D-glucan--UDP glucosyltransferase
UDP-glucose-1,3-beta-D-glucan glucosyltransferase
UDP-glucose--3-beta-D-glucan glucosyltransferase
[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP.
UDP-glucose + a phenol = UDP + an aryl beta-D-glucoside.
alpha,alpha-trehalose-phosphate synthase (GDP-forming)
GDP-glucose-glucosephosphate glucosyltransferase
trehalose phosphate synthase (GDP-forming)
D-glucose 6-phosphate + GDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + GDP + H(+).
fucosylgalactoside 3-alpha-galactosyltransferase
[blood group substance] alpha-galactosyltransferase
blood-group substance alpha-dependent galactosyltransferase
blood-group substance B-dependent galactosyltransferase
fucosylglycoprotein 3-alpha-galactosyltransferase
glycoprotein-fucosylgalactoside alpha-galactosyltransferase
histo-blood substance alpha-dependent galactosyltransferase
UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D-galactosyltransferase
UDPgalactose:O-alpha-L-fucosyl(1->2)D-galactose alpha-D-galactosyltransferase
Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.
an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H(+) + UDP.
beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
glycoprotein 4-beta-galactosyltransferase
UDP-galactose--glycoprotein galactosyltransferase
Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor.
High activity is shown toward such residues in branched-chain polysaccharides when these are linked by beta-1,6 links to galactose residues; lower activity toward residues linked to galactose by beta-1,3 links.
an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
17alpha-estradiol 3-O-(beta-D-glucuronate) + UDP-N-acetyl-alpha-D-glucosamine = 17alpha-(N-acetyl-alpha-D-glucosaminyl)estradiol 3-glucosiduronate + H(+) + UDP.
glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
fucosylgalactose alpha-N-acetylgalactosaminyltransferase
fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
histo-blood group A acetylgalactosaminyltransferase
Can use a number of 2-fucosyl-galactosides as acceptors.
an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H(+) + UDP.
polypeptide N-acetylgalactosaminyltransferase
protein-UDP acetylgalactosaminyltransferase
The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP.
L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP.
polygalacturonate 4-alpha-galacturonosyltransferase
[(1->4)-alpha-D-galacturonosyl](n) + UDP-alpha-D-galacturonate = [(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP.
lipopolysaccharide 3-alpha-galactosyltransferase
lipopolysaccharide 1,3-galactosyltransferase
lipopolysaccharide galactosyltransferase
UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase
UDP-galactose:polysaccharide galactosyltransferase
uridine diphosphate galactose:lipopolysaccharide alpha-3-galactosyltransferase
uridine diphosphogalactose-lipopolysaccharide alpha,3-galactosyltransferase
Transfers D-galactosyl residues to D-glucose in the partially completed core of lipopolysaccharide (cf. EC 2.4.1.56, EC 2.4.1.58 and EC 2.4.1.73).
UDP-alpha-D-galactose + [lipopolysaccharide] = UDP + 3-alpha-D-galactosyl-[lipopolysaccharide].
1,2-diacylglycerol 3-beta-galactosyltransferase
UDPgalactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase
UDP-galactose:diacylglycerol galactosyltransferase
UDP galactose-1,2-diacylglycerol galactosyltransferase
UDP-galactose-diacylglyceride galactosyltransferase
uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase
This enzyme adds only one galactosyl group to the diacylglycerol; EC 2.4.1.241 adds a galactosyl group to the product of the above reaction.
There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3).
MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis.
a 1,2-diacyl-sn-glycerol + UDP-alpha-D-galactose = a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+) + UDP.
2-hydroxyacylsphingosine 1-beta-galactosyltransferase
This membrane-bound, endoplasmic reticulum-located enzyme catalyzes the last step in the synthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.
It has a strong preference for ceramides that contain hydroxylated fatty acids.
an N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP.
a N-(2-hydroxyacyl)sphing-4-enine + UDP-alpha-D-galactose = a 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphing-4-enine + H(+) + UDP.
The acceptor is a heteroglycan primer containing mannose, galactose and xylose.
GDP-mannose + heteroglycan = GDP + 2(or 3)-alpha-D-mannosyl-heteroglycan.
[(1->4)-beta-D-glucosyl](n) + phosphate = [(1->4)-beta-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.
Involved in the synthesis of carbohydrate units in complement (cf. EC 2.4.1.66).
(5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP.
poly(glycerol-phosphate) alpha-glucosyltransferase
UDP glucose-poly(glycerol-phosphate) alpha-glucosyltransferase
Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls.
This enzyme, isolated from Bacillus subtilis 168, adds an alpha-D-glucose to the free OH groups of the glycerol units.
The enzyme has a strong preference for UDP-alpha-glucose as the sugar donor.
It has no activity with poly(ribitol phosphate).
4-O-{[(2R)-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl undecaprenyl diphosphate + n UDP-alpha-D-glucose = 4-O-{[(2R)-2-alpha-D-glucosyl-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl undecaprenyl diphosphate + n H(+) + n UDP.
poly(ribitol-phosphate) beta-glucosyltransferase
UDP-D-glucose polyribitol phosphate glucosyl transferase
Involved in the biosynthesis of poly ribitol phosphate teichoic acids in the cell wall of the bacterium Bacillus subtilis W23.
This enzyme adds a beta-D-glucose to the hydroxyl group at the 2 position of the ribitol phosphate units.
4-O-[(D-ribitylphospho)(n)-D-ribitylphospho-(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-alpha-D-glucose = 4-O-[(2-beta-D-glucosyl-D-ribitylphospho)(n)-D-ribitylphospho-(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n H(+) + n UDP.
undecaprenyl-phosphate mannosyltransferase
di-trans,octa-cis-undecaprenyl phosphate + GDP-alpha-D-mannose = D-mannosyl di-trans,octa-cis-undecaprenyl phosphate + GDP.
lipopolysaccharide N-acetylglucosaminyltransferase
Transfers N-acetylglucosaminyl residues to a D-galactose residue in the partially completed lipopolysaccharide core (cf. EC 2.4.1.44, EC 2.4.1.58 and EC 2.4.1.73).
UDP-N-acetyl-alpha-D-glucosamine + [lipopolysaccharide] = UDP + N-acetyl-alpha-D-glucosaminyl-[lipopolysaccharide].
lipopolysaccharide glucosyltransferase I
Transfers glucosyl residues to the backbone portion of lipopolysaccharide (cf. EC 2.4.1.44, EC 2.4.1.56 and EC 2.4.1.73).
UDP-glucose + [lipopolysaccharide] = UDP + D-glucosyl-[lipopolysaccharide].
CDP-abequose:alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-PP-Und alpha-1,3-abequosyltransferase
The enzyme from Salmonella participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B and D1-D3 groups.
The enzyme is able to transfer abequose, paratose, or tyvelose, depending on the availability of the specific dideoxyhexose in a particular strain.
alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP-alpha-D-abequose = alpha-D-Abe-(1->3)-alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP + H(+).
alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP-3,6-dideoxy-alpha-D-mannose = alpha-D-Tyv-(1->3)-alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP + H(+).
The substrate is also known as gangloside GM2, the product as gangloside GM1a.
ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose = ganglioside GM1 (d18:1(4E)) + H(+) + UDP.
Glucosylates the cyanohydrins of butanone and pentan-3-one as well as that of acetone.
2-hydroxy-2-methylpropanenitrile + UDP-alpha-D-glucose = H(+) + linamarin + UDP.
alpha,alpha-trehalose + phosphate = beta-D-glucose 1-phosphate + D-glucose.
3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase
(Le(a))-dependent (alpha-3/4)-fucosyltransferase
beta-acetylglucosaminylsaccharide fucosyltransferase
blood group Lewis alpha-4-fucosyltransferase
blood-group substance Le(a)-dependent fucosyltransferase
guanosine diphosphofucose-beta-acetylglucosaminylsaccharide 4-alpha-L-fucosyltransferase
guanosine diphosphofucose-glycoprotein 4-alpha-fucosyltransferase
guanosine diphosphofucose-glycoprotein 4-alpha-L-fucosyltransferase
Lewis(Le) blood group gene-dependent alpha-(1->3/4)-L-fucosyltransferase
Lewis blood group alpha-(1->3/4)-fucosyltransferase
Normally acts on a glycoconjugate where R (see CA line) is a glycoprotein or glycolipid.
Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity toward the glucose residue in free lactose.
Fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152 which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4.
Enzymes catalyzing the 4-alpha-fucosylation of the GlcNAc in beta-D-Gal-(1->3)-beta-GlcNAc sequences (with some activity also as 3-alpha-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans.
In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-alpha- and 4-alpha-fucosyltransferase activities.
a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+).
Involved in the synthesis of carbohydrate units in complement (cf. EC 2.4.1.50).
(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-glucose = (5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP.
galactinol--raffinose galactosyltransferase
galactinol-raffinose galactosyltransferase
This enzyme also catalyzes galactosyl transfer from stachyose to raffinose (shown by labeling).
For synthesis of the substrate, see EC 2.4.1.123.
alpha-D-galactosyl-(1->3)-1D-myo-inositol + raffinose = myo-inositol + stachyose.
glycoprotein 6-alpha-L-fucosyltransferase
GDP-fucose--glycoprotein fucosyltransferase
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha(1->6)fucosyltransferase
GDP-L-fucose-glycoprotein fucosyltransferase
guanosine diphosphofucose-glycoprotein fucosyltransferase
Catalyzes a reaction similar to that of EC 2.4.1.214, but transfers the L-fucosyl group from GDP-beta-L-fucose to form an alpha-1,6-linkage rather than an alpha-1,3-linkage.
GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein].
type 1 galactoside alpha-(1,2)-fucosyltransferase
beta-galactoside alpha1->2 fucosyltransferase
blood group H alpha-2-fucosyltransferase
blood-group substance H-dependent fucosyltransferase
galactoside 2-alpha-L-fucosyltransferase
guanosine diphosphofucose-beta-D-galactosyl-alpha-2-L-fucosyltransferase
guanosine diphosphofucose-galactoside 2-L-fucosyltransferase
guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide alpha-L-fucosyltransferase
guanosine diphosphofucose-glycoprotein 2-alpha-fucosyltransferase
guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase
secretor-type beta-galactoside alpha1->2 fucosyltransferase
The enzyme acts on a glycoconjugates where the substituent group is a glycoprotein or glycosphingolipid.
The recognized moiety of the substrate is known as a type 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen.
The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates (see EC 2.4.1.344).
a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-beta-D-GlcNAc derivative + GDP + H(+).
a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + GDP + H(+).
poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase
poly(ribitol-phosphate) N-acetylglucosaminyltransferase
UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase
Involved in the biosynthesis of poly(ribitol phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus.
This enzyme adds an N-acetyl-alpha-D-glucosamine to the hydroxyl group at the 2 position of the ribitol phosphate units.
4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-N-acetyl-alpha-D-glucosamine = 4-O-([2-N-acetyl-alpha-D-glucosaminyl-1-D-ribitylphospho](n)-di{[2R]-1-glycerylphospho})-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n H(+) + n UDP.
UDP glucose-arylamine glucosyltransferase
UDP-glucose + an arylamine = UDP + an N-D-glucosylarylamine.
lipopolysaccharide glucosyltransferase II
Transfers glucosyl residues to the D-galactosyl-D-glucosyl side-chains in the partially completed core of lipopolysaccharide (cf. EC 2.4.1.44, EC 2.4.1.56 and EC 2.4.1.58).
UDP-glucose + lipopolysaccharide = UDP + alpha-D-glucosyl-lipopolysaccharide.
Involved in the biosynthesis of galactose-containing glycosaminoglycan of Dictyostelium discoideum.
UDP-alpha-D-galactose + glycosaminoglycan = UDP + D-galactosylglycosaminoglycan.
Ficaprenyl phosphate is the best substrate; other polyprenols can also act as substrates, more slowly.
UDP-glucose + polyprenyl phosphate = UDP + polyprenylphosphate-glucose.
globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase
galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase
uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase
Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity.
UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity.
Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates.
globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = globoside Gb4Cer (d18:1(4E)) + H(+) + UDP.
UDP-glucose-ceramide glucosyltransferase
Sphingosine and dihydrosphingosine can also act as acceptors; CDP-glucose can act as donor.
an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP.
UDP-glucose-apigenin beta-glucosyltransferase
UDP-glucose-luteolin beta-D-glucosyltransferase
A number of flavones, flavonones and flavonols can function as acceptors.
UDP-glucose + 5,7,3',4'-tetrahydroxyflavone = UDP + 7-O-beta-D-glucosyl-5,7,3',4'-tetrahydroxyflavone.
luteolin + UDP-alpha-D-glucose = H(+) + luteolin 7-O-beta-D-glucoside + UDP.
apigenin + UDP-alpha-D-glucose = apigenin 7-O-beta-D-glucoside + H(+) + UDP.
galactinol--sucrose galactosyltransferase
1-alpha-D-galactosyl-myo-inositol:sucrose 6-alpha-D-galactosyltransferase
4-Nitrophenyl-alpha-D-galactopyranoside can also act as donor.
Also catalyzes an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123).
alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo-inositol + raffinose.
dolichyl-phosphate beta-D-mannosyltransferase
Acts only on long-chain polyprenyl phosphates and alpha-dihydropolyprenyl phosphates, larger than C35.
a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP.
UDP-glucose-p-hydroxymandelonitrile glucosyltransferase
uridine diphosphoglucose-cyanohydrin glucosyltransferase
uridine diphosphoglucose-p-hydroxymandelonitrile glucosyltransferase
Acts on a wide range of substrates in vitro, including cyanohydrins, terpenoids, phenolics, hexanol derivatives and plant hormones, in a regiospecific manner.
Involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.14.36 and EC 1.14.14.37.
This reaction prevents the disocciation and release of toxic hydrogen cyanide.
(S)-4-hydroxymandelonitrile + UDP-alpha-D-glucose = dhurrin + H(+) + UDP.
N-acetyl-beta-D-glucosaminide beta-(1,3)-galactosyltransferase
glucosaminylgalactosylglucosylceramide 4-beta-galactosyltransferase
glucosaminylgalactosylglucosylceramide beta-galactosyltransferase
lactotriaosylceramide 4-beta-galactosyltransferase
The enzyme transfers galactose from UDP-alpha-D-galactose to the 3-position of substrates with a non-reducing terminal N-acetyl-beta-D-glucosamine (beta-GlcNAc) residue.
It can act on both glycolipids and glycoproteins, generating a structure known as the type 1 histo-blood group antigen precursor.
an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
N-acetyllactosaminide 3-alpha-galactosyltransferase
beta-D-galactosyl-N-acetylglucosaminylglycopeptide alpha-1,3-galactosyltransferase
glucosaminylglycopeptide alpha-1,3-galactosyltransferase
N-acetyllactosaminide alpha-1,3-galactosyltransferase
UDP-Gal:Gal-beta-1->4GlcNAc-R alpha-1->3-galactosyltransferase
UDP-Gal:N-acetyllactosaminide alpha-1,3-D-galactosyltransferase
UDPgalactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl-glycopeptide alpha-1,3-D-galactosyltransferase
UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase
uridine diphosphogalactose-acetyllactosamine alpha1->3-galactosyltransferase
uridine diphosphogalactose-acetyllactosamine galactosyltransferase
uridine diphosphogalactose-galactosylacetylglucosaminylgalactosyl-glucosylceramide galactosyltransferase
Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha1-acid glycoprotein and N-acetyllactosamine (beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine), but not on 2'-fucosylated-N-acetyllactosamine.
The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor.
a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
globoside alpha-N-acetylgalactosaminyltransferase
globoside Gb4Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = globoside Forssman (d18:1(4E)) + H(+) + UDP.
N-acetylglucosamine (beta1,4)galactosyltransferase
UDP-galactose-N-acetylglucosamine beta-D-galactosyltransferase
UDP-galactose--N-acetylglucosamine beta-D-galactosyltransferase
The reaction is catalyzed by a component of EC 2.4.1.22, which is identical with EC 2.4.1.38, and by an enzyme from the Golgi apparatus of animal tissues.
N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP.
UDP-glucose flavonol 3-O-glucosyltransferase
Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside.
a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-glucoside + H(+) + UDP.
(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase
ganglioside GM3 acetylgalactosaminyltransferase
UDP acetylgalactosamine-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide acetylgalactosaminyltransferase
UDP-N-acetylgalactosamine GM3 N-acetylgalactosaminyltransferase
uridine diphosphoacetylgalactosamine-acetylneuraminylgalactosylglucosylceramide acetylgalactosaminyltransferase
uridine diphosphoacetylgalactosamine-ganglioside GM3 acetylgalactosaminyltransferase
uridine diphosphoacetylgalactosamine-hematoside acetylgalactosaminyltransferase
Catalyzes the formation of the gangliosides (i.e. sialic-acid-containing glycosphingolipids) GM2, GD2 and SM2 from GM3, GD3 and SM3, respectively.
Asialo-GM3 and lactosylceramide are also substrates, but glycoproteins and oligosaccharides are not substrates.
ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GM2 (d18:1(4E)) + H(+) + UDP.
The acceptor is the asparagine residue in a sequence of the form Asn-Xaa-(Ser/Thr).
L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein] + UDP.
sn-glycerol-3-phosphate 1-galactosyltransferase
The product is hydrolyzed by a phosphatase to isofloridoside, which is involved in osmoregulation (cf. EC 2.4.1.137).
sn-glycerol 3-phosphate + UDP-alpha-D-galactose = 1-O-alpha-D-galactosyl-sn-glycerol 3-phosphate + H(+) + UDP.
Acts on a range of beta-1,3-oligoglucans, and on glucans of laminarin type.
Different from EC 2.4.1.30 and EC 2.4.1.31.
Sucrose:sucrose 1(F)-beta-D-fructosyltransferase
2 sucrose = 1(F)-beta-D-fructosylsucrose + D-glucose.
2,1-fructan:2,1-fructan 1-fructosyltransferase
1,2-beta-D-fructan:1,2-beta-D-fructan 1(F)-beta-D-fructosyltransferase
1,2-beta-D-fructan 1(F)-fructosyltransferase
1,2-beta-fructan 1(F)-fructosyltransferase
[beta-D-fructosyl-(2->1)-]m + [beta-D-fructosyl-(2->1)-]n = [beta-D-fructosyl-(2->1)-]m-1 + [beta-D-fructosyl-(2->1)-]n+1.
alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-acetylglucosaminyltransferase
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus.
Its action is required before the other N-acetylglucosaminyltransferases involved in the process (GlcNAcT-II through VI) can act.
While the natural substrate (produced by EC 3.2.1.113) is described here, the minimal substrate recognized by the enzyme is alpha-D-Man-(1->3)-beta-D-Man-R.
N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
The enzyme catalyzes the addition of N-acetyl-alpha-D-glucosamine to the core 1 structure of O-glycans forming core 2.
O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) + UDP.
O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H(+) + UDP.
Acts on other hydroxy- and dihydroxy-derivatives of 9,10-anthraquinone.
alizarin + UDP-alpha-D-glucose = 1-hydroxy-2-(beta-D-glucosyloxy)-9,10-anthraquinone + H(+) + UDP.
o-dihydroxycoumarin 7-O-glucosyltransferase
Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin.
7,8-dihydroxycoumarin + UDP-alpha-D-glucose = daphnin + H(+) + UDP.
Vitexin is a flavonoid from Cannabis sativa (hemp) and some populations of Silene alba.
UDP-alpha-D-glucose + vitexin = H(+) + UDP + vitexin 2''-O-beta-D-glucoside.
Isovitexin is a flavonoid from petals of Silene alba.
isovitexin + UDP-alpha-D-glucose = H(+) + isovitexin 2''-O-beta-D-glucoside + UDP.
dolichyl-phosphate-mannose--protein mannosyltransferase
dolichol phosphomannose-protein mannosyltransferase
dolichyl-phosphate-mannose-protein mannosyltransferase
Transfers mannosyl residues to the hydroxy of serine or threonine residues, producing cell-wall mannoproteins.
Acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C35.
a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+).
a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate + H(+).
tRNA-queuosine alpha-mannosyltransferase
This enzyme, found in higher vertebrates, modifies tRNA(Asp) at the wobble position of the anticodon loop.
GDP-alpha-D-mannose + queuosine(34) in tRNA(Asp) = GDP + H(+) + O-4''-alpha-D-mannosylqueuosine(34) in tRNA(Asp).
Sinapyl alcohol can also act as acceptor.
(E)-coniferol + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-trans-coniferol + H(+) + UDP.
alpha-1,4-glucan-protein synthase (ADP-forming)
Builds up alpha-1,4-glucan chains covalently bound to protein, thus acting as an initiator of glycogen synthesis.
ADP-glucose + protein = ADP + alpha-D-glucosyl-protein.
Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor.
trans-2-coumarate + UDP-alpha-D-glucose = H(+) + trans-beta-D-glucosyl-2-hydroxycinnamate + UDP.
UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase
UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase
uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase
The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates.
Does not catalyze glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91).
In conjunction with EC 1.14.20.4, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside.
It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself.
an anthocyanidin + H(+) + UDP-alpha-D-glucose = an anthocyanidin 3-O-beta-D-glucoside + UDP.
cyanidin + UDP-alpha-D-glucose = cyanidin 3-O-beta-D-glucoside + H(+) + UDP.
delphinidin + UDP-alpha-D-glucose = delphinidin 3-O-beta-D-glucoside + UDP.
pelargonidin + UDP-alpha-D-glucose = pelargonidin 3-O-beta-D-glucoside + UDP.
peonidin + UDP-alpha-D-glucose = peonidin 3-O-beta-D-glucoside + UDP.
cyanidin 3-O-rutinoside 5-O-glucosyltransferase
cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase
uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase
Isolated from the plants Silene dioica (red campion), Iris ensata (Japanese iris) and Iris hollandica (Dutch iris).
Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides.
The enzyme does not catalyze the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.
cyanidin 3-O-rutinoside + UDP-alpha-D-glucose = cyanidin 3-O-rutinoside 5-O-beta-D-glucoside + H(+) + UDP.
pelargonidin 3-O-rutinoside + UDP-alpha-D-glucose = H(+) + pelargonidin 3-O-rutinoside 5-O-beta-D-glucoside + UDP.
dolichyl-phosphate beta-glucosyltransferase
Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, more slowly.
a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-D-glucosyl phosphate + UDP.
UDP-glucose-zeatin 7-glucosyltransferase
uridine diphosphoglucose-zeatin 7-glucosyltransferase
Acts on a range of N(6)-substituted adenines, including zeatin and N(6)-benzylaminopurine, but not N(6)-benzyladenine.
With some acceptors, 9-beta-D-glucosides are also formed.
an N(6)-alkylaminopurine + UDP-alpha-D-glucose = an N(6)-alkylamino-7-beta-D-glucosylpurine + H(+) + UDP.
Some other hydroxycinnamates, including 4-coumarate, ferulate and caffeate, can also act as acceptors, more slowly.
Only glucose esters, not glucosides, are formed (cf. EC 2.4.1.126).
(E)-sinapate + UDP-alpha-D-glucose = 1-O-(trans-sinapoyl)-beta-D-glucose + UDP.
indole-3-acetate beta-glucosyltransferase
(indol-3-yl)acetate + UDP-alpha-D-glucose = 1-O-(indol-3-ylacetyl)-beta-D-glucose + UDP.
N-acetylgalactosaminide beta-1,3-galactosyltransferase
glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
uridine diphosphogalactose-mucin beta-(1->3)-galactosyltransferase
The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen.
The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + H(+) + UDP.
An enzyme from plants involved in the formation of raffinose and stachyose (cf. EC 2.4.1.67 and EC 2.4.1.82).
myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-(1->3)-1D-myo-inositol + H(+) + UDP.
sucrose--1,6-alpha-glucan 3(6)-alpha-glucosyltransferase
The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain.
This enzyme extends (1->6)-alpha-D-glucans by both alpha(1->3) and alpha(1->6) linkages, with one of the linkage types being dominant.
[(1->6)-alpha-D-glucosyl](n) + sucrose = (1->3)-alpha-D-glucosyl-[(1->6)-alpha-D-glucosyl](n) + D-fructose.
hydroxycinnamate 4-beta-glucosyltransferase
Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120).
(E)-4-coumarate + UDP-alpha-D-glucose = 4-O-(beta-D-glucosyl)-trans-4-coumarate + H(+) + UDP.
(+)-Neomenthol can also act as acceptor.
(-)-menthol + UDP-alpha-D-glucose = (-)-menthyl beta-D-glucoside + H(+) + UDP.
scopoletin + UDP-alpha-D-glucose = H(+) + scopolin + UDP.
bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-center, as it is in Gram-negative and some Gram-positive organisms.
The undecaprenol involved is ditrans,octacis-undecaprenol.
Involved in the synthesis of cell-wall peptidoglycan.
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+).
GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway.
ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+).
GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway.
Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway.
beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+).
xylosylprotein 4-beta-galactosyltransferase
UDP-D-galactose:D-xylose galactosyltransferase
UDP-D-galactose:xylose galactosyltransferase
uridine diphosphogalactose-xylose galactosyltransferase
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
3-O-(beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP.
galactosylxylosylprotein 3-beta-galactosyltransferase
uridine diphosphogalactose-galactosylxylose galactosyltransferase
3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP.
galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase
3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-2-O-phosphoxylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-2-O-P-Xyl]-L-seryl-[protein] + H(+) + UDP.
UDP-glucose--vanillate 1-glucosyltransferase
A number of substituted benzoic acids and, more slowly, cinnamic acids, can act as acceptors.
Vanillin is the best acceptor investigated.
3,4,5-trihydroxybenzoate + UDP-alpha-D-glucose = 1-O-galloyl-beta-D-glucose + UDP.
UDP-alpha-D-glucose + vanillate = 1-O-(4-hydroxy-3-methoxybenzoyl)-beta-D-glucose + UDP.
3,4-dihydroxybenzoate + UDP-alpha-D-glucose = 1-O-(3,4-dihydroxy-benzoyl)-beta-D-glucose + UDP.
sn-glycerol-3-phosphate 2-alpha-galactosyltransferase
The product is hydrolyzed by a phosphatase to floridoside (cf. EC 2.4.1.96).
sn-glycerol 3-phosphate + UDP-alpha-D-galactose = 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate + H(+) + UDP.
mannotetraose 2-alpha-N-acetylglucosaminyltransferase
alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-D-Man + UDP-N-acetyl-alpha-D-glucosamine = alpha-D-Man-(1->3)-[alpha-D-GlcNAc-(1->2)]-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-D-Man + H(+) + UDP.
Neither free phosphate nor maltose 1-phosphate is an intermediate in the reaction.
2 alpha-D-glucose 1-phosphate + H2O = D-maltose + 2 phosphate.
sucrose:1,6-, 1,3-alpha-D-glucan 3-alpha- and 6-alpha-D-glucosyltransferase
sucrose-1,6(3)-alpha-glucan 6(3)-alpha-glucosyltransferase
This enzyme forms both alpha(1->3) and alpha(1->6) linkages in approximately equal amounts by alternating the linkage type.
Transfers alternately an alpha-D-glucosyl residue from sucrose to the 6-position and the 3-position of the non-reducing terminal residue of an alpha-D-glucan, thus producing a glucan having alternating alpha-(1->6)- and alpha-(1->3)-linkages.
N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase
N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP.
chitobiosyldiphosphodolichol beta-mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase
GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+).
alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
alpha-1,6-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
uridine diphosphoacetylglucosamine-alpha-1,6-mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase
uridine diphosphoacetylglucosamine-alpha-D-mannoside beta1-2-acetylglucosaminyltransferase
uridine diphosphoacetylglucosamine-mannoside alpha1->6-acetylglucosaminyltransferase
Its activity initiates the synthesis of the second antenna of di-antennary complex N-glycans.
While the natural substrate (produced by EC 3.2.1.114) is described here, the minimal substrate recognized by the enzyme is alpha-D-Man-(1->6)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)]-beta-D-Man-R.
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase III
The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus.
The residue added by the enzyme at position 4 of the beta-linked mannose of the trimannosyl core of N-glycans is known as a bisecting GlcNAc.
Unlike GlcNAc residues added to other positions, it is not extended or modified.
In addition, its presence prevents the action of other branching enzymes involved in the process such as GlcNAc-T IV (EC 2.4.1.145) and GlcNAc-T V (EC 2.4.1.155), and thus increased activity of GlcNAc-T III leads to a decrease in highly branched N-glycan structures.
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
alpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferase
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV
uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase IV
By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
The enzyme catalyzes the addition of N-acetyl-alpha-D-glucosamine to the core 2 structure of O-glycans.
3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->3)-[beta-D-GlcNAc-(1->6)]-alpha-D-GalNAc}-L-seryl-[protein] + H(+) + UDP.
3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->3)-[beta-D-GlcNAc-(1->6)]-alpha-D-GalNAc}-L-threonyl-[protein] + H(+) + UDP.
acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
The product of the enzyme is known as core 3, one of the eight core structures of mucin-type O-glycans.
O-Linked glycans are polysaccharides or oligosaccharides that are linked to a protein via the oxygen atom in the side chain of an L-serine or L-threonine residue.
3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP.
3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP.
acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV
3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP.
3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP.
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase
poly-N-acetyllactosamine extension enzyme
Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on glycoproteins, glycolipids, and oligosaccharides.
a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase
I-branching beta1,6-N-acetylglucosaminyltransferase
The enzyme acts on poly-N-acetyllactosamine [glycan chains of beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine units connected by beta(1,3) linkages] attached to proteins or lipids.
It transfers a GlcNAc residue by beta(1,6) linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-glucosaminyl-(1->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase
GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase
guanosine diphosphofucose-glucoside alpha-1->3-fucosyltransferase
Lewis-negative alpha-3-fucosyltransferase
Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid.
This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+).
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase
dolichyl-phosphate acetylglucosaminyltransferase
dolichyl-phosphate alpha-N-acetylglucosaminyltransferase
The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism.
The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15).
a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = a dolichyl N-acetyl-alpha-D-glucosaminyl phosphate + UDP.
alpha-1,6-mannosyl-glycoprotein 6-beta-N-acetylglucosaminyltransferase
alpha-1,3(6)-mannosylglycoprotein beta-1,6-N-acetylglucosaminyltransferase
alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase
UDP-N-acetylglucosamine:alpha-mannoside-beta1,6 N-acetylglucosaminyltransferase
uridine diphosphoacetylglucosamine-alpha-mannoside beta1->6-acetylglucosaminyltransferase
It catalyzes the addition of N-acetylglucosamine in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes.
N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
indolylacetyl-myo-inositol galactosyltransferase
indol-3-ylacetyl-myo-inositol galactoside synthase
uridine diphosphogalactose-indolylacetylinositol galactosyltransferase
indole-3-acetyl-1D-myo-inositol + UDP-alpha-D-galactose = 5-O-(indol-3-ylacetyl)-myo-inositol D-galactoside + H(+) + UDP.
13-hydroxydocosanoate 13-beta-glucosyltransferase
13-glucosyloxydocosanoate 2'-beta-glucosyltransferase
UDP-glucose-13-hydroxydocosanoate glucosyltransferase
13-beta-D-Glucosyloxydocosanoate can also act as acceptor, leading to the formation by Candida bogoriensis of the extracellular glycolipid, hydroxydocosanoate sophoroside diacetate.
13-hydroxydocosanoate + UDP-alpha-D-glucose = 13-(beta-D-glucosyloxy)docosanoate + H(+) + UDP.
flavonol-3-O-glucoside L-rhamnosyltransferase
uridine diphosphorhamnose-flavonol 3-O-glucoside rhamnosyltransferase
A configuration-inverting rhamnosyltransferase that converts flavonol 3-O-glucosides to 3-O-rutinosides.
Also acts, more slowly, on rutin, quercetin 3-O-galactoside and flavonol 3-O-rhamnosides.
a flavonol 3-O-beta-D-glucoside + UDP-beta-L-rhamnose = a flavonol 3-O-[alpha-L-rhamnosyl-(1->6)-beta-D-glucoside] + H(+) + UDP.
pyridoxine 5'-O-beta-D-glucosyltransferase
UDP-glucose-pyridoxine glucosyltransferase
4'-deoxypyridoxine and pyridoxamine can also act as acceptors, more slowly.
pyridoxine + UDP-alpha-D-glucose = 5'-O-beta-D-glucosylpyridoxine + H(+) + UDP.
oligosaccharide 4-alpha-D-glucosyltransferase
The enzyme acts on amylose, amylopectin, glycogen and maltooligosaccharides.
No detectable free glucose is formed, indicating the enzyme does not act as a hydrolase.
The enzyme from the bacterium Cellvibrio japonicus has the highest activity with maltotriose as a donor, and also accepts maltose, while the enzyme from amoeba does not accept maltose.
Oligosaccharides with 1->6 linkages cannot function as donors, but can act as acceptors.
Unlike EC 2.4.1.25, this enzyme can transfer only a single glucosyl residue.
Transfers the non-reducing terminal alpha-D-glucose residue from a (1->4)-alpha-D-glucan to the 4-position of a free glucose or of a glucosyl residue at the non-reducing terminus of a (1->4)-alpha-D-glucan, thus bringing about the rearrangement of oligosaccharides.
alpha-D-aldosyl(1) beta-D-fructoside + D-aldose(2) = D-aldose(1) + alpha-D-aldosyl(2) beta-D-fructoside.
N-acetylneuraminylgalactosylglucosylceramide beta-1,4-N-acetylgalactosaminyltransferase
Only substances containing sialic acid residues can act as acceptors; bovine fetuin is the best acceptor tested.
ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = beta-D-GalNAc-(1->4)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer + H(+) + UDP.
raffinose--raffinose alpha-galactosyltransferase
The 3(F) position of raffinose can also act as galactosyl acceptor.
Involved in the accumulation of the tetrasaccharides lychnose and isolychnose in the leaves of Cerastium arvense and other plants of the family Caryophyllaceae during late autumn.
2 raffinose = 1(F)-alpha-D-galactosylraffinose + sucrose.
sucrose 6(F)-alpha-galactosyltransferase
Involved in the synthesis of the trisaccharide planteose and higher analogs in the seeds of Plantago and Sesamum species.
sucrose + UDP-alpha-D-galactose = 6(F)-alpha-D-galactosylsucrose + H(+) + UDP.
In association with EC 2.4.2.39, brings about the synthesis of xyloglucan.
Concurrent transfers of glucose and xylose are essential for this synthesis.
Transfers a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-(1->4)-D-glucosyl-D-glucose linkage.
The 4'-methoxy isoflavones biochanin A and formononetin and, more slowly, the 4'-hydroxy isoflavones genistein and daidzein, can act as acceptors.
The enzyme does not act on isoflavanones, flavones, flavanones, flavanols or coumarins.
a 7-hydroxyisoflavone + UDP-alpha-D-glucose = a 7-hydroxyisoflavone 7-O-beta-D-glucoside + H(+) + UDP.
formononetin + UDP-alpha-D-glucose = ononin + UDP.
biochanin A + UDP-alpha-D-glucose = biochanin A 7-O-beta-D-glucoside + H(+) + UDP.
daidzein + UDP-alpha-D-glucose = daidzein 7-O-beta-D-glucoside + UDP.
genistein + UDP-alpha-D-glucose = genistein 7-O-beta-D-glucoside + H(+) + UDP.
methyl-ONN-azoxymethanol beta-D-glucosyltransferase
Brings about the biosynthesis of the toxic substance cycasin in the leaves of Japanese cycad, Cycas revoluta.
methylazoxymethanol + UDP-alpha-D-glucose = cycasin + H(+) + UDP.
salicyl-alcohol beta-D-glucosyltransferase
salicyl alcohol + UDP-alpha-D-glucose = H(+) + salicin + UDP.
Not identical with EC 2.4.1.192 or EC 2.4.1.193.
a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside + H(+) + UDP.
glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase
glucuronylgalactosylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase
uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I
Involved in the biosynthesis of chondroitin sulfate.
Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase
glucuronyl-N-acetylgalactosaminylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase
UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-beta-D-galactosaminylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase
uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II
The human form of this enzyme is a bifunctional glycosyltransferase, which also has the EC 2.4.1.226 activity required for the synthesis of the chondroitin sulfate disaccharide repeats.
Similar chondroitin synthase 'copolymerases' can be found in Pasteurella multocida and Escherichia coli.
3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
Acts on the plant hormone gibberellin GA3 and related compounds.
gibberellin A3 + UDP-alpha-D-glucose = gibberellin A3 O-beta-D-glucoside + H(+) + UDP.
4-coumarate, 2-coumarate, benzoate, feruloate and caffeate can also act as acceptors, more slowly.
Involved in the biosynthesis of chlorogenic acid in the root of the sweet potato.
(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-beta-D-glucose + UDP.
hydroxymandelonitrile glucosyltransferase
3,4-Dihydroxymandelonitrile can also act as acceptor.
4-hydroxymandelonitrile + UDP-alpha-D-glucose = H(+) + taxiphyllin + UDP.
lactosylceramide beta-1,3-galactosyltransferase
R may be an oligosaccharide or a glycolipid.
Lactose can also act as acceptor, more slowly.
Involved in the elongation of oligosaccharide chains, especially in glycolipids.
a beta-D-galactosyl-(1->4)-beta-D-glucosyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosaminyl derivative + H(+) + UDP.
lipopolysaccharide N-acetylmannosaminouronosyltransferase
Involved in the biosynthesis of common antigen in Enterobacteriaceae.
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-mannosaminouronate = beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
hydroxyanthraquinone glucosyltransferase
A range of anthraquinones and some flavones can act as acceptors; best substrates are emodin, anthrapurpurin, quinizarin, 2,6-dihydroxyanthraquinone and 1,8-dihydroxyanthraquinone.
UDP-glucose + an hydroxyanthraquinone = UDP + a glucosyloxyanthraquinone.
Involved with EC 2.3.1.129 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram negative bacteria.
a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP.
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP.
A glucan primer is needed to begin the reaction, which brings about elongation of the glucan chains.
[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-alpha-D-glucosyl](n+1) + H(+) + UDP.
galactolipid-galactolipid galactosyltransferase
The enzyme converts monogalactosyldiacylglycerol to digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol.
All residues are connected by beta linkages.
The activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants, which is performed by EC 2.4.1.46 and EC 2.4.1.241.
Note that the beta,beta-digalactosyldiacylglycerol formed by this enzyme is different from the more common alpha,beta-digalactosyldiacylglycerol formed by EC 2.4.1.241.
The enzyme provides an important mechanism for the stabilization of the chloroplast membranes during freezing and drought stress.
2 a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[beta-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol.
Naringenin and hesperetin can act as acceptors.
UDP-glucose + a flavanone = UDP + a flavanone 7-O-beta-D-glucoside.
(2S)-naringenin + UDP-alpha-D-glucose = (2S)-naringenin 7-O-beta-D-glucoside + H(+) + UDP.
(2S)-hesperetin + UDP-alpha-D-glucose = (2S)-hesperetin 7-O-beta-D-glucoside + H(+) + UDP.
The first reaction of this enzyme is to catalyze its own glucosylation, normally at a specific Tyr of the protein if this group is free; when the Tyr is replaced by Thr or Phe, the enzyme's self-glucosylation activity is lost but its intermolecular transglucosylation ability remains.
It continues to glucosylate an existing glucosyl group until a length of about 5-13 residues has been formed.
Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11.
Not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added).
It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose.
Similarly it is not highly specific for the acceptor, using water (i.e. hydrolyzing UDP-glucose) among others.
Various forms of the enzyme exist, and different forms predominate in different organs.
Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa.
L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP.
[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+) + UDP.
N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase
Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + UDP.
N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-glucose = beta-D-glucosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
luteolin + UDP-alpha-D-glucuronate = H(+) + luteolin 7-O-beta-D-glucuronide + UDP.
luteolin-7-O-glucuronide 2''-O-glucuronosyltransferase
uridine diphosphoglucuronate-luteolin 7-O-glucuronide glucuronosyltransferase
The enzyme participates in the biosynthesis of luteolin triglucuronide, the major flavone found in the photosynthetically-active mesophyll of the primary leaves of Secale cereale (rye).
luteolin 7-O-beta-D-glucuronide + UDP-alpha-D-glucuronate = H(+) + luteolin 7-O-[(beta-D-glucuronosyl)-(1->2)-(beta-D-glucuronide)] + UDP.
luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase
luteolin 7-O-[(beta-D-glucuronosyl)-(1->2)-(beta-D-glucuronide)] + UDP-alpha-D-glucuronate = H(+) + luteolin 7-O-[(beta-D-glucuronosyl)-(1->2)-(beta-D-glucuronide)] 4'-O-beta-D-glucuronide + UDP.
Some other sapogenins can act as glucosyl acceptors.
Involved in the biosynthesis of plant saponins.
Not identical with EC 2.4.1.173 or EC 2.4.1.193.
nuatigenin + UDP-alpha-D-glucose = H(+) + nuatigenin 3-beta-D-glucopyranoside + UDP.
Not identical with EC 2.4.1.173 or EC 2.4.1.192.
(25S)-5beta-spirostan-3beta-ol + UDP-alpha-D-glucose = (25S)-5beta-spirostan-3beta-yl beta-D-glucoside + H(+) + UDP.
4-hydroxybenzoate 4-O-beta-D-glucosyltransferase
4-hydroxybenzoate + UDP-alpha-D-glucose = 4-(beta-D-glucosyloxy)benzoate + H(+) + UDP.
N-hydroxythioamide S-beta-glucosyltransferase
desulfoglucosinolate-uridine diphosphate glucosyltransferase
thiohydroximate beta-D-glucosyltransferase
uridine diphosphoglucose-thiohydroximate glucosyltransferase
The enzyme specifically glucosylates the thiohydroximate functional group.
It is involved in the biosynthesis of glucosinolates in cruciferous plants, and acts on aliphatic, aromatic, and indolic substrates.
(Z)-2-phenyl-1-thioacetohydroximate + UDP-alpha-D-glucose = (Z)-desulfoglucotropeolin + UDP.
a (Z)-omega-(methylsulfanyl)alkyl-thiohydroximate + UDP-alpha-D-glucose = an aliphatic (Z)-desulfo-glucosinolate + UDP.
(Z)-2-(indol-3-yl)-1-thioacetohydroximate + UDP-alpha-D-glucose = (Z)-indolylmethyl desulfoglucosinolate + UDP.
nicotinate + UDP-alpha-D-glucose = N-(beta-D-glucosyl)nicotinate + UDP.
high-mannose-oligosaccharide beta-1,4-N-acetylglucosaminyltransferase
The activity of the intersecting mannose residue as acceptor is dependent on two other mannose residues attached by alpha-1,3 and alpha-1,6 links.
Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked alpha-(1->6) to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum.
phosphatidylinositol N-acetylglucosaminyltransferase
UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase
uridine diphosphoacetylglucosamine alpha1,6-acetyl-D-glucosaminyltransferase
Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes.
In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P).
In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H(+) + UDP.
beta-mannosylphosphodecaprenol--mannooligosaccharide 6-mannosyltransferase
Involved in the formation of mannooligosaccharides in the membrane of Mycobacterium smegmatis.
beta-D-mannosylphosphodecaprenol + (1->6)-alpha-D-mannosyloligosaccharide = decaprenol phosphate + (1->6)-alpha-D-mannosyl-(1->6)-alpha-D-mannosyl-oligosaccharide.
alpha-1,6-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI
uridine diphosphoacetylglucosamine-glycopeptide beta-1->4-acetylglucosaminyltransferase VI
The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus.
It transfers GlcNAc in beta1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by beta linkages.
No homologous enzyme appears to exist in mammals.
N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase
The enzyme is involved in the detoxification of the benzoxazinoids DIBOA (2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one) and DIMBOA (2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) which are stored as the respective non-toxic glucosides in the vacuoles in some plants, most commonly from the family of Poaceae (grasses).
Benzoxazinoids are known to exhibit antimicrobial, antifeedant, and antiinsecticidal effects and are involved in the interaction of plants with other plants, insects, or microorganisms.
DIMBOA + UDP-alpha-D-glucose = DIMBOA beta-D-glucoside + H(+) + UDP.
DIBOA + UDP-alpha-D-glucose = DIBOA beta-D-glucoside + H(+) + UDP.
trans-zeatin O-beta-D-glucosyltransferase
uridine diphosphoglucose-zeatin O-glucosyltransferase
Unlike EC 2.4.1.215, UDP-xylose can also act as donor (cf. EC 2.4.2.40).
trans-zeatin + UDP-alpha-D-glucose = H(+) + O-beta-D-glucosyl-trans-zeatin + UDP.
Galactogen from Helix pomatia is the most effective acceptor.
UDP-alpha-D-galactose + galactogen = UDP + (1->6)-beta-D-galactosylgalactogen.
lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-glucosamine = a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP.
Does not use cello-oligosaccharides as either donor or acceptor.
breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.
diglucosyl diacylglycerol synthase (1,2-linking)
monoglucosyl diacylglycerol (1->2) glucosyltransferase
a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol + UDP-alpha-D-glucose = 1,2-diacyl-3-O-[alpha-D-glucosyl-(1-> 2)-alpha-D-glucosyl]-sn-glycerol + H(+) + UDP.
cis-Caffeic acid also serves as a glucosyl acceptor with the enzyme from Sphagnum fallax kinggr.
The corresponding trans-isomers are not substrates.
cis-4-coumarate + UDP-alpha-D-glucose = 4'-O-beta-D-glucosyl-cis-4-coumarate + H(+) + UDP.
The enzyme purified from navel orange albedo tissue also acts on the related tetranortriterpenoid nomilin.
H2O + limonin + UDP-alpha-D-glucose = glucosyl-limonin + 2 H(+) + UDP.
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
Reaction also occurs with beta-D-galactopyranosyl-(1->3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.
beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine.
Adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc.
Highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA.
[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP.
N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP.
Acts with EC 3.1.3.69 to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.
ADP-alpha-D-glucose + sn-glycerol 3-phosphate = 2-O-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + ADP + H(+).
glycoprotein 3-alpha-L-fucosyltransferase
GDP-fucose:beta-N-acetylglucosamine (Fuc to (Fuc-alpha1->6-GlcNAc)-Asn-peptide) alpha1->3-fucosyltransferase
GDP-L-Fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,3-fucosyltransferase
The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue.
This enzyme catalyzes a reaction similar to that of EC 2.4.1.68, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage.
The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[(1->4)-alpha-L-Fuc]-beta-D-GlcNAc}-L-asparaginyl-[protein].
The enzyme from maize can use cis-zeatin and UDPglucose as substrates, but not cis-ribosylzeatin, trans-zeatin or trans-ribosylzeatin.
Unlike EC 2.4.1.203 UDP-xylose cannot act as a donor.
cis-zeatin + UDP-alpha-D-glucose = H(+) + O-beta-D-glucosyl-cis-zeatin + UDP.
trehalose 6-phosphate:phosphate beta-D-glucosyltransferase
The enzyme from Lactococcus lactis is specific for trehalose 6-phosphate.
Differs from EC 2.4.1.64 in that trehalose is not a substrate.
alpha,alpha-trehalose 6-phosphate + phosphate = beta-D-glucose 1-phosphate + D-glucose 6-phosphate.
The enzyme is absolutely specific for GDP-mannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration.
In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate.
(2R)-3-phosphoglycerate + GDP-alpha-D-mannose = 2-O-(alpha-D-mannosyl)-3-phosphoglycerate + GDP + H(+).
Hydroquinone is the most effective acceptor, but over 40 phenolic compounds are also glucosylated, but at lower rates.
hydroquinone + UDP-alpha-D-glucose = H(+) + hydroquinone O-beta-D-glucopyranoside + UDP.
UDPG:vomilenine 21beta-D-glucosyltransferase
The indole alkaloid raucaffricine accumulates during the culture of Rauvolfia cell suspensions.
UDP-alpha-D-glucose + vomilenine = H(+) + raucaffricine + UDP.
Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole.
After enzymic or chemical hydrolysis, indican forms indoxyl, which, in turn, is converted in the presence of oxygen to the dye indigo.
indoxyl + UDP-alpha-D-glucose = H(+) + indican + UDP.
The enzyme, found in animals and plants, is involved in the biosynthesis of O-fucosylated proteins.
In EGF domains, the attachment of fucose to serine or threonine occurs within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+).
GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-fucosyl)-L-threonyl-[protein] + GDP + H(+).
GDP-beta-L-fucose + L-seryl-[EGF-like domain protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + GDP + H(+).
GDP-beta-L-fucose + L-threonyl-[EGF-like domain protein] = 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + GDP + H(+).
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase
The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharide alpha-Neu5A-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-L-alpha-Fuc, which is attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains.
The substrate is provided by EC 2.4.1.221.
3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP.
3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP.
glucuronosyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
glucuronosylgalactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Enzyme involved in the initiation of heparin and heparan sulfate synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core.
Apparently products of both the human EXTL2 and EXTL3 genes can catalyze this reaction.
In Caenorhabditis elegans, the product of the rib-2 gene displays this activity as well as that of EC 2.4.1.224.
3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
alpha-N-acetylglucosaminyltransferase II
glucuronyl-N-acetylglucosaminylproteoglycan alpha-1,4-N-acetylglucosaminyltransferase
Involved in the biosynthesis of heparin and heparan sulfate.
Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the EC 2.4.1.225 activity required for the synthesis of the heparan sulfate disaccharide repeats.
Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-alpha-N-acetylglucosaminyltransferase activity.
In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223.
3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + H(+) + UDP.
N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase
N-acetylglucosaminylproteoglycan beta-1,4-glucuronyltransferase
Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the EC 2.4.1.244 activity required for the synthesis of the heparan sulfate disaccharide repeats.
3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein] + H(+) + UDP.
N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase
Involved in the biosynthesis of chondroitin and dermatan sulfate.
The human chondroitin synthetase is a bifunctional glycosyltransferase, which also has the EC 2.4.1.175 activity required for the synthesis of the chondroitin sulfate disaccharide repeats.
There is also another human protein with apparently only the 3-beta-glucuronosyltransferase activity.
3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP.
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP.
lactosylceramide 4-alpha-galactosyltransferase
Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase
a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = globoside Gb3Cer (d18:1(4E)) + H(+) + UDP.
[Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase
Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors.
In Dictyostelium Skp1 is modified by the linear pentasaccharide Galalpha1-6Galalpha1-L-Fucalpha1-2Galbeta1-3GlcNAc, which is attached to a hydroxyproline residue at position 143.
This enzyme catalyzes the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue.
trans-4-hydroxy-L-prolyl-[Skp1 protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + O-(N-acetyl-alpha-D-glucosaminyl)-trans-4-hydroxy-L-prolyl-[Skp1 protein] + UDP.
The enzyme from Thermoanaerobacter brockii can act with alpha-1,2-oligoglucans, such as selaginose, as substrate, but more slowly.
The enzyme is inactive when dissaccharides with linkages other than alpha-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates.
kojibiose + phosphate = beta-D-glucose 1-phosphate + D-glucose.
alpha,alpha-trehalose phosphorylase (configuration-retaining)
Unlike EC 2.4.1.64, this enzyme retains its anomeric configuration.
Vanadate is a strong competitive inhibitor of this reversible reaction.
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate.
initiation-specific alpha-1,6-mannosyltransferase
In Saccharomyces cerevisiae, this enzyme catalyzes an essential step in the outer chain elongation of N-linked oligosaccharides.
Man8GlcNAc and Man9GlcNAc are equally good substrates.
Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.
Acts on the endogenous flavonols kaempferol and quercetin, to a lesser extent on myricetin and fisetin, and weakly on galangin and isorhamnetin.
The reaction can occur equally well in both directions.
kaempferol + UDP-alpha-D-galactose = H(+) + kaempferol 3-O-beta-D-galactoside + UDP.
flavanone 7-O-glucoside 2''-O-beta-L-rhamnosyltransferase
Acts on the 7-O-glucoside of naringenin and hesperetin, also the flavone 7-O-glucosides of luteolin and apigenin.
flavanone 7-O-beta-D-glucoside + UDP-beta-L-rhamnose = flavanone 7-O-[alpha-L-rhamnosyl-(1->2)-beta-D-glucoside] + H(+) + UDP.
UDP-glucose:flavonol 7-O-glucosyltransferase
Acts on the flavonols gossypetin (8-hydroxyquercetin) and to a lesser extent on quercetin, kaempferol and myricetin.
a 7-O-hydroxy-flavonol + UDP-alpha-D-glucose = a flavonol 7-O-beta-D-glucoside + H(+) + UDP.
delphinidin 3,5-di-O-glucoside 3'-O-glucosyltransferase
UDP-glucose:anthocyanin 3'-O-glucosyltransferase
Isolated from the plant Gentiana triflora (clustered gentian).
delphinidin 3,5-bis-O-beta-D-glucoside + UDP-alpha-D-glucose = delphinidin 3,3',5-tri-O-beta-D-glucoside + H(+) + UDP.
flavonol-3-O-glucoside glucosyltransferase
One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 and EC 2.4.1.240).
TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowly.
a flavonol 3-O-beta-D-glucoside + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside + H(+) + UDP.
flavonol-3-O-glycoside glucosyltransferase
One of three specific glucosyltransferases in pea (Pisum sativum) that successively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 and EC 2.4.1.239).
a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside + H(+) + UDP.
UDP-galactose:MGDG galactosyltransferase
UDP-galactose-dependent digalactosyldiacylglycerol synthase
Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalyzed by EC 2.4.1.46.
When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol.
While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions.
DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids.
The enzyme has been localized to the outer side of chloroplast envelope membranes.
a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-D-galactose = 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+) + UDP.
starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase
Unlike EC 2.4.1.11 and EC 2.4.1.21 which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose.
Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose.
In such mutants, only amylopectin is produced in the endosperm or pollen.
[(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+).
fructan:fructan 6(G)-fructosyltransferase
This enzyme catalyzes the transfer of the terminal (2->1)-linked beta-D-fructosyl group of a mono- or oligosaccharide substituent on O-1 of the fructose residue of sucrose onto O-6 of its glucose residue.
For example, if 1-kestose [1(F)-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6(G)-di-beta-D-fructofuranosylsucrose.
In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent; alternatively, this may be indicated by the presence and/or absence of primes.
Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor.
Side reactions catalyzed are transfer of a beta-D-fructosyl group between compounds of the structure 1(F)-(1-beta-D-fructofuranosyl)m-6(G)-(1-beta-D-fructofuranosyl)n sucrose, where m >= 0 and n = 1 for the donor, and m >= 0 and n >= 0 for the acceptor.
[1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0, n >= 0).
N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase
The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end.
The N-acetyl-beta-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments.
Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP.
The enzyme-catalyzed reaction is reversible.
In the reverse direction to that shown above, the enzyme is specific for alpha,alpha-trehalose as substrate, as it cannot use alpha- or beta-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose.
While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-alpha-D-glucose to the same extent, that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-alpha-D-glucose and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-alpha-D-glucose.
an NDP-alpha-D-glucose + D-glucose = a ribonucleoside 5'-diphosphate + alpha,alpha-trehalose + H(+).
ADP-alpha-D-glucose + D-glucose = ADP + alpha,alpha-trehalose + H(+).
GDP-mannose can be replaced by ADP-mannose but with a concomitant decrease in activity.
The product of this reaction is dephosphorylated by EC 3.1.3.79 to form the non-reducing disaccharide mannosylfructose, which is the major endogenous osmolyte produced by several alpha-proteobacteria in response to osmotic stress.
The F in the product name is used to indicate that the fructose residue of sucrose carries the substituent.
beta-D-fructose 6-phosphate + GDP-alpha-D-mannose = beta-D-fructofuranosyl alpha-D-mannopyranoside 6(F)-phosphate + GDP + H(+).
beta-D-galactosyl-(1->4)-L-rhamnose phosphorylase
D-galactosyl-beta1->4-L-rhamnose phosphorylase
The enzyme from Clostridium phytofermentans is also active toward toward beta-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose in this order.
Differs from 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211) in being active toward L-rhamnose and inactive toward N-acetyl hexosamine derivatives.
beta-D-galactosyl-(1->4)-L-rhamnose + phosphate = alpha-D-galactose 1-phosphate + L-rhamnopyranose.
cycloisomaltooligosaccharide glucanotransferase
Specific for (1->6)-alpha-D-glucans (dextrans) and, unlike cyclomaltodextrin glucanotransferase (EC 2.4.1.19), without activity toward (1->4)-alpha-D-glucans, such as amylose.
It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points.
The enzyme from Bacillus circulans T-3040 has been shown to form cycloisomalto-oligosaccharides of three sizes (7, 8 and 9 glucose units).
It will also catalyze the disproportionation of two isomalto-oligosaccharides molecules to yield a series of isomalto-oligosachharides and the addition of D-glucose to cycloisomalto-oligosaccharides with ring opening to form isomalto-oligosaccharides.
cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond.
UDP-glucose:anthocyanin 3',5'-O-glucosyltransferase
Ternatins are a group of polyacetylated delphinidin glucosides that confer blue color to the petals of butterfly pea (Clitoria ternatea).
This enzyme catalyzes two reactions in the biosynthesis of ternatin C5: the conversion of delphinidin 3-O-(6''-O-malonyl)-beta-D-glucoside to delphinidin 3-O-(6''-O-malonyl)-beta-D-glucoside-3'-O-beta-D-glucoside, followed by the conversion of the later to ternatin C5, by transferring two glucosyl groups in a stepwise manner.
delphinidin 3-O-(6''-O-malonyl)-beta-D-glucoside + 2 UDP-alpha-D-glucose = 2 H(+) + ternatin C5 + 2 UDP.
D-inositol-3-phosphate glycosyltransferase
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
The enzyme, which belongs to the GT-B fold superfamily, catalyzes the first dedicated reaction in the biosynthesis of mycothiol.
The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate.
A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate.
1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + H(+) + UDP.
GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase
The enzyme is involved in the biosynthesis of the exopolysaccharide xanthan.
beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + GDP-alpha-D-mannose = beta-D-Man-(1->4)-beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+).
GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase
In the bacterium Gluconacetobacter xylinus (previously known as Acetobacter xylinum) the enzyme is involved in the biosynthesis of the exopolysaccharide acetan.
In Xanthomonas campestris the enzyme is involved in the biosynthesis of the exopolysaccharide xanthan.
beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-1-di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+).
The enzyme is specific for UDP-D-glucuronate as a sugar donor and flavones with substitution ortho- to the 7-OH group such as baicalein (6-OH), scutellarein (6-OH) and wogonin (8-OMe).
baicalein + UDP-alpha-D-glucuronate = baicalin + UDP.
scutellarein + UDP-alpha-D-glucuronate = scutellarin + UDP.
UDP-alpha-D-glucuronate + wogonin = UDP + wogonin 7-O-beta-D-glucuronate.
cyanidin-3-O-glucoside 2''-O-glucuronosyltransferase
The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-alpha-D-glucuronate.
Involved in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis.
cyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucuronate = cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside + H(+) + UDP.
O-linked N-acetylglucosaminyltransferase
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
EC 2.4.1.255 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.
L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP.
L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP.
dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase
Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol alpha1,2-glucosyltransferase
This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an alpha-1,2-linkage to the outermost D-glucose in the long branch.
The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
GDP-Man:Man2GlcNAc2-PP-Dol alpha-1,6-mannosyltransferase
Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation (cf. EC 2.4.1.132) of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway.
alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+).
dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
Dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate.
Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichyl to Man9Glc-NAc2-PP-dolichyl on the lumenal side use dolichyl beta-D-mannosyl phosphate.
The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalyzed by ALG3.
a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
dolichyl-P-Man:Man6GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase
Dol-P-Man:Man6GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase
Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate.
ALG9 mannosyltransferase catalyzes the addition of two different alpha-1,2-mannose residues - the addition of alpha-1,2-mannose to Man6GlcNAc2-PP-dolichol (EC 2.4.1.259) and the addition of alpha-1,2-mannose to Man8GlcNAc2-PP-dolichol (EC 2.4.1.261).
a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
dolichyl-P-Man:Man7GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl alpha6-mannosyltransferase
Dol-P-Man:Man7GlcNAc2-PP-Dol alpha-1,6-mannosyltransferase
a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
dolichyl-P-Man:Man8GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase
Dol-P-Man:Man8GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase
Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate.
ALG9 mannosyltransferase catalyzes the addition of two different alpha-1,2-mannose residues - the addition of alpha-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of alpha-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
soyasapogenol B + UDP-alpha-D-glucuronate = H(+) + soyasapogenol B 3-O-beta-D-glucuronate + UDP.
soyasapogenol A + UDP-alpha-D-glucuronate = H(+) + soyasapogenol A 3-O-beta-D-glucuronate + UDP.
soyasapogenol E + UDP-alpha-D-glucuronate = H(+) + soyasapogenol E 3-O-beta-D-glucuronate + UDP.
The enzyme acts better on (S)-2-trans-abscisate than the natural (S)-2-cis isomer, abscisate, or its enantiomer, the (R)-2-cis isomer.
2-cis-(+)-abscisate + UDP-alpha-D-glucose = beta-D-glucopyranosyl cis-(+)-abscisate + UDP.
2-trans-(+)-abscisate + UDP-alpha-D-glucose = beta-D-glucopyranosyl trans-(+)-abscisate + UDP.
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronosyltransferase
D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase
The enzyme is involved in the biosynthesis of the exopolysaccharides xanthan (in the bacterium Xanthomonas campestris) and acetan (in the bacterium Gluconacetobacter xylinus).
alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-1-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-glucuronate = beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol alpha-1->3-glucosyltransferase
The successive addition of three glucose residues by EC 2.4.1.267, 2.4.1.265 and EC 2.4.1.256 represents the final stage of the lipid-linked oligosaccharide assembly.
a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyzes the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85.
The activity is dependent on divalent cations (Mn(2+), Co(2+), or Mg(2+)).
The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose.
The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor.
The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate.
This enzyme catalyzes the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria.
(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-diphosphate + H(+).
(2R)-3-phosphoglycerate + ADP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + ADP + H(+).
(2R)-3-phosphoglycerate + GDP-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + GDP + H(+).
(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H(+) + UDP.
dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
Dol-P-Glc:Man9GlcNAc2-PP-Dol alpha-1->3-glucosyltransferase
The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 and EC 2.4.1.256 represents the final stage of the lipid-linked oligosaccharide assembly.
a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+).
Persephonella marina possesses two enzymatic systems for the synthesis of glucosylglycerate.
The first one is a single-step pathway in which glucosylglycerate synthase catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate.
The second system is a two-step pathway in which EC 2.4.1.266 catalyzes the conversion of NDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85.
(R)-glycerate + ADP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + ADP + H(+).
Rhodothermus marinus can also form mannosylglycerate via a two-step pathway catalyzed by EC 2.4.1.217 and EC 3.1.3.70.
Depending on experimental conditions mannosylglycerate synthase is more or less specific for the GDP-mannose and D-glycerate.
(R)-glycerate + GDP-alpha-D-mannose = (2R)-2-O-(alpha-D-mannosyl)-glycerate + GDP + H(+).
mannosylglucosyl-3-phosphoglycerate synthase
The enzyme is involved in synthesis of 2-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate.
Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.
(2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + GDP-alpha-D-mannose = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-3-phospho-glycerate + GDP + H(+).
In the plants Crocus sativus and Gardenia jasminoides this enzyme esterifies a free carboxyl group of crocetin and some crocetin glycosyl esters.
The enzyme from Gardenia can also form glucosyl esters with 4-coumarate, caffeate and ferulate.
crocetin + UDP-alpha-D-glucose = beta-D-glucosyl crocetin + UDP.
beta-D-glucosyl crocetin + UDP-alpha-D-glucose = bis(beta-D-glucosyl) crocetin + UDP.
beta-D-gentiobiosyl crocetin + UDP-alpha-D-glucose = beta-D-gentiobiosyl beta-D-glucosyl crocetin + UDP.
soyasapogenol B glucuronide galactosyltransferase
Part of the biosynthetic pathway for soyasaponins.
soyasapogenol B 3-O-beta-D-glucuronate + UDP-alpha-D-galactose = H(+) + soyasaponin III + UDP.
soyasaponin III + UDP-beta-L-rhamnose = H(+) + soyasaponin I + UDP.
glucosylceramide beta-1,4-galactosyltransferase
Involved in the synthesis of several different major classes of glycosphingolipids.
a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP.
neolactotriaosylceramide beta-1,4-galactosyltransferase
lactotriaosylceramide beta-1,4-galactosyltransferase
a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP.
The reaction proceeds in two steps with the monoglucoside as an intermediate.
all-trans-zeaxanthin + 2 UDP-alpha-D-glucose = 2 H(+) + 2 UDP + zeaxanthin bis(beta-D-glucoside).
10-deoxymethynolide desosaminyltransferase
DesVII is the glycosyltransferase responsible for the attachment of dTDP-D-desosamine to 10-deoxymethynolide or narbonolide during the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in the bacterium Streptomyces venezuelae.
Activity requires an additional protein partner, DesVIII.
10-deoxymethynolide + dTDP-alpha-D-desosamine = 10-deoxymethymycin + dTDP + H(+).
3-alpha-mycarosylerythronolide B desosaminyl transferase
The enzyme is involved in erythromycin biosynthesis.
3-O-alpha-L-mycarosylerythronolide B + dTDP-alpha-D-desosamine = dTDP + erythromycin D + H(+).
The enzymes from Clostridium phytofermentans is specific for nigerose, and shows only 0.5% relative activity with kojibiose (cf. EC 2.4.1.230).
nigerose + phosphate = beta-D-glucose 1-phosphate + D-glucose.
The enzyme is specific for N,N'-diacetylchitobiose and does not phosphorylyze other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose.
N,N'-diacetylchitobiose + phosphate = N-acetyl-alpha-D-glucosamine 1-phosphate + N-acetyl-D-glucosamine.
4-O-beta-D-mannosyl-D-glucose phosphorylase
This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343.
4-O-beta-D-mannopyranosyl-D-glucopyranose + phosphate = alpha-D-mannose 1-phosphate + D-glucose.
3-O-alpha-D-glucosyl-L-rhamnose phosphorylase
The enzyme does not phosphorylate alpha,alpha-trehalose, kojibiose, nigerose, or maltose.
In the reverse phosphorolysis reaction the enzyme is specific for L-rhamnose as acceptor and beta-D-glucose 1-phosphate as donor.
3-O-alpha-D-glucosyl-L-rhamnose + phosphate = beta-D-glucose 1-phosphate + L-rhamnopyranose.
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose (cf. EC 2.4.1.284), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-alpha-D-glucosamine.
2-deoxystreptamine + UDP-N-acetyl-alpha-D-glucosamine = 2'-N-acetylparomamine + H(+) + UDP.
Involved in the biosynthesis of kanamycin B and kanamycin C.
Also catalyzes EC 2.4.1.283, but activity is only one fifth of that with UDP-alpha-D-glucose.
2-deoxystreptamine + UDP-alpha-D-glucose = 2'-deamino-2'-hydroxyparomamine + H(+) + UDP.
UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase
Involved in biosynthesis of the aminoglycoside antibiotic neomycin.
ribostamycin + UDP-N-acetyl-alpha-D-glucosamine = 2'''-acetyl-6'''-hydroxyneomycin C + H(+) + UDP.
Isolated from the plant Antirrhinum majus (snapdragon).
Involved in the biosynthesis of aurones, plant flavonoids that provide yellow color to the flowers.
2',4,4',6'-tetrahydroxychalcone + UDP-alpha-D-glucose = 2',4,4',6'-tetrahydroxychalcone 4'-O-beta-D-glucoside + H(+) + UDP.
2',3,4,4',6'-pentahydroxychalcone + UDP-alpha-D-glucose = 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + H(+) + UDP.
rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,4/1,5-galactofuranosyltransferase
arabinogalactan galactofuranosyl transferase 1
Isolated from Mycobacterium tuberculosis and M.smegmatis, the enzyme has dual beta-(1->4) and beta-(1->5) transferase action.
Involved in the formation of the cell wall in mycobacteria.
alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 2 UDP-alpha-D-galactofuranose = beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 2 H(+) + 2 UDP.
galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase
Isolated from Mycobacterium tuberculosis.
The enzyme adds approximately twenty-eight galactofuranosyl residues with alternating 1->5 and 1->6 links forming a galactan domain with approximately thirty galactofuranosyl residues.
beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 28 UDP-alpha-D-galactofuranose = [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + 28 H(+) + 28 UDP.
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
Isolated from Mycobacterium smegmatis and Mycobacterium tuberculosis.
The enzyme catalyzes the addition of a rhamnosyl unit to N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol, completing the synthesis of the linkage unit that attaches the arabinogalactan moiety to the peptidoglycan moiety in Mycobacterial cell wall.
dTDP-beta-L-rhamnose + N-acetyl-alpha-D-glucosaminyl-1-diphospho-trans,octa-cis-decaprenol = alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol + dTDP + H(+).
N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
Part of a bacterial N-linked glycosylation pathway.
N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP.
N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase
N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-alpha-D-galactosaminyl-(1->4)-N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,heptacis-undecaprenyl diphosphate + UDP.
GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase
N-acetyl-alpha-D-galactosaminyl-(1->4)-N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,heptacis-undecaprenyl diphosphate + 3 UDP-N-acetyl-alpha-D-galactosamine = [alpha-D-GalNAc-(1->4)]4-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + 3 H(+) + 3 UDP.
GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase
Isolated from the bacterium Campylobacter jejuni.
[alpha-D-GalNAc-(1->4)]4-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-alpha-D-glucose = [alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-[alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + H(+) + UDP.
cyanidin + UDP-alpha-D-galactose = cyanidin 3-O-beta-D-galactoside + H(+) + UDP.
anthocyanin 3-O-sambubioside 5-O-glucosyltransferase
Isolated from the plant Matthiola incana (stock).
No activity with anthocyanidin 3-O-glucosides.
an anthocyanidin 3-O-beta-D-sambubioside + UDP-alpha-D-glucose = an anthocyanidin 5-O-beta-D-glucoside 3-O-beta-D-sambubioside + H(+) + UDP.
anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase
Isolated from the plant Petunia hybrida.
It does not act on an anthocyanidin 3-O-rutinoside.
an anthocyanidin 3-O-[2-O-(4-coumaroyl)-alpha-L-rhamnosyl-(1->6)-beta-D-glucoside] + UDP-alpha-D-glucose = an anthocyanidin 3-O-[2-O-(4-coumaroyl)-alpha-L-rhamnosyl-(1->6)-beta-D-glucoside] 5-O-beta-D-glucoside + H(+) + UDP.
anthocyanidin 3-O-glucoside 2''-O-glucosyltransferase
Isolated from Ipomoea nil (Japanese morning glory).
an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose = an anthocyanidin 3-O-sophoroside + 2 H(+) + UDP.
anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
Isolated from the plants Perilla frutescens var. crispa, Verbena hybrida, Dahlia variabilis and Gentiana triflora (clustered gentian).
It will also act on anthocyanidin 3-O-(6-O-malonylglucoside) and is much less active with hydroxycinnamoylglucose derivatives.
There is no activity in the absence of the 3-O-glucoside group.
an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose = an anthocyanidin 3,5-di-O-beta-D-glucoside + 2 H(+) + UDP.
cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)
Isolated from the plant Dianthus caryophyllus (carnation).
Also acts on other anthocyanidins and with other acyl-glucose donors.
1-O-(trans-sinapoyl)-beta-D-glucose + cyanidin 3-O-beta-D-glucoside = (E)-sinapate + cyanidin 3,5-di-O-beta-D-glucoside.
cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)
Isolated from the plant Delphinium grandiflorum (delphinium).
Also acts on other anthocyanidins and with other acyl-glucose derivatives.
1-O-(4-hydroxy-3-methoxybenzoyl)-beta-D-glucose + cyanidin 3-O-beta-D-glucoside = cyanidin 3,7-di-O-beta-D-glucoside + vanillate.
2'-deamino-2'-hydroxyneamine 1-alpha-D-kanosaminyltransferase
Involved in the biosynthetic pathway of kanamycins.
The enzyme characterized from the bacterium Streptomyces kanamyceticus can also accept UDP-alpha-D-glucose with lower efficiency.
2'-deamino-2'-hydroxyneamine + UDP-alpha-D-kanosamine = H(+) + kanamycin A + UDP.
neamine + UDP-alpha-D-kanosamine = H(+) + kanamycin B + UDP.
paromamine + UDP-alpha-D-kanosamine = H(+) + kanamycin C + UDP.
2'-deamino-2'-hydroxyparomamine + UDP-alpha-D-kanosamine = H(+) + kanamycin X + UDP.
The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin.
dTDP-4-O-demethyl-beta-L-noviose + novobiocic acid = desmethyldescarbamoylnovobiocin + dTDP + H(+).
UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-galactosyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of Escherichia coli O7:K1 (VW187).
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-galactose = beta-D-Gal-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,4-galactosyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14.
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-galactose = beta-D-Gal-(1->4)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
UDP-Glc:alpha-D-GlcNAc-glucosaminyl-diphosphoundecaprenol beta-1,3-glucosyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-glucose = beta-D-Glc-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
UDP-GalNAc:alpha-D-GalNAc-diphosphoundecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of Escherichia coli serotype O86.
N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-galactosamine = alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
GDP-Fuc:beta-D-Gal-1,3-alpha-D-GalNAc-1,3-alpha-GalNAc-diphosphoundecaprenol alpha-1,2-fucosyltransferase
The enzyme is involved in the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.
beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate + GDP-beta-L-fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+).
UDP-Gal:alpha-L-Fuc-1,2-beta-Gal-1,3-alpha-GalNAc-1,3-alpha-GalNAc-diphosphoundecaprenol alpha-1,3-galactosyltransferase
The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.
alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-galactose = alpha-D-Gal-(1->3)-[alpha-L-Fuc-(1->2)]-beta-D-Gal-(1->3)-alpha-D-GalNAc-(1->3)-alpha-D-GalNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.
UDP-alpha-D-glucose + vancomycin aglycone = devancoaminyl-vancomycin + UDP.
devancoaminyl-vancomycin + dTDP-beta-L-4-epi-vancosamine = chloroorienticin B + dTDP + H(+).
protein O-mannose beta-1,4-N-acetylglucosaminyltransferase
The human protein is involved in the formation of a phosphorylated trisaccharide on a threonine residue of alpha-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-threonyl-[protein] + H(+) + UDP.
protein O-mannose beta-1,3-N-acetylgalactosaminyltransferase
The human protein is specific for UDP-N-acetyl-alpha-D-galactosamine as donor.
The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of alpha-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
3-O-(N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-Thr-[protein] + H(+) + UDP.
The glucosyl group forms a 1->6 bond to the glucosyloxy moiety at C-20 of ginsenoside Rd.
Isolated from sanchi ginseng (Panax notoginseng).
(20S)-ginsenoside Rd + UDP-alpha-D-glucose = (20S)-ginsenoside Rb1 + H(+) + UDP.
diglucosyl diacylglycerol synthase (1,6-linking)
monoglucosyl diacylglycerol (1->6) glucosyltransferase
The enzyme is found in several bacterial species.
The enzyme from Bacillus subtilis is specific for glucose.
The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo.
The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1'-sn-glycerol).
a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc)-sn-glycerol + H(+) + UDP.
a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc)-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc-(1->6)-beta-D-Glc)-sn-glycerol + H(+) + UDP.
The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
dTDP-alpha-D-mycaminose + tylactone = 5-O-beta-D-mycaminosyltylactone + dTDP + H(+).
O-mycaminosyltylonolide 6-deoxyallosyltransferase
5-O-beta-D-mycaminosyltylonolide + dTDP-6-deoxy-alpha-D-allose = demethyllactenocin + dTDP + H(+).
demethyllactenocin + dTDP-beta-L-mycarose = demethylmacrocin + dTDP + H(+).
beta-1,4-mannooligosaccharide phosphorylase
The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyzes the reversible phosphorolysis of beta-1,4-mannooligosaccharide with a minimum size of three monomers.
[(1->4)-beta-D-mannosyl](n) + phosphate = [(1->4)-beta-D-mannosyl](n-1) + alpha-D-mannose 1-phosphate.
1,4-beta-mannosyl-N-acetylglucosamine phosphorylase
The enzyme isolated from the anaerobic bacterium Bacteroides thetaiotaomicron is involved in the degradation of host-derived N-glycans.
4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = alpha-D-mannose 1-phosphate + N-acetyl-D-glucosamine.
The enzyme occurs in cellulolytic bacteria and fungi.
It catalyzes the reversible phosphorolysis of cellobionic acid.
In the synthetic direction it produces 4-O-beta-D-glucopyranosyl-D-glucuronate from alpha-D-glucose 1-phosphate and D-glucuronate with low activity.
4-O-beta-D-glucopyranosyl-D-gluconate + phosphate = alpha-D-glucose 1-phosphate + D-gluconate.
devancosaminyl-vancomycin vancosaminetransferase
desvancosaminyl-vancomycin vancosaminetransferase
devancosamine-vancomycin TDP-vancosaminyltransferase
The enzyme, isolated from the bacterium Amycolatopsis orientalis, catalyzes the ultimate step in the biosynthesis of the antibiotic vancomycin.
devancoaminyl-vancomycin + dTDP-beta-L-vancosamine = dTDP + H(+) + vancomycin.
7-deoxyloganetic acid glucosyltransferase
Isolated from the plant Catharanthus roseus (Madagascar periwinkle).
Involved in loganin and secologanin biosynthesis.
7-deoxyloganetate + UDP-alpha-D-glucose = 7-deoxyloganate + H(+) + UDP.
Isolated from the plants Catharanthus roseus (Madagascar periwinkle) and Gardenia jasminoides (cape jasmine).
7-deoxyloganetin + UDP-alpha-D-glucose = 7-deoxyloganin + H(+) + UDP.
TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli.
The trisaccharide of the product (lipid III) is the repeat unit of ECA.
beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose = alpha-D-FucNAc4-(1->4)-beta-D-ManNAcA-(1->4)-D-GlcNAc-undecaprenyl diphosphate + dTDP + H(+).
Isolated from the bacterium Streptomyces galilaeus.
Forms a complex with its accessory protein AknT, and has very low activity in its absence.
The enzyme can also use dTDP-2-deoxy-beta-L-fucose.
Involved in the biosynthesis of other aclacinomycins.
aklavinone + dTDP-beta-L-rhodosamine = aclacinomycin T + dTDP + 2 H(+).
aclacinomycin-T 2-deoxy-L-fucose transferase
The enzyme, isolated from the bacterium Streptomyces galilaeus, is involved in the biosynthesis of other aclacinomycins.
It will slowly add a second 2-deoxy-L-fucose unit to aclacinomycin S in vitro.
aclacinomycin T + dTDP-2-deoxy-beta-L-fucose = aclacinomycin S + dTDP + H(+).
aclacinomycin S + dTDP-2-deoxy-beta-L-fucose = 2-deoxy-alpha-L-fucosylaclacinomycin S + dTDP + H(+).
Isolated from the bacterium Saccharopolyspora erythraea.
dTDP-beta-L-mycarose + erythronolide B = 3-O-alpha-L-mycarosylerythronolide B + dTDP + H(+).
The enzyme, isolated from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum, catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate.
It also acts on sucrose with lower activity.
phosphate + sucrose 6(F)-phosphate = alpha-D-glucose 1-phosphate + beta-D-fructose 6-phosphate.
beta-D-glucosyl crocetin beta-1,6-glucosyltransferase
The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271).
beta-D-glucosyl crocetin + UDP-alpha-D-glucose = beta-D-gentiobiosyl crocetin + H(+) + UDP.
bis(beta-D-glucosyl) crocetin + UDP-alpha-D-glucose = beta-D-gentiobiosyl beta-D-glucosyl crocetin + H(+) + UDP.
beta-D-gentiobiosyl beta-D-glucosyl crocetin + UDP-alpha-D-glucose = bis(beta-D-gentiobiosyl) crocetin + H(+) + UDP.
8-demethyltetracenomycin C L-rhamnosyltransferase
Isolated from Streptomyces olivaceus Tu2353.
In vitro it can also utilize other 6-deoxy D- or L-hexoses.
8-demethyltetracenomycin C + dTDP-beta-L-rhamnose = 8-demethyl-8-alpha-L-rhamnosyl-tetracenomycin C + dTDP + H(+).
1,2-alpha-glucosylglycerol phosphorylase
2-O-alpha-D-glucopyranosylglycerol phosphorylase
The enzyme has been isolated from the bacterium Bacillus selenitireducens.
In the absence of glycerol the enzyme produces alpha-D-glucopyranose and phosphate from beta-D-glucopyranose 1-phosphate.
In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation.
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = beta-D-glucose 1-phosphate + glycerol.
The enzyme has been isolated from the bacterium Listeria innocua.
It catalyzes the reversible phosphorolysis of beta-(1->2)-D-glucans.
The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units.
In the synthetic reaction starting from sophorose and alpha-D-glucose 1-phosphate the average polymerisation degree is 39.
[(1->2)-beta-D-glucosyl](n) + phosphate = [(1->2)-beta-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.
The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyzes a reversible reaction.
Substrates for the phosphorolytic reaction are alpha-1,3-linked oligoglucans with a polymerisation degree of 3 or more.
Nigerose (i.e. 3-O-alpha-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279).
[(1->3)-alpha-D-glucosyl](n) + phosphate = [(1->3)-alpha-D-glucosyl](n-1) + beta-D-glucose 1-phosphate.
dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase
The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, participates in the N-glycosylation of proteins.
Dolichol used by archaea is different from that used by eukaryotes; it is much shorter (C55-C60), it is alpha,omega-saturated and it may have additional unsaturated positions in the chain.
an archaeal dolichyl N-acetyl-alpha-D-glucosaminyl phosphate + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate = an archaeal dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy- beta-D-glucuronosyl)-N-acetyl- alpha-D-glucosaminyl phosphate + H(+) + UDP.
The enzymes from cyanobacteria are involved in the biosynthesis of galactolipids found in their photosynthetic membranes.
The enzyme belongs to the GT2 family of configuration-inverting glycosyltranferases.
a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + H(+) + UDP.
1,2-diacylglycerol 3-alpha-glucosyltransferase
1,2-diacylglycerol 3-glucosyltransferase
UDP-glucose-diacylglycerol glucosyltransferase
uridine diphosphoglucose-diacylglycerol glucosyltransferase
The enzyme from the bacterium Acholeplasma laidlawii, which lacks a celll wall, produces the major non-bilayer lipid in the organism.
The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids.
The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases.
Many diacylglycerols with long-chain acyl groups can act as acceptors.
a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol + H(+) + UDP.
The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyzes the ultimate step in the biosynthesis of the antifungal agent validamycin A.
UDP-alpha-D-glucose + validoxylamine A = H(+) + UDP + validamycin A.
The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyzes a reversible reaction.
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate = alpha-D-mannose 1-phosphate + D-mannose.
In the synthetic direction it produces oligosaccharides with a degree of polymerization (DP) of 3, 4 and 5.
The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues.
[(1->2)-beta-D-mannosyl](n) + phosphate = [(1->2)-beta-D-mannosyl](n-1) + alpha-D-mannose 1-phosphate.
The enzyme, characterized from the bacterium Escherichia coli O55:H7, participates in the biosynthesis of an O-antigen.
The reaction involves anomeric inversion, and does not require any metal ions.
The enzyme is highly specific toward the acceptor, exclusively recognizing lacto-N-biose, but can accept GDP-L-fucose as the donor with almost the same activity as with GDP-beta-L-colitose.
beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + GDP-beta-L-colitose = alpha-L-colitosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + GDP + H(+).
The enzyme, found in Mycobacteria, can also use UDP-alpha-D-glucose with much lower catalytic efficiency.
ADP-alpha-D-glucose + alpha-D-glucose 1-phosphate = ADP + alpha-maltose 1-phosphate + H(+).
UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol alpha-1,3-galactosyltransferase
The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O3.
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-galactose = alpha-D-Gal-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP.
type 2 galactoside alpha-(1,2)-fucosyltransferase
beta-galactoside alpha(1->2)fucosyltransferase
guanosine diphosphofucose-lactose fucosyltransferase
guanosine diphospho-L-fucose-lactose fucosyltransferase
H-gene-encoded beta-galactoside alpha(1->2)fucosyltransferase
The enzyme acts on a glycoconjugates where the substituent is a glycoprotein or glycosphingolipid.
The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen.
a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP + H(+).
phosphatidyl-myo-inositol alpha-mannosyltransferase
guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + GDP-alpha-D-mannose = a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D-myo-inositol] + GDP + H(+).
phosphatidyl-myo-inositol dimannoside synthase
a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D-myo-inositol] + GDP-alpha-D-mannose = a 2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + GDP + H(+).
a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-6-acyl-mannopyranosyl-(1<->6)-D-myo-inositol] + GDP-alpha-D-mannose = 2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + GDP + H(+).
alpha,alpha-trehalose-phosphate synthase (ADP-forming)
ADP-glucose--glucose-phosphate glucosyltransferase
The enzyme has been reported from the yeast Saccharomyces cerevisiae and from mycobacteria.
The enzyme from Mycobacterium tuberculosis can also use UDP-alpha-D-glucose, but the activity with ADP-alpha-D-glucose, which is considered the main substrate in vivo, is higher.
ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate + H(+).
N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-alpha-mannosyltransferase
The enzyme is involved in the biosynthesis of the linker region of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotypes O8, O9 and O9a.
GDP-alpha-D-mannose + N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate = alpha-D-mannosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+).
mannosyl-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-alpha-mannosyltransferase
It has no activity with N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol (Cf. EC 2.4.1.348).
alpha-D-mannosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP-alpha-D-mannose = alpha-D-mannosyl-(1->3)-alpha-D-mannosyl-(1->3)-alpha-D-mannosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP + 2 H(+).
mogrol + UDP-alpha-D-glucose = H(+) + mogroside IE + UDP.
rhamnogalacturonan I rhamnosyltransferase
The enzyme, characterized from Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan type I.
It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 7.
alpha-D-galacturonosyl-[(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n) + UDP-beta-L-rhamnose = [(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP.
The enzyme has been characterized from the bacterium Meiothermus silvanus.
(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate = (R)-glycerate + alpha-D-glucose 1-phosphate.
The enzyme, isolated from the fungus Sordaria araneosa, is involved in the biosynthesis of the glycoside antibiotic sordarin.
GDP-6-deoxy-alpha-D-altrose + sordaricin = 4'-O-demethylsordarin + GDP + H(+).
(R)-mandelonitrile beta-glucosyltransferase
The enzyme, characterized from Prunus dulcis (almond), is involved in the biosynthesis of the cyanogenic glycosides (R)-prunasin and (R)-amygdalin.
(R)-mandelonitrile + UDP-alpha-D-glucose = (R)-prunasin + H(+) + UDP.
poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase
Involved in the biosynthesis of poly(ribitol-phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus.
This enzyme adds an N-acetyl-beta-D-glucosamine to the OH group at the 2 position of the ribitol phosphate units.
4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n UDP-N-acetyl-alpha-D-glucosamine = 4-O-([2-N-acetyl-beta-D-glucosaminyl-1-D-ribitylphospho](n)-di{[2R]-1-glycerylphospho})-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n H(+) + n UDP.
glucosyl-dolichyl phosphate glucuronosyltransferase
The enzyme, characterized from the halophilic archaeon Haloferax volcanii, participates in the protein N-glycosylation pathway.
Dolichol used by archaea is different from that used by eukaryotes.
It is much shorter (C55-C60) and is alpha,omega-saturated.
However, in vitro the enzyme was also able to act on a substrate with an unsaturated end.
an archaeal dolichyl alpha-D-glucosyl phosphate + UDP-alpha-D-glucuronate = an archaeal dolichyl beta-D-glucuronosyl-(1->4)-alpha-D-glucosyl phosphate + H(+) + UDP.
Phlorizin inhibits sodium-linked glucose transporters.
It gives the characteristic flavor of apples and cider.
phloretin + UDP-alpha-D-glucose = H(+) + phlorizin + UDP.
Isolated from strawberries (Fragaria X ananassa).
Acts best on phloroisovalerophenone and phlorobutyrophenone but will also glycosylate many other phenolic compounds.
A minor product of the reaction is the 5-O-beta-D-glucoside.
a 2-acylphloroglucinol + UDP-alpha-D-glucose = a 2-acylphloroglucinol 1-O-beta-D-glucoside + UDP.
glucosylglycerol phosphorylase (configuration-retaining)
2-O-alpha-D-glucosylglycerol phosphorylase (retaining)
The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-alpha-D-glucopyranosyl-glycerol when the environmental salt concentration decreases.
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = alpha-D-glucose 1-phosphate + glycerol.
2-hydroxyflavanone C-glucosyltransferase
The enzyme has been characterized in Oryza sativa (rice), various Citrus spp., Glycine max (soybean), and Fagopyrum esculentum (buckwheat).
Flavanone substrates require a 2-hydroxy group.
The meta-stable flavanone substrates such as 2-hydroxynaringenin exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione, which are the actual substrates for the glucosyl-transfer reaction (see EC 1.14.14.162).
The enzyme can also act on dihydrochalcones.
The enzymes from citrus plants can catalyze a second C-glycosylation reaction at position 5.
a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-oxodihydrochalcone + H(+) + UDP.
GDP-mannose:di-myo-inositol-1,3'-phosphate beta-1,2-mannosyltransferase
The enzyme from the hyperthermophilic bacterium Thermotoga maritima is involved in the synthesis of the solutes 2-O-(beta-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate and 2-O-(beta-D-mannosyl-(1->2)-beta-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate.
bis(myo-inositol) 1,3'-phosphate + 2 GDP-alpha-D-mannose = 2-O-(beta-D-mannosyl-(1->2)-beta-D-mannosyl)-bis(myo-inositol) 1,3'-phosphate + 2 GDP + 2 H(+).
The enzyme from Leuconostoc spp. is responsible for producing alpha-(1->3) branches in alpha-(1->6) glucans by transferring the glucose residue from fructose to a 3-hydroxyl group of a glucan.
sucrose + a (1->6)-alpha-D-glucan = D-fructose + a (1->6)-alpha-D-glucan containing a (1->3)-alpha-D-glucose branch.
The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C20(S)-OH group of dammarane derivative substrates, including protopanaxatriol, dammarenediol II, (20S)-ginsenoside Rh2, and (20S)-ginsenoside Rg3.
It does not act on the 20R epimer of protopanaxadiol, or on ginsenosides that are glucosylated at the C-6 position, such as ginsenoside Rh1 or ginsenoside Rg2.
(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP.
(20S)-protopanaxatriol + UDP-alpha-D-glucose = (20S)-ginsenoside F1 + H(+) + UDP.
(20S)-ginsenoside Rg3 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP.
(20S)-ginsenoside Rh2 + UDP-alpha-D-glucose = (20S)-ginsenoside F2 + H(+) + UDP.
dammarenediol-II + UDP-alpha-D-glucose = (20S)-20-O-(beta-D-glucosyl)-3-hydroxydammarene + H(+) + UDP.
protopanaxadiol-type ginsenoside 3-O-glucosyltransferase
The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the free C-3-OH group of (20S)-protopanaxadiol and ginsenoside C-K.
(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside Rh2 + H(+) + UDP.
(20S)-ginsenoside C-K + UDP-alpha-D-glucose = (20S)-ginsenoside F2 + H(+) + UDP.
protopanaxadiol-type ginsenoside-3-O-glucoside 2''-O-glucosyltransferase
The enzyme, characterized from the plant Panax ginseng, transfers a glucosyl moiety to the 2'' position of the glucose moiety in the protopanaxadiol-type ginsenoside-3-O-glucosides (20S)-ginsenoside Rh2 and ginsenoside F2.
(20S)-ginsenoside Rh2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rg3 + H(+) + UDP.
(20S)-ginsenoside F2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP.
The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of ginsenoside F1.
The enzyme also glucosylates the C-20 position of protopanaxatriol, which forms ginsenoside F1 (cf. EC 2.4.1.363).
However, unlike EC 2.4.1.367, it is not able to glucosylate the C-6 position of protopanaxatriol when position C-20 is not glucosylated.
(20S)-ginsenoside F1 + UDP-alpha-D-glucose = (20S)-ginsenoside Rg1 + H(+) + UDP.
The enzyme, characterized from the plant Panax ginseng, glucosylates the C-6 position of protopanaxatriol and ginsenoside F1.
(20S)-protopanaxatriol + UDP-alpha-D-glucose = (20S)-ginsenoside Rh1 + H(+) + UDP.
The enzyme has been characterized from the saponin-producing crucifer plant Barbarea vulgaris.
oleanolate + UDP-alpha-D-glucose = H(+) + oleanolate 3-O-beta-D-glucoside + UDP.
The enzyme, found in pathogenic strains of the bacteria Escherichia coli and Salmonella enterica, catalyzes the transfer of glucosyl groups to C-5 of one, two, or three of the 2,3-hydroxybenzoyl units of the siderophore enterobactin, forming C-glucosylated derivatives known as salmochelins.
enterobactin + UDP-alpha-D-glucose = monoglucosyl-enterobactin + UDP.
monoglucosyl-enterobactin + UDP-alpha-D-glucose = diglucosyl-enterobactin + H(+) + UDP.
diglucosyl-enterobactin + UDP-alpha-D-glucose = H(+) + triglucosyl-enterobactin + UDP.
inositol phosphorylceramide mannosyltransferase
The simplest complex sphingolipid of yeast, inositol-phospho-alpha-hydroxyphytoceramide (IPC), is usually mannosylated to yield mannosyl-inositol-phospho-alpha hydroxyphytoceramide (MIPC).
The enzyme is located in the Golgi apparatus, and utilizes GDP-alpha-D-mannose as the mannosyl group donor.
It consists of a catalytic subunit (SUR1 or CSH1) and a regulatory subunit (CSG2).
a 1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base + GDP-alpha-D-mannose = an alpha-D-mannosyl-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base + GDP + H(+).
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-alpha-mannosylpolymerase
The enzyme is involved in the biosynthesis of polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a.
The enzymes consists of two domains that are responsible for the 1->2 and 1->3 linkages, respectively.
[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP + 2 H(+).
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP-alpha-D-mannose = [alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n+1)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP + 2 H(+).
This enzyme extends the glucan chain by an alpha(1->3) linkage.
[(1->3)-alpha-D-glucosyl](n) + sucrose = [(1->3)-alpha-D-glucosyl](n+1) + D-fructose.
This enzyme introduces alpha(1->2) branches into (1->6)-alpha-D-glucans.
sucrose + a (1->6)-alpha-D-glucan = D-fructose + a (1->6)-alpha-D-glucan containing a (1->2)-alpha-D-glucose branch.
The enzyme, characterized from Leishmania parasites, is involved in synthesis of mannogen, a beta-(1->2)-mannan oligosaccharide used by the organisms as a carbohydrate reserve.
[(1->2)-beta-D-mannosyl](n) + GDP-alpha-D-mannose = [(1->2)-beta-D-mannosyl](n+1) + GDP + H(+).
rhamnogalacturonan I galactosyltransferase
The enzyme, characterized from the plant Vigna angularis (azuki beans), participates in the biosynthesis of rhamnogalacturonan I, one of the components of pectin in plant cell wall.
It does not require any metal ions, and prefers substrates with a degree of polymerization larger than 9.
Transfer of a beta-galactosyl residue in a beta-(1->4) linkage from UDP-alpha-D-galactose to rhamnosyl residues within the rhamnogalacturonan I backbone.
The enzyme, found in animals and insects, is involved in the biosynthesis of the alpha-D-xylosyl-(1->3)-alpha-D-xylosyl-(1->3)-beta-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains.
Glycosylation takes place at the serine in the C-X-S-X-P-C motif.
The enzyme is bifunctional also being active with UDP-alpha-xylose as donor (EC 2.4.2.63).
When present on Notch proteins, the trisaccharide functions as a modulator of the signaling activity of this protein.
L-seryl-[EGF-like domain protein] + UDP-alpha-D-glucose = 3-O-(beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP.
dTDP-Rha:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-rhamnosyltransferase
The enzyme, characterized from several Salmonella strains, participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B, D and E groups.
alpha-D-galactosyl-di-trans,octa-cis-undecaprenyl diphosphate + dTDP-beta-L-rhamnose = alpha-L-rhamnosyl-(1->3)-alpha-D-galactosyl-1-diphospho-di-trans,octa-cis-undecaprenol + dTDP + H(+).
GDP-mannose:alpha-L-Rha-(1->3)-alpha-D-Gal-PP-Und alpha-1,4-mannosyltransferase
The enzyme from Salmonella participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B, and D1 groups.
alpha-L-rhamnosyl-(1->3)-alpha-D-galactosyl-1-diphospho-di-trans,octa-cis-undecaprenol + GDP-alpha-D-mannose = alpha-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+).
GDP-Man:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-mannosyltransferase
alpha-D-galactosyl-di-trans,octa-cis-undecaprenyl diphosphate + GDP-alpha-D-mannose = alpha-D-mannosyl-(1->3)-alpha-D-galactosyl-diphospho-di-trans,octa-cis-undecaprenol + GDP + H(+).
GDP-Man:alpha-D-Man-(1->3)-alpha-D-Gal diphosphoundecaprenol alpha-1,2-mannosyltransferase
alpha-D-mannosyl-(1->3)-alpha-D-galactosyl-diphospho-di-trans,octa-cis-undecaprenol + GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + GDP + H(+).
dTDP-Rha:alpha-D-Man-(1->3)-alpha-D-Gal diphosphoundecaprenol alpha-1,2-rahmnosyltransferase
alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + dTDP-beta-L-rhamnose = alpha-L-Rha-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + dTDP + H(+).
CDP-abequose:alpha-L-Rha2OAc-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-PP-Und alpha-1,3-abequosyltransferase
alpha-L-2OAcRha-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP-alpha-D-abequose = alpha-D-Abe-(1->3)-alpha-L-Rha2OAc-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Gal-di-trans,octa-cis-undecaprenyl diphosphate + CDP + H(+).
GDP-Man:alpha-L-Rha-(1->3)-alpha-D-Gal-PP-Und beta-1,4-mannosyltransferase
The enzyme participates in the biosynthesis of the O antigens produced by group E and D2 strains of the pathogenic bacterium Salmonella enterica.
alpha-L-rhamnosyl-(1->3)-alpha-D-galactosyl-1-diphospho-di-trans,octa-cis-undecaprenol + GDP-alpha-D-mannose = beta-D-Man-(1->4)-alpha-L-Rha-(1->3)-alpha-D-Gal-diphospho-di-trans,octa-cis-undecaprenol + GDP + H(+).
The enzyme, characterized from the bacterium Bacillus licheniformis DSM-13, is an extremely promiscuous glycosyltransferase.
It can accept ADP-, GDP-, CDP-, TDP-, or UDP-activated glycose molecules as donors, and can glycosylate a large number of substrates, catalyzing O-, N-, or S-glycosylation.
While D-glucose is the primarily reported sugar being transferred, the enzyme has been shown to transfer D-galactose, 2-deoxy-D-glucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, L-fucose, L-rhamnose, D-glucuronate, and D-viosamine.
an NDP-glycose + an acceptor = a glycosylated acceptor + NDP.
sucrose + UDP-alpha-D-galactose = H(+) + loliose + UDP.
Can also catalyze ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5.
a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate.
a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + a purine nucleobase.
guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine.
adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate.
phosphate + xanthosine = alpha-D-ribose 1-phosphate + xanthine.
inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine.
2'-deoxyadenosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + adenine.
2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine.
2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + hypoxanthine.
Unlike EC 2.4.2.3 and EC 2.4.2.4, this enzyme can accept both the ribonucleoside uridine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine.
The reaction is reversible, and the enzyme does not distinguish between alpha-D-ribose 1-phosphate and 2-deoxy-alpha-D-ribose 1-phosphate in the synthetic direction.
phosphate + uridine = alpha-D-ribose 1-phosphate + uracil.
cytidine + phosphate = alpha-D-ribose 1-phosphate + cytosine.
2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + uracil.
phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine.
The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage.
The mammalian enzyme also accepts 2'-deoxyuridine.
In some tissues also catalyzes deoxyribosyltransferase reactions of the type catalyzed by EC 2.4.2.6.
Base(1) and base(2) represent various purines and pyrimidines.
D-ribosyl-base(1) + base(2) = D-ribosyl-base(2) + base(1).
2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + base(1).
5-Amino-4-imidazolecarboxamide can replace adenine.
AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine.
hypoxanthine-guanine phosphoribosyltransferase
Guanine and purine-6-thiol can replace hypoxanthine.
diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine.
diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + guanine.
diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil.
orotidine-5'-phosphate pyrophosphorylase
The enzyme from higher eukaryotes also catalyzes the reaction listed as EC 4.1.1.23.
diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate.
beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + H(+) + nicotinamide.
glutamine phosphoribosylpyrophosphate amidotransferase
phosphoribosyldiphosphate 5-amidotransferase
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine.
phosphate + urate D-ribonucleoside = alpha-D-ribose 1-phosphate + urate.
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP.
phosphoribosyl-anthranilate diphosphorylase
phosphoribosyl-anthranilate pyrophosphorylase
In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24).
diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate.
nicotinate-nucleotide diphosphorylase (carboxylating)
nicotinate-nucleotide pyrophosphorylase (carboxylating)
quinolinate phosphoribosyltransferase (decarboxylating)
The reaction is catalyzed in the opposite direction.
Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD+ biosynthesis enzyme shared by both eukaryotes and prokaryotes.
CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate.
dioxotetrahydropyrimidine phosphoribosyltransferase
dioxotetrahydropyrimidine-ribonucleotide diphosphorylase
dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase
Acts, in the reverse direction, on uracil and other pyrimidines and pteridines containing a 2,4-diketo structure.
5,6-dihydrouridine 5'-monophosphate + diphosphate = 5,6-dihydrouracil + 5-phospho-alpha-D-ribose 1-diphosphate.
nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase
Also acts on benzimidazole, and the clostridial enzyme acts on adenine to form 7-alpha-D-ribosyladenine 5'-phosphate.
The product of the reaction, alpha-ribazole 5'-phosphate, forms part of the corrin biosynthesis pathway and is a substrate for EC 2.7.8.2.
It can also be dephosphorylated to form alpha-ribazole by the action of EC 3.1.3.73.
5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate.
xanthine-guanine phosphoribosyltransferase
xanthosine 5'-phosphate pyrophosphorylase
diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine.
[(1->4)-beta-D-xylan](n) + UDP-alpha-D-xylose = [(1->4)-beta-D-xylan](n+1) + H(+) + UDP.
7-O-beta-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors.
apigenin 7-O-beta-D-glucoside + UDP-alpha-D-apiose = 7-O-(beta-D-apiofuranosyl-1,2-beta-D-glucosyl)-5,7,4'-trihydroxyflavone + H(+) + UDP.
UDP-xylose-core protein beta-D-xylosyltransferase
uridine diphosphoxylose-core protein beta-xylosyltransferase
uridine diphosphoxylose-protein xylosyltransferase
L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP.
dTDP-dihydrostreptose--streptidine-6-phosphate dihydrostreptosyltransferase
dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP + H(+) + O-(1->4)-alpha-L-dihydrostreptosyl-streptidine 6-phosphate.
5'-deoxy-5'-methylthioadenosine phosphorylase
methylthioadenosine nucleoside phosphorylase
Also acts on 5'-deoxyadenosine and other analogs having 5'-deoxy groups.
phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.
5'-deoxyadenosine + phosphate = 5-deoxy-alpha-D-ribose 1-phosphate + adenine.
tRNA-guanosine(34) preQ1 transglycosylase
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34.
In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine.
The enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn).
This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway.
7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-aminomethyl-7-carbaguanosine(34) in tRNA + guanine.
poly(adenosine diphosphate ribose) polymerase
The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
NAD(+)--protein-arginine ADP-ribosyltransferase
NAD(P)(+)--arginine ADP-ribosyltransferase
NAD(P)(+)--protein-arginine ADP-ribosyltransferase
Arginine residues in proteins act as acceptors.
Free arginine, agmatine [(4-aminobutyl)guanidine], arginine methyl ester and guanidine can also do so.
The enzyme from some, but not all, species can also use NADP(+) as acceptor (giving rise to N(omega)-[(2'-phospho-ADP)-D-ribosyl]-protein-L-arginine as the product), but more slowly.
Catalyzes the NAD(+)-dependent activation of EC 4.6.1.1.
Some bacterial enterotoxins possess similar enzymatic activities (cf. EC 2.4.2.36).
L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide.
L-arginyl-[protein] + NADP(+) = H(+) + N(omega)-(2'-phospho-ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide.
a dolichyl phosphate + UDP-alpha-D-xylose = a dolichyl D-xylosyl phosphate + UDP.
dolichyl-xylosyl-phosphate--protein xylosyltransferase
a dolichyl D-xylosyl phosphate + L-seryl-[protein] = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+).
indolylacetylinositol arabinosyltransferase
arabinosylindolylacetylinositol synthase
indole-3-acetyl-1D-myo-inositol + UDP-beta-L-arabinopyranose = (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside + H(+) + UDP.
flavonol-3-O-glycoside xylosyltransferase
Flavonol 3-O-glucoside, flavonol 3-O-galactoside and, more slowly, rutin, can act as acceptors.
a flavonol 3-O-glycoside + UDP-alpha-D-xylose = a flavonol 3-O-[beta-D-xylosyl-(1->2)-beta-D-glycoside] + H(+) + UDP.
NAD(+)--diphthamide ADP-ribosyltransferase
Dihtheria toxin and some other bacterial toxins catalyze this reaction, which inactivates translation elongation factor 2 (EF2).
The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria.
The relevant histidine of EF2 is His(715) in mammals, His(699) in yeast and His(600) in Pyrococcus horikoshii.
diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide.
NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase
NAD-azoferredoxin (ADPribose)transferase
NAD-dinitrogen-reductase ADP-D-ribosyltransferase
The combined action of this enzyme and EC 3.2.2.24 controls the activity level of nitrogenase (EC 1.18.6.1).
In the presence of ammonium, the product of nitrogenase, this enzyme covalently links an ADP-ribose moiety to a specific arginine residue of the dinitrogenase reductase component of nitrogenase, blocking its activity.
L-arginyl-[dinitrogen reductase] + NAD(+) = H(+) + N(omega)-alpha-(ADP-D-ribosyl)-L-arginyl-[dinitrogen reductase] + nicotinamide.
glycoprotein 2-beta-D-xylosyltransferase
Specific for N-linked oligosaccharides (N-glycans).
N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-alpha-D-xylose = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-[beta-D-Xyl-(1->2)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP.
uridine diphosphoxylose-xyloglucan 6alpha-xylosyltransferase
In association with EC 2.4.1.168 this enzyme brings about the synthesis of xyloglucan.
Concurrent transfers of glucose and xylose are necessary for this synthesis.
Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-(1->6)-D-xylosyl-D-glucose linkage.
uridine diphosphoxylose-zeatin xylosyltransferase
Does not act on UDP-glucose (cf. EC 2.4.1.103).
UDP-alpha-D-xylose + zeatin = H(+) + O-beta-D-xylosylzeatin + UDP.
xylogalacturonan beta-1,3-xylosyltransferase
The enzyme from Arabidopsis thaliana could transfer D-xylose from UDP-D-xylose onto oligogalacturonide acceptors.
The enzyme did not show significant activity with UDP-glucose, UDP-galactose, or UDP-N-acetyl-D-glucosamine as sugar donors.
Transfers a xylosyl residue from UDP-D-xylose to a D-galactose residue in xylogalacturonan, forming a beta-1,3-D-xylosyl-D-galactose linkage.
UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase
beta-glucoside alpha-1,3-xylosyltransferase
UDP-alpha-D-xylose:beta-D-glucoside 3-alpha-D-xylosyltransferase
3-O-(beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-L-seryl-[EGF-like domain protein] + H(+) + UDP.
lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
4-amino-4-deoxy-L-arabinose lipid A transferase
lipid A 4-amino-4-deoxy-L-arabinosyltransferase
undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
undecaprenyl phosphate-alpha-L-Ara4N transferase
Integral membrane protein present in the inner membrane of certain Gram negative endobacteria.
In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA.
In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules.
The Salmonella typhimurium enzyme can add arabinose units to both positions.
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + lipid IVA = lipid IIA + di-trans,octa-cis-undecaprenyl phosphate.
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + lipid A (E. coli) = beta-L-Ara4N-lipid A (E. coli) + di-trans,octa-cis-undecaprenyl phosphate.
2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A = (beta-L-Ara4N)2-(Kdo)2-lipid A + 2 di-trans,octa-cis-undecaprenyl phosphate.
No activity with S-methyl-5'-thioadenosine.
The catabolism of of 5'-methylthioadenosine in Pseudomonas aeruginosa involves deamination to S-methyl-5'-thioinosine (EC 3.5.4.31) and phosphorolysis to hypoxanthine.
phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.
decaprenyl-phosphate phosphoribosyltransferase
5-phospho-alpha-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase
5-phospho-alpha-D-ribose 1-pyrophosphate:decaprenyl phosphate 5-phosphoribosyltransferase
Has some activity with other polyprenyl phosphates.
5-phospho-alpha-D-ribose 1-diphosphate + H(+) + trans,octa-cis-decaprenyl phosphate = diphosphate + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose 5-phosphate.
galactan 5-O-arabinofuranosyltransferase
Isolated from Mycobacterium tuberculosis and Corynebacterium glutamicum.
These arabinofuranosyl groups form the start of an arabinofuranan chain as part of the of the cell wall in mycobacteria.
Adds an alpha-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-beta-D-arabinofuranose at the 5-O-position of the eighth, tenth and twelfth galactofuranose unit of the galactofuranan chain of [beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol.
arabinofuranan 3-O-arabinosyltransferase
Adds an alpha-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-beta-D-arabinofuranose at the 3-O-position of an alpha-(1->5)-arabinofuranan chain attached to a beta-(1->5)-galactofuranan chain.
transfer ribonucleic acid guanine(15) transglycosylase
Archaeal tRNAs contain the modified nucleoside archaeosine at position 15.
This archaeal enzyme catalyzes the exchange of guanine at position 15 of tRNA with the base preQ0, which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97).
7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine.
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin.
5-phospho-alpha-D-ribose 1-diphosphate + neamine = 5''-phosphoribostamycin + diphosphate.
cyanidin 3-O-galactoside 2''-O-xylosyltransferase
cyanidin 3-O-beta-D-galactoside + UDP-alpha-D-xylose = cyanidin 3-O-[beta-D-xylosyl-(1->2)-beta-D-galactoside] + H(+) + UDP.
anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
Isolated from the plants Matthiola incana (stock) and Arabidopsis thaliana (mouse-eared cress).
The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1->6)-glucoside and cyanidin 3-O-(6-acylglucoside).
There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside.
an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-xylose = an anthocyanidin 3-O-beta-D-sambubioside + 2 H(+) + UDP.
triphosphoribosyl-dephospho-CoA synthase
2'-(5''-triphosphoribosyl)-3-dephospho-CoA synthase
ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP.
The reaction involves the formation of a new alpha (1''->2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP.
The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61 to the apo-[acyl-carrier-protein] subunit (gamma-subunit) of EC 4.1.3.6 thus converting it from an apo-enzyme into a holo-enzyme.
Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66.
3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine.
undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
undecaprenyl-phosphate Ara4FN transferase
The enzyme shows no activity with UDP-4-amino-4-deoxy-beta-L-arabinose.
di-trans,octa-cis-undecaprenyl phosphate + UDP-4-deoxy-4-formamido-beta-L-arabinose = 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP.
beta-ribofuranosylphenol 5'-phosphate synthase
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase
beta-ribofuranosylaminobenzene 5'-phosphate synthase
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea.
It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea.
4-hydroxybenzoate + 5-phospho-alpha-D-ribose 1-diphosphate + H(+) = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate.
nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase
The enzyme is involved in the biosynthesis of phenolic cobamides in the Gram-positive bacterium Sporomusa ovata.
It can also transfer the phospho-D-ribosyl group to 4-methylphenol and 5,6-dimethylbenzimidazole.
The related EC 2.4.2.21 also transfers the phospho-D-ribosyl group from nicotinate D-ribonucleotide to 5,6-dimethylbenzimidazole, but shows no activity with 4-methylphenol or phenol.
nicotinate beta-D-ribonucleotide + phenol = H(+) + nicotinate + phenyl 5-phospho-alpha-D-ribofuranoside.
The enzyme from the plant Euonymus alatus also catalyzes the 3-O-D-xylosylation of other flavonols (e.g. quercetin, isorhamnetin, rhamnetin, myricetin, fisetin) with lower activity.
kaempferol + UDP-alpha-D-xylose = H(+) + kaempferol 3-O-beta-D-xyloside + UDP.
The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes.
The activity with CMP and UMP requires activation by cAMP.
AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate.
CMP + phosphate = alpha-D-ribose 1,5-bisphosphate + cytosine.
phosphate + UMP = alpha-D-ribose 1,5-bisphosphate + uracil.
The enzyme, found in plants and mosses, catalyzes the O-arabinosylation of hydroxyprolines in hydroxyproline-rich glycoproteins.
The enzyme acts on the first hydroxyproline in the motif Val-hydroxyPro-hydroxyPro-Ser.
trans-4-hydroxy-L-prolyl-[protein] + UDP-beta-L-arabinofuranose = H(+) + O-(beta-L-arabinofuranosyl)-trans-4-hydroxy-L-prolyl-[protein] + UDP.
sulfide-dependent adenosine diphosphate thiazole synthase
This iron dependent enzyme, found in most archaea, is involved in the biosynthesis of thiamine phosphate.
The homologous enzyme from plants and fungi (EC 2.4.2.60) uses an intrinsic cysteine as sulfur donor and, unlike the archaeal enzyme, is a single turn-over enzyme.
glycine + hydrogen sulfide + NAD(+) = ADP-5-ethyl-4-methylthiazole-2-carboxylate + H(+) + 3 H2O + nicotinamide.
cysteine-dependent adenosine diphosphate thiazole synthase
This iron dependent enzyme, found in fungi, plants, and some archaea, is involved in the thiamine phosphate biosynthesis pathway.
It is a single turn-over enzyme since the cysteine residue is not regenerated in vivo.
The homologous enzyme in archaea (EC 2.4.2.59) uses sulfide as sulfur donor.
[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 2 H(+) + 3 H2O + nicotinamide.
alpha-dystroglycan beta1,4-xylosyltransferase
This eukaryotic enzyme catalyzes a step in the biosynthesis of the glycan moiety of the membrane protein alpha-dystroglycan.
It is specific for the second ribitol 5-phosphate in the nascent glycan chain as acceptor.
3-O-[Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-xylose = 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP.
3-O-[(D-ribitylphospho)2-3-N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-O-6-phospho-alpha-D-mannosyl]-L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-[beta-D-xylosyl-(1->4)-(D-ribitylphospho)2-3-N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-O-6-phospho-alpha-D-mannosyl]-L-seryl-[protein] + H(+) + UDP.
3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-xylosyl-(1->3)-alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-L-seryl-[EGF-like domain protein] + H(+) + UDP.
The enzyme, found in animals and insects, xylosylates at the serine in the C-X-S-X-P-C motif of epidermal growth factor-like (EGF-like) domains.
The enzyme is bifunctional also being active with UDP-alpha-glucose as donor (EC 2.4.1.376).
L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP.
tRNA-guanosine(34) queuine transglycosylase
queuine(34) transfer ribonucleate ribosyltransferase
In eukaryotes and a small number of prokaryotes queuine is salvaged and incorporated into tRNA directly via a base-exchange reaction, replacing guanine.
guanosine(34) in tRNA + queuine = guanine + queuosine(34) in tRNA.
beta-galactoside alpha-(2,6)-sialyltransferase
beta-galactosamide alpha-2,6-sialyltransferase
beta-galactoside alpha-2,6-sialyltransferase
lactosylceramide alpha-2,6-N-sialyltransferase
The enzyme acts on the terminal non-reducing beta-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H(+).
CMP-N-acetyl-beta-neuraminate + N-acetyl-beta-lactosamine = CMP + H(+) + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine.
a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = CMP + H(+) + N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminide alpha-2,3-sialyltransferase
The enzyme recognizes the sequence beta-D-galactosyl-(1->3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids.
When acting on gangloside GM1a, it forms gangloside GD1a.
a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl derivative + CMP + H(+).
CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) = CMP + ganglioside GD1a (d18:1(4E)) + H(+).
alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
N-acetyl-alpha-D-galactosamine linked to threonine or serine is also an acceptor, when substituted at the 3-position.
a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl-(1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D-galactosaminyl derivative + CMP + H(+).
beta-galactoside alpha-2,3-sialyltransferase
The acceptor is Galbeta-(1->3)-GalNAc-R, where R is H, a threonine or serine residue in a glycoprotein, or a glycolipid.
a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP + H(+).
galactosyldiacylglycerol alpha-2,3-sialyltransferase
The beta-D-galactosyl residue of the oligosaccharide of glycoproteins may also act as acceptor.
a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + CMP-N-acetyl-beta-neuraminate = 1,2-diacyl-3-[3-(N-acetyl-alpha-D-neuraminyl)-beta-D-galactosyl]-sn-glycerol + CMP + H(+).
N-acetyllactosaminide alpha-2,3-sialyltransferase
cytidine monophosphoacetylneuraminate-beta-galactosyl(1->4)acetylglucosaminide alpha2->3-sialyltransferase
neolactotetraosylceramide alpha-2,3-sialyltransferase
The enzyme recognizes the sequence beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl (known as type 2 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids.
The enzyme from chicken brain was shown to act on neolactotetraosylceramide, producing ganglioside LM1.
a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + CMP + H(+).
a neolactoside nLc4Cer(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a neolactoside IV(3)-alpha-NeuAc-nLc4Cer(d18:1(4E)) + CMP + H(+).
alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide 6-alpha-sialyltransferase
alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase
cytidine monophosphoacetylneuraminate-(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide-alpha-2,6-sialyltransferase
Attaches N-acetylneuraminic acid in alpha-2,6-linkage to N-acetylgalactosamine only when present in the structure of alpha-N-acetylneuraminyl-(2->3)-beta-galactosyl-(1->3)-N-acetylgalactosaminyl-R, where R may be protein or p-nitrophenol.
an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+).
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase
cytidine monophosphoacetylneuraminate-ganglioside GM3
ganglioside GD3 synthetase sialyltransferase
an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+).
lactosylceramide alpha-2,3-sialyltransferase
cytidine monophosphoacetylneuraminate-lactosylceramide alpha2,3- sialyltransferase
cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase
a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = CMP + ganglioside GM3 (d18:1(4E)) + H(+).
N-acetylglucosaminide alpha-(2,6)-sialyltransferase
alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylglucosaminide 6-alpha-sialyltransferase
N-acetylglucosaminide (alpha 2->6)-sialyltransferase
Attaches N-acetylneuraminic acid in alpha-2,6-linkage to N-acetyl-beta-D-glucosamine.
The enzyme from rat liver also acts on beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl residues, but more slowly.
an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-beta-D-GlcNAc-R + CMP + H(+).
alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + CMP-N-acetyl-beta-neuraminate = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + CMP + H(+).
lipid IVA 3-deoxy-D-manno-octulosonic acid transferase
3-deoxy-D-manno-oct-2-ulosonic acid transferase
3-deoxy-manno-octulosonic acid transferase
The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.13).
The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus and Haemophilus influenzae catalyze the transfer of a single 3-D-manno-oct-2-ulosonate residue from CMP-3-D-manno-oct-2-ulosonate to lipid IVA.
The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes.
CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
a lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = an alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase
The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.12).
alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
an alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = an alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
(Kdo)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase
The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-octulosonate residues and generate genus-specific epitopes.
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
(Kdo)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase
The enzyme from Chlamydia psittaci transfers four KDO residues to lipid A, forming a branched tetrasaccharide with the structure alpha-KDO-(2,8)-[alpha-KDO-(2,4)]-alpha-KDO-(2,4)-alpha-KDO (cf. EC 2.4.99.12, EC 2.4.99.13 and EC 2.4.99.14).
alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-octulosonate = alpha-Kdo-(2->4)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP + H(+).
alpha1,4-glucan:maltose-1-P maltosyltransferase
The enzyme from from the bacterium Mycobacterium smegmatis is specific for maltose.
It has no activity with alpha-D-glucose.
[(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate.
S-adenosylmethionine:tRNA ribosyltransferase-isomerase
The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn.
It is part of the queuosine biosynthesis pathway.
7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-methionine.
dolichyl-diphosphooligosaccharide--protein glycotransferase
Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains.
The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2.
However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved.
Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine.
Occurs on the cytosolic face of the endoplasmic reticulum.
The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein].
alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein].
undecaprenyl-diphosphooligosaccharide--protein glycotransferase
A bacterial enzyme that has been isolated from Campylobacter jejuni and Campylobacter lari.
It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains.
Occurs on the external face of the plasma membrane.
The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine.
2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase
This multiunctional enzyme catalyzes both the removal of nicotinamide from NADP(+), forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming NAADP(+), a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes.
In addition, the enzyme also catalyzes EC 3.2.2.6.
NADP(+) + nicotinate = nicotinamide + nicotinate-adenine dinucleotide phosphate.
dolichyl-phosphooligosaccharide-protein glycotransferase
dolichyl-monophosphooligosaccharide-protein glycotransferase
The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins.
It is different from EC 2.4.99.18 which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes.
The enzyme participates in the N-glycosylation of proteins in some archaea.
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
Transferring alkyl or aryl groups, other than methyl groups
Will not accept larger prenyl diphosphates as efficient donors.
dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate.
thiamine:base 2-methyl-4-aminopyrimidine-5-methenyltransferase
Various bases and thiol compounds can act instead of pyridine.
pyridine + thiamine = 5-(2-hydroxyethyl)-4-methylthiazole + heteropyrithiamine.
The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components.
The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate.
However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase.
In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products.
In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme.
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate.
2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate.
4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine phosphate.
S-adenosyl-L-methionine = homoserine lactone + S-methyl-5'-thioadenosine.
Eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues.
ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine.
UDP-N-acetylglucosamine 1-carboxyvinyltransferase
phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase
pyruvate-UDP-acetylglucosamine transferase
pyruvate-uridine diphospho-N-acetylglucosamine transferase
pyruvate-uridine diphospho-N-acetyl-glucosamine transferase
pyruvic-uridine diphospho-N-acetylglucosaminyltransferase
UDP-N-acetylglucosamine 1-carboxyvinyl-transferase
UDP-N-acetylglucosamine enoylpyruvyltransferase
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine.
2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-ribitylamino)uracil + riboflavin.
Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate.
The enzyme will not accept larger prenyl diphosphates as efficient donors.
(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate.
The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea).
The enzyme exists in varying types of multifunctional proteins in different organisms.
The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate.
The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor.
The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant toward other amine acceptors, such as spermidine and cadaverine.
putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine.
aquocob(I)alamin vitamin B12s adenosyltransferase
ATP:cob(I)alamin Cobeta-adenosyltransferase
cob(I)yrinic acid a,c-diamide adenosyltransferase
The corrinoid adenosylation pathway comprises three steps: (i) reduction of Co(III) to Co(II) by a one-electron transfer.
This can occur non-enzymically in the presence of dihydroflavin nucleotides or reduced flavoproteins.
(ii) Co(II) is bound by corrinoid adenosyltransferase, resulting in displacement of the lower axial ligand by an aromatic residue.
The reduction potential of the 4-coordinate Co(II) intermediate is raised by ~250 mV compared with the free compound, bringing it to within physiological range.
This is followed by a second single-electron transfer from either free dihydroflavins or the reduced flavin cofactor of flavoproteins, resulting in reduction to Co(I).
(iii) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP, resulting in transfer of the deoxyadenosyl group and oxidation of the cobalt atom to Co(III) state.
Three types of corrinoid adenosyltransferases, not related by sequence, have been described.
In the anaerobic bacterium Salmonella enterica they are encoded by the cobA gene (a housekeeping enzyme involved in both adenosylcobalamin de novo biosynthesis and salvage), the pduO gene (involved in (S)-propane-1,2-diol utilization), and the eutT gene (involved in ethanolamine utilization).
Since EutT hydrolyzes triphosphate during catalysis, it is classified as a separate enzyme.
The mammalian enzyme belongs to the PduO type.
The enzyme can act on other corrinoids, such as cob(II)inamide.
2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate.
2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate.
2 ATP + 2 cob(II)inamide + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)inamide + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate.
A group of enzymes of broad specificity.
R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group.
Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
glutathione + RX = a halide anion + an S-substituted glutathione + H(+).
1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+).
3-phosphoshikimate 1-carboxyvinyltransferase
3-enol-pyruvoylshikimate-5-phosphate synthase
5-enolpyruvylshikimate-3-phosphate synthase
3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate.
(cis-prenyl)n-diphosphate + isopentenyl diphosphate = (cis-prenyl)(n+1)-diphosphate + diphosphate.
farnesyl-diphosphate farnesyltransferase
This microsomal enzyme catalyzes the first committed step in the biosynthesis of sterols.
In the absence of NAD(P)H, presqualene diphosphate (PSPP) is accumulated.
When NAD(P)H is present, presqualene diphosphate does not dissociate from the enzyme during the synthesis of squalene from farnesyl diphosphate (FPP).
High concentrations of FPP inhibit the production of squalene but not of PSPP.
2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene.
2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene.
The enzyme from mammalia is highly specific for spermidine, cf. EC 2.5.1.16 and EC 2.5.1.23.
S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine.
The enzyme has been originally characterized from the protist Euglena gracilis.
The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylsulfanyl)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency.
propane-1,3-diamine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + norspermidine + S-methyl-5'-thioadenosine.
N(6)-dimethylallyladenine + S-adenosyl-L-methionine = discadenine + H(+) + S-methyl-5'-thioadenosine.
tRNA-uridine aminocarboxypropyltransferase
3-[(3S)-3-amino-3-carboxypropyl]uridine (acp3U) is a highly conserved modification found in tRNA core region in bacteria and eukaryotes that confers thermal stability on tRNA.
The enzyme from the bacterium Escherichia coli catalyzes the modification of uridine(47) in the V-loop of tRNAs for Arg(2), Ile(1), Ile(2), Ile(2)v, Lys, Met, Phe, Val(2)A, and Val(2)B.
The human homologs DTWD1 and DTWD2 are responsible for acp3U formation at positions 20 and 20a, respectively, in the D-loop of several cytoplasmic tRNAs.
a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-thioadenosine.
S-adenosyl-L-methionine + uridine(47) in tRNA(Phe) = 3-[(3S)-3-amino-3-carboxypropyl]uridine(47) in tRNA(Phe) + H(+) + S-methyl-5'-thioadenosine.
The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage.
a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+).
adenylate dimethylallyltransferase (AMP-dependent)
Involved in the biosynthesis of cytokinins in plants.
Some isoforms from the plant Arabidopsis thaliana are specific for AMP while others also have the activity of EC 2.5.1.112.
AMP + dimethylallyl diphosphate = diphosphate + N(6)-(dimethylallyl)adenosine 5'-phosphate.
Will not use larger prenyl diphosphates as efficient donors.
dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate.
Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate.
all-trans-heptaprenyl-diphosphate synthase
This enzyme catalyzes the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7.
The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = all-trans-heptaprenyl diphosphate + 4 diphosphate.
ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
ditrans,polycis-undecaprenyl-diphosphate synthase
Undecaprenyl pyrophosphate synthase catalyzes the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall.
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate.
geranylgeranyl-diphosphate geranylgeranyltransferase
The enzyme condenses two molecules of geranylgeranyl diphosphate to give prephytoene diphosphate, followed by rearrangement of the cyclopropylcarbinyl intermediate to 15-cis-phytoene.
2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate.
dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-enyl)-L-tryptophan + diphosphate.
Will also use as acceptor aspulvinone G, a hydroxylated derivative of the complex phenolic pigment aspulvinone E.
aspulvinone E + 2 dimethylallyl diphosphate = aspulvinone H + 2 diphosphate.
trihydroxypterocarpan dimethylallyltransferase
dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan dimethyltransferase
dimethylallylpyrophosphate:3,6a,9-trihydroxypterocarpan dimethylallyltransferase
dimethylallylpyrophosphate:trihydroxypterocarpan dimethylallyl transferase
Part of the glyceollin biosynthesis system in soybean.
(6aS,11aS)-3,6a,9-trihydroxypterocarpan + dimethylallyl diphosphate = (6aS,11aS)-2-dimethylallyl-3,6a,9-trihydroxypterocarpan + diphosphate.
(6aS,11aS)-3,6a,9-trihydroxypterocarpan + dimethylallyl diphosphate = (6aS,11aS)-4-dimethylallyl-3,6a,9-trihydroxypterocarpan + diphosphate.
The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A.
The enzyme can act on nocardicin E, F, and G, producing isonocardicin A, B, and C, respectively.
However, the in vivo substrate is believed to be nocardicin G.
nocardicin G + S-adenosyl-L-methionine = H(+) + isonocardicin C + S-methyl-5'-thioadenosine.
nocardicin E + S-adenosyl-L-methionine = H(+) + isonocardicin A + S-methyl-5'-thioadenosine.
This enzyme, involved in the biosynthesis of ubiquinone, attaches a polyprenyl side chain to a 4-hydroxybenzoate ring, producing the first ubiquinone intermediate that is membrane bound.
The number of isoprenoid subunits in the side chain varies in different species.
The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency.
4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate.
4-hydroxybenzoate + all-trans-nonaprenyl diphosphate = 4-hydroxy-3-all-trans-nonaprenylbenzoate + diphosphate.
4-hydroxybenzoate + all-trans-hexaprenyl diphosphate = 4-hydroxy-3-all-trans-hexaprenylbenzoate + diphosphate.
4-hydroxybenzoate + all-trans-heptaprenyl diphosphate = 4-hydroxy-3-all-trans-heptaprenylbenzoate + diphosphate.
4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate.
4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-hydroxy-3-all-trans-decaprenylbenzoate + diphosphate.
phosphoglycerol geranylgeranyltransferase
(S)-3-O-geranylgeranylglyceryl phosphate synthase
Catalyzes the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria.
It catalyzes the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate.
The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 1.1.1.261, EC 2.5.1.42 and EC 2.7.7.67, which lead to the formation of CDP-unsaturated archaeol.
(2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate.
geranylgeranylglycerol-phosphate geranylgeranyltransferase
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase
Carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in archaea.
4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and alpha-glycerophosphate cannot act as prenyl-acceptor substrates.
The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 1.1.1.261, EC 2.5.1.41, which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP-unsaturated archaeol.
(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + diphosphate.
3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine.
The reaction of this bacterial enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: (1) NAD(+)-dependent dehydrogenation of either putrescine or spermidine. (2) Attack by water forming 4-aminobutanal (and releasing ammonia or propane-1,3-diamine, respectively). (3) Condensation of 4-aminobutanal with putrescine, which forms homospermidine and restores NAD(+).
Differs from the eukaryotic enzyme EC 2.5.1.45, which cannot use putrescine as donor of the aminobutyl group.
2 putrescine = NH4(+) + sym-homospermidine.
putrescine + spermidine = propane-1,3-diamine + sym-homospermidine.
homospermidine synthase (spermidine-specific)
The reaction occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: (1) NAD(+)-dependent dehydrogenation of spermidine to dehydrospermidine. (2) Attack by water forming 4-aminobutanal (and releasing propane-1,3-diamine). (3) Condensation of 4-aminobutanal with purescine, which forms homospermidine and restores NAD(+).
This enzyme is more specific than EC 2.5.1.44, which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group.
Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio).
The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity.
Catalyzes the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor.
The reaction occurs in four steps: NAD(+)-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d).
Hence the overall reaction is transfer of a 4-aminobutyl group.
For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor.
Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29.
[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine.
O(3)-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide)
Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors.
hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine.
O-succinyl-L-homoserine succinate-lyase (adding cysteine)
Also reacts with H2S and methanethiol as replacing agents, producing homocysteine and methionine, respectively.
In the absence of thiol, can also catalyze beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate.
O-acetylhomoserine aminocarboxypropyltransferase
O-acetyl-L-homoserine acetate-lyase (adding methanethiol)
Also reacts with other thiols and H2S, producing homocysteine or thioethers.
The name methionine synthase is more commonly applied to EC 2.1.1.13.
The enzyme from Saccharomyces cerevisiae also catalyzes the reaction of EC 2.5.1.47, but more slowly.
methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine.
hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-homocysteine.
O-acetyl-L-serine acetate-lyase (adding N(6)-substituted adenine)
The enzyme acts not only on zeatin but also on other N(6)-substituted adenines.
The reaction destroys their cytokinin activity and forms the corresponding 3-(adenin-9-yl)-L-alanine.
O-acetyl-L-serine + zeatin = acetate + H(+) + L-lupinate.
beta-pyrazolylalanine synthase (acetylserine)
O(3)-acetyl-L-serine acetate-lyase (adding pyrazole)
Highly specific for acetylserine and pyrazole.
O-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate + H(+).
O(3)-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl)
Brings about the biosynthesis of L-mimosine in Leucaena sp. and Mimosa.
3,4-dihydroxypyridine + O-acetyl-L-serine = 3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate + H(+).
O(3)-acetyl-L-serine acetate-lyase (adding uracil)
Both L-willardiine and L-isowillardiine are produced in the reaction.
O-acetyl-L-serine + uracil = 3-(uracil-1-yl)-L-alanine + acetate + H(+).
2-dehydro-3-deoxy-phosphoheptonate aldolase
2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
deoxy-D-arabino-heptulosonate-7-phosphate synthetase
D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
phospho-2-dehydro-3-deoxyheptonate aldolase
phospho-2-keto-3-deoxyheptanoate aldolase
phospho-2-keto-3-deoxyheptonate aldolase
D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate.
2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating)
2-dehydro-3-deoxy-phosphooctonate aldolase
2-keto-3-deoxy-8-phosphooctonic synthetase
3-deoxy-D-manno-octulosonate-8-phosphate synthase
3-deoxy-D-mannooctulosonate-8-phosphate synthetase
3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase
3-deoxyoctulosonic 8-phosphate synthetase
D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate.
N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating)
H2O + N-acetyl-D-mannosamine + phosphoenolpyruvate = N-acetylneuraminate + phosphate.
N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase
N-acetylneuraminate 9-phosphate synthetase
N-acylneuraminate-9-phosphate pyruvate-lyase (pyruvate-phosphorylating)
Acts on N-glycoloyl and N-acetyl-derivatives.
an N-acyl-D-mannosamine 6-phosphate + H2O + phosphoenolpyruvate = an N-acylneuraminate 9-phosphate + phosphate.
This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes.
Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein.
These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59.
The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic.
Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction.
(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein].
protein geranylgeranyltransferase type I
type I protein geranyl-geranyltransferase
This enzyme, along with EC 2.5.1.58 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes.
Catalyzes the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein.
These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58.
Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families.
The Zn(2+) is required for peptide, but not for isoprenoid, substrate binding.
geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein].
protein geranylgeranyltransferase type II
type II protein geranyl-geranyltransferase
This enzyme, along with EC 2.5.1.58 and EC 2.5.1.59, constitutes the protein prenyltransferase family of enzymes.
Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs.
Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP).
Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion.
(4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)methyltransferase (hydrolyzing)
The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active center.
The terminal tetrapyrrole is then hydrolyzed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues.
In the presence of a second enzyme, EC 4.2.1.75, which is often called cosynthase, the product is cyclized to form uroporphyrinogen III.
If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I.
H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+).
The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur.
The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate.
chlorophyllide a + H(+) + phytyl diphosphate = chlorophyll a + diphosphate.
fluoride + S-adenosyl-L-methionine = 5'-deoxy-5'-fluoroadenosine + L-methionine.
The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O(3)-acetyl-L-serine, in contrast with EC 2.5.1.47, which acts only on O(3)-acetyl-L-serine.
H(+) + hydrogen sulfide + O-phospho-L-serine = L-cysteine + phosphate.
N(2)-(2-carboxyethyl)arginine synthetase
Requires thiamine diphosphate and catalyzes the first step in the clavulanic-acid biosynthesis pathway.
The 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group.
D-glyceraldehyde 3-phosphate + L-arginine = H(+) + N(2)-(2-carboxyethyl)-L-arginine + phosphate.
Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage; it is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail.
The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis.
Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums.
2 dimethylallyl diphosphate = (R,R)-chrysanthemyl diphosphate + diphosphate.
The product of this reaction is an intermediate in the synthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of most features of the mycobacterial cell wall, including peptidoglycan, linker unit galactan and arabinan.
Neryl diphosphate can also act as substrate.
(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-farnesyl diphosphate + diphosphate.
Lavandulyl diphosphate is a monoterpene with a non-head-to-tail linkage; it is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail.
When this enzyme is incubated with prenyl diphosphate and isopentenyl diphosphate, it also forms the regular monoterpene geranyl diphosphate.
The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67) when prenyl diphosphate is the sole substrate.
2 dimethylallyl diphosphate = (R)-lavandulyl diphosphate + diphosphate.
In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly.
Along with EC 1.14.14.142 and EC 2.5.1.71, this enzyme forms part of the sophoraflavanone-G biosynthesis pathway.
(2S)-naringenin + dimethylallyl diphosphate = diphosphate + sophoraflavanone B.
leachianone-G 2''-dimethylallyltransferase
leachianone G 2''-dimethylallyltransferase
The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a prenyl group to the 2'' position of another prenyl group attached at postiion 8 of leachianone G.
The enzyme is specific for prenyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate.
Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly.
Along with EC 1.14.14.142 and EC 2.5.1.70, this enzyme forms part of the sophoraflavanone-G biosynthesis pathway.
dimethylallyl diphosphate + leachianone G = diphosphate + sophoraflavanone G.
Quinolinate synthase catalyzes the second step in the de novo biosynthesis of NAD(+) from aspartate in some bacteria, with EC 1.4.3.16 catalyzing the first step and EC 2.4.2.19 the third step.
In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme.
dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate.
O-phospho-L-seryl-tRNA:Cys-tRNA synthase
In organisms like Archaeoglobus fulgidus lacking EC 6.1.1.16 for the direct Cys-tRNA(Cys) formation, Cys-tRNA(Cys) is produced by an indirect pathway, in which EC 6.1.1.27 ligates O-phosphoserine to tRNA(Cys), and EC 2.5.1.73 converts the produced O-phospho-L-seryl-tRNA(Cys) to Cys-tRNA(Cys).
The SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism.
Methanosarcina mazei can use both pathways, the direct route using EC 6.1.1.16 and the indirect pathway with EC 6.1.1.27 and EC 2.5.1.73.
H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-cysteinyl-tRNA(Cys) + phosphate.
1,4-dihydroxy-2-naphthoate polyprenyltransferase
This enzyme catalyzes a step in the synthesis of menaquinone, in which the prenyl chain synthesized by polyprenyl diphosphate synthase is transferred to 1,4-dihydroxy-2-naphthoate (DHNA).
The bacterial enzyme is an inner membrane protein, with the C-terminus located in the periplasm.
It is highly specific for DHNA but not for a specific length of the prenyl chain.
1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-octaprenyl diphosphate + H(+) = 2-demethylmenaquinol-8 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-hexaprenyl diphosphate + H(+) = 2-demethylmenaquinol-6 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-heptaprenyl diphosphate + H(+) = 2-demethylmenaquinol-7 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-nonaprenyl diphosphate + H(+) = 2-demethylmenaquinol-9 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-decaprenyl diphosphate + H(+) = 2-demethylmenaquinol-10 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-undecaprenyl diphosphate + H(+) = 2-demethylmenaquinol-11 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-dodecaprenyl diphosphate + H(+) = 2-demethylmenaquinol-12 + CO2 + diphosphate.
1,4-dihydroxy-2-naphthoate + all-trans-tridecaprenyl diphosphate + H(+) = 2-demethylmenaquinol-13 + CO2 + diphosphate.
adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA.
It is highly specific for O-phospho-L-serine and sulfite.
The reaction proceeds through a dehydroalanine (2-aminoacrylic acid) intermediate.
The enzyme from Methanosarcina acetivorans is evolutionarily related to EC 4.2.3.1, but the reaction is more similar to that of EC 2.5.1.65.
H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate.
(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate.
This enzyme is required for correct xylem specification through regulation of the lifetime of the xylem elements.
S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + thermospermine.
This enzyme is more flexible toward the aromatic substrate than EC 2.5.1.34, but similar to that enzyme, accepts only dimethylallyl diphosphate as the prenyl donor.
dimethylallyl diphosphate + L-tryptophan = 7-(3-methylbut-2-enyl)-L-tryptophan + diphosphate.
The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis.
It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate.
The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate.
The enzyme is involved in the biosynthesis of C25-C25 membrane lipids.
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate.
hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
(all-trans)-hexaprenyl-diphosphate synthase
The enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and prenyl diphosphate.
(2E,6E,10E)-geranylgeranyl diphosphate + 2 isopentenyl diphosphate = all-trans-hexaprenyl diphosphate + 2 diphosphate.
hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
The enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and prenyl diphosphate.
(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = all-trans-hexaprenyl diphosphate + 3 diphosphate.
all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]
(2E,6E)-Farnesyl diphosphate and geranylgeranyl diphosphate are less effective as substrates than geranyl diphosphate.
The enzyme is involved in the synthesis of the side chain of menaquinone-9.
In Oryza sativa the enzyme SPS2 is involved in providing solanesyl diphosphate for plastoquinone-9 formation.
(2E)-geranyl diphosphate + 7 isopentenyl diphosphate = all-trans-nonaprenyl diphosphate + 7 diphosphate.
all-trans-nonaprenyl-diphosphate synthase [geranylgeranyl-diphosphate specific]
Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate.
The plant Arabidopsis thaliana has two different enzymes that catalyze this reaction.
SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains.
(2E,6E,10E)-geranylgeranyl diphosphate + 5 isopentenyl diphosphate = all-trans-nonaprenyl diphosphate + 5 diphosphate.
trans,polycis-decaprenyl diphosphate synthase
(2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase
The enzyme is involved in the biosynthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of essential mycobacterial cell wall components, such as the mycolyl-arabinogalactan-peptidoglycan complex and lipoarabinomannan.
(2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate + 7 diphosphate.
ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation.
The yeast Saccharomyces cerevisiae has two different enzymes that catalyze this reaction.
Rer2p synthesizes a well-defined family of polyprenols of 13-18 isoprene residues with dominating C80 (16 isoprene residues) extending to C120, while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits.
The enzyme from Arabidopsis thaliana catalyzes the formation of polyprenyl diphosphates with predominant carbon number C120.
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate.
trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific]
Highest activity with (2Z,6E)-farnesyl diphosphate as allylic substrate.
Broad product specificity with the major product being dodecaprenyl diphosphate.
Synthesizes even C70 prenyl diphosphate as the maximum chain-length product.
(2Z,6E)-farnesyl diphosphate + 9 isopentenyl diphosphate = di-trans,nona-cis-dodecaprenyl diphosphate + 9 diphosphate.
(2Z,6E)-farnesyl diphosphate + 10 isopentenyl diphosphate = di-trans,deca-cis-tridecaprenyl diphosphate + 10 diphosphate.
(2Z,6E)-farnesyl diphosphate + 11 isopentenyl diphosphate = di-trans,undeca-cis-tetradecaprenyl diphosphate + 11 diphosphate.
tritrans,polycis-undecaprenyl-diphosphate synthase [geranylgeranyl-diphosphate specific]
This enzyme is involved in the biosynthesis of the glycosyl carrier lipid in some archaebacteria.
Unlike EC 2.5.1.31, its counterpart in most bacteria, it prefers geranylgeranyl diphosphate to farnesyl diphosphate as the allylic substrate, resulting in production of a tritrans,polycis variant of undecaprenyl diphosphate.
geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate.
all-trans-octaprenyl-diphosphate synthase
This enzyme catalyzes the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8.
The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate = all-trans-octaprenyl diphosphate + 5 diphosphate.
all-trans-decaprenyl-diphosphate synthase
This enzyme catalyzes the condensation reactions resulting in the formation of all-trans-decaprenyl diphosphate, the isoprenoid side chain of ubiquinone-10 and menaquinone-10.
The enzyme adds seven isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = all-trans-decaprenyl diphosphate + 7 diphosphate.
This enzyme, originally characterized from wild tomato, specifically forms (2Z,6Z)-farnesyl diphosphate via neryl diphosphate and isopentenyl diphosphate.
In wild tomato it is involved in the biosynthesis of several sesquiterpenes.
dimethylallyl diphosphate + 2 isopentenyl diphosphate = (2Z,6Z)-farnesyl diphosphate + 2 diphosphate.
The enzyme is involved in shikonin biosynthesis.
It has a strict substrate specificity for geranyl diphosphate.
(2E)-geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-hydroxybenzoate + diphosphate.
This enzyme, isolated from the marine bacterium Salinispora tropica, catalyzes an early step in the pathway leading to biosynthesis of the proteosome inhibitor salinosporamide A.
The enzyme is very similar to EC 2.5.1.63 but does not accept fluoride.
chloride + S-adenosyl-L-methionine = 5'-chloro-5'-deoxyadenosine + L-methionine.
Involved in the biosynthesis of the polysaccharide xanthan.
30-40% of terminal mannose residues of xanthan have a 4,6-O-(1-carboxyethan-1,1-diyl) ketal group.
It also acts on the 6-O-acetyl derivative of the inner mannose unit.
beta-D-Man-(1->4)-beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + phosphoenolpyruvate = 4,6-Me(COOH)C-beta-D-Man-(1->4)-beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + phosphate.
Typical of Staphylococcus aureus and some other bacteria such as Heliobacillus sp.
2 (2E,6E)-farnesyl diphosphate = 15-cis-4,4'-diapophytoene + 2 diphosphate.
The enzyme requires a divalent metal ion, the highest activity values are observed in the presence of Mn(2+) and CO(2+) (10 mM).
2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose + H2O + phosphoenolpyruvate = phosphate + pseudaminate.
Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase
The enzyme is responsible for pyruvylation of subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa.
fumigaclavine A dimethylallyltransferase
Fumigaclavine C is an ergot alkaloid produced by some fungi of the Trichocomaceae family.
Activity does not require any metal ions.
dimethylallyl diphosphate + fumigaclavine A = diphosphate + fumigaclavine C.
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + H2O + phosphoenolpyruvate = N,N-diacetyllegionaminate + phosphate.
geranylpyrophosphate--olivetolic acid geranyltransferase
The enzyme can also use neryl diphosphate as substrate, forming cannabinerolate.
(2E)-geranyl diphosphate + olivetolate = cannabigerolate + diphosphate.
Unlike EC 2.5.1.21, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme.
This compound is then converted into either squalene (by EC 1.3.1.96) or botryococcene (EC 1.3.1.97).
2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate.
agmatine/cadaverine aminopropyl transferase
triamine/agmatine aminopropyltransferase
The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria.
The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency.
The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency.
agmatine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + N(1)-aminopropylagmatine + S-methyl-5'-thioadenosine.
7,8-dihydropterin-6-yl-methyl-4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase
The enzyme, which has been studied in the archaeon Methanocaldococcus jannaschii, is involved in the biosynthesis of tetrahydromethanopterin.
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate = diphosphate + N-[(7,8-dihydropterin-6-yl)methyl]-4-(beta-D-ribofuranosyl)aniline 5'-phosphate.
The enzyme from the fungus Aspergillus fumigatus can also prenylate other tryptophan-containing cyclic dipeptides.
Prenylation occurs mainly at C-2, but also at C-3.
Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, cyclotryprostatins, spirotryprostatins, fumitremorgins and verruculogen.
brevianamide F + dimethylallyl diphosphate = diphosphate + tryprostatin B.
Catalyzes the last step in the biosynthetic pathway of the indole alkaloid fumitremorgin A.
The enzyme from the fungus Neosartorya fischeri is also active with fumitremorgin B and 12alpha,13alpha-dihydroxyfumitremorgin C.
dimethylallyl diphosphate + verruculogen = diphosphate + fumitremorgin A.
2-(3-amino-3-carboxypropyl)histidine synthase
Modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical.
The enzyme is present in archae and eukaryotes but not in eubacteria.
L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine.
brevianamide F prenyltransferase (deoxybrevianamide E-forming)
brevianamide F reverse prenyltransferase
The enzyme from the fungus Aspergilus sp. MF297-2 is specific for brevianamide F, while the enzyme from Aspergillus versicolor accepts a broad range of trytophan-containing cyclic dipeptides.
Involved in the biosynthetic pathways of several indole alkaloids such as paraherquamides and malbrancheamides.
brevianamide F + dimethylallyl diphosphate = deoxybrevianamide E + diphosphate.
12alpha,13alpha-dihydroxyfumitremorgin C prenyltransferase
The enzyme from the fungus Aspergillus fumigatus also shows some activity with fumitremorgin C.
12alpha,13alpha-dihydroxyfumitremorgin C + dimethylallyl diphosphate = diphosphate + fumitremorgin B.
4-hydroxyphenylpyruvate 3-dimethylallyltransferase
The enzyme's product feeds into the biosynthesis of the aminocoumarin antibiotics clorobiocin and novobiocin.
3-(4-hydroxyphenyl)pyruvate + dimethylallyl diphosphate = 3-dimethylallyl-4-hydroxyphenylpyruvate + diphosphate.
adenylate dimethylallyltransferase (ADP/ATP-dependent)
The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP.
Other isoforms, such as IPT1 from Arabidopsis thaliana and the enzyme from the common hop, Humulus lupulus, also have a lower activity with AMP (cf. EC 2.5.1.27).
ADP + dimethylallyl diphosphate = diphosphate + N(6)-(dimethylallyl)adenosine 5'-diphosphate.
ATP + dimethylallyl diphosphate = diphosphate + N(6)-(dimethylallyl)adenosine 5'-triphosphate.
[CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase
CysO-thiocarboxylate-dependent cysteine synthase
The enzyme participates in an alternative pathway for L-cysteine biosynthesis that involves a protein-bound thiocarboxylate as the sulfide donor.
The enzyme from the bacterium Mycobacterium tuberculosis also has very low activity with O(3)-acetyl-L-serine (cf. EC 2.5.1.65).
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + O-phospho-L-serine = [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-Cys + phosphate.
tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase
The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases.
This modification is essential for translational reading-frame maintenance.
The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNA(Phe).
4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-methyl-5'-thioadenosine.
Involved in the biosynthesis of the vitamin E tocopherols.
While the enzyme from the cyanobacterium Synechocystis PCC 6803 has an appreciable activity with geranylgeranyl diphosphate (EC 2.5.1.116), the enzyme from the plant Arabidopsis thaliana has only a low activity with that substrate.
H(+) + homogentisate + phytyl diphosphate = 2-methyl-6-phytyl-1,4-benzene-1,4-diol + CO2 + diphosphate.
Involved in the biosynthesis of the vitamin E, tocotrienols.
While the enzyme from the bacterium Synechocystis PCC 6803 has higher activity with phytyl diphosphate (EC 2.5.1.115) the enzymes from barley, rice and wheat have only a low activity with that substrate.
(2E,6E,10E)-geranylgeranyl diphosphate + H(+) + homogentisate = 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2 + diphosphate.
Part of the biosynthesis pathway of plastoquinol-9.
The enzymes purified from the plant Arabidopsis thaliana and the alga Chlamydomonas reinhardtii are also active in vitro with unsaturated C10-C20 prenyl diphosphates, producing main products that are not decarboxylated.
all-trans-nonaprenyl diphosphate + H(+) + homogentisate = 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2 + diphosphate.
beta-(isoxazolin-5-on-2-yl)-L-alanine synthase
The enzyme from the plants Lathyrus odoratus (sweet pea) and L.sativus (grass pea) also forms 3-(5-oxoisoxazolin-4-yl)-L-alanine in vitro (cf. EC 2.5.1.119).
However, only 3-(5-oxoisoxazolin-2-yl)-L-alanine is formed in vivo.
3-(5-oxoisoxazolin-2-yl)-L-alanine is the biosynthetic precursor of the neurotoxin N(3)-oxalyl-L-2,3-diaminopropanoic acid, the cause of lathyrism.
Closely related and possibly identical to EC 2.5.1.47 and EC 2.5.1.51.
isoxazolin-5-one + O-acetyl-L-serine = 3-(5-oxoisoxazolin-2-yl)-L-alanine + acetate + H(+).
beta-(isoxazolin-5-on-4-yl)-L-alanine synthase
3-(5-oxoisoxazolin-4-yl)-L-alanine is an antifungal antibiotic produced by the bacterium Streptomyces platensis.
The enzymes from the plants Lathyrus odoratus (sweet pea), L.sativus (grass pea) and Citrullus vulgaris (watermelon) that catalyze EC 2.5.1.118 also catalyze this reaction in vitro, but not in vivo.
isoxazolin-5-one + O-acetyl-L-serine = 3-(5-oxoisoxazolin-4-yl)-L-alanine + acetate + H(+).
S-adenosyl-L-methionine acts as both a radical generator and as the source of the transferred adenosyl group.
3-[(1-carboxyvinyl)-oxy]benzoate + H2O + S-adenosyl-L-methionine = 6-amino-6-deoxyfutalosine + H(+) + hydrogencarbonate + L-methionine.
5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase
dihydrophenazine-1-carboxylate dimethylallyltransferase
The enzyme is involved in the biosynthesis of prenylated phenazines by the bacterium Streptomyces anulatus.
It is specific for both prenyl diphosphate and 5,10-dihydrophenazine 1-carboxylate.
5,10-dihydrophenazine 1-carboxylate + dimethylallyl diphosphate = 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate + diphosphate.
The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.
dimethylallyl diphosphate + L-tyrosine = 4-O-dimethylallyl-L-tyrosine + diphosphate.
Isolated from the bacterium Streptomyces cinnamonensis.
In vitro the enzyme also forms traces of 3-geranylflaviolin.
(2E)-geranyl diphosphate + flaviolin = 3-linalylflaviolin + diphosphate.
6-linalyl-2-O,3-dimethylflaviolin synthase
6-(3,7-dimethylocta-1,6-dien-3-yl)-5,7-dihydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase
The enzyme is involved in biosynthesis of the polyketide-isoprenoid furaquinocin D in the bacterium Streptomyces sp. KO-3988.
It catalyzes the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 6-linalyl-2-O,3-dimethylflaviolin and 7-O-geranyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.125) in a 10:1 ratio.
(2E)-geranyl diphosphate + 2-O,3-dimethylflaviolin = 6-linalyl-2-O,3-dimethylflaviolin + diphosphate.
7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase
The enzyme is involved in furaquinocin biosynthesis in the bacterium Streptomyces sp. KO-3988.
It catalyzes the transfer of a geranyl group to 2-O,3-dimethylflaviolin to yield 7-O-geranyl-2-O,3-dimethylflaviolin and 6-linalyl-2-O,3-dimethylflaviolin (cf. EC 2.5.1.124) in a 1:10 ratio.
(2E)-geranyl diphosphate + 2-O,3-dimethylflaviolin + H(+) = 7-O-geranyl-2-O,3-dimethylflaviolin + diphosphate.
The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity).
The long-chain polyamines stabilize double-stranded DNA at high temperatures.
In contrast to EC 2.5.1.127, this enzyme does not accept norspermine as a substrate.
norspermidine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + norspermine + S-methyl-5'-thioadenosine.
The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity).
In contrast to EC 2.5.1.23 and EC 2.5.1.126, this enzyme shows no activity with propane-1,3-diamine.
norspermine + S-adenosyl 3-(methylsulfanyl)propylamine = caldopentamine + 2 H(+) + S-methyl-5'-thioadenosine.
N(4)-bis(aminopropyl)spermidine synthase
The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N(4)-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature.
When spermine is used as substrate, the enzyme forms N(4)-aminopropylspermine.
2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine.
The enzyme produces the modified flavin cofactor prenylated FMNH2, which is required by EC 4.1.1.98 and EC 4.1.1.102.
The enzyme acts as a flavin prenyltransferase, linking a prenyl moiety to the flavin N-5 and C-6 atoms and thus adding a fourth non-aromatic ring to the flavin isoalloxazine group.
dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2.
2-carboxy-1,4-naphthoquinone phytyltransferase
1,4-diketo-2-naphthoate phytyltransferase
1,4-dioxo-2-naphthoate phytyltransferase
This enzyme, founds in plant and cyanobacteria, catalyzes a step in the synthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I.
The enzyme catalyzes the transfer of the phytyl chain synthesized by EC 1.3.1.83 to 2-carboxy-1,4-naphthoquinone.
1,4-dioxo-2-naphthoate + H(+) + phytyl diphosphate = CO2 + demethylphylloquinone + diphosphate.
(4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase
The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.
[5-(aminomethyl)furan-3-yl]methyl diphosphate + gamma-L-glutamyltyramine = (4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine + diphosphate.
3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase
2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase
The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (KDN).
The human sialic acid synthase (EC 2.5.1.57) is also able to catalyze the reaction.
KDN is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
D-mannose 6-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate 9-phosphate + phosphate.
The enzyme catalyzes the addition of a geranylgeranyl hydrophobic chain to bacteriochlorophyllide a via an ester bond with the 17-propionate residue.
The side chain is later modified to a phytyl chain, resulting in bacteriochlorophyll a.
(2E,6E,10E)-geranylgeranyl diphosphate + bacteriochlorophyllide a + H(+) = diphosphate + geranylgeranyl-bacteriochlorophyllide a.
cystathionine beta-synthase (O-acetyl-L-serine)
O-acetylserine dependent cystathionine beta-synthase
The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22).
L-homocysteine + O-acetyl-L-serine = acetate + H(+) + L,L-cystathionine.
validamine 7-phosphate valienyltransferase
The enzyme, characterized from several Streptomyces strains, is involved in the biosynthesis of the antifungal agent validamycin A.
GDP-valienol + validamine 7-phosphate = GDP + H(+) + validoxylamine A 7'-phosphate.
2-acylphloroglucinol 4-prenyltransferase
The enzyme, characterized from hop (Humulus lupulus), acts on phlorisovalerophenone, phlormethylbutanophenone, and phlorisobutanophenone during the synthesis of bitter acids.
It also acts with much lower activity on naringenin chalcone.
Forms a complex with EC 2.5.1.137 which catalyzes additional prenylation reactions.
a 2-acylphloroglucinol + dimethylallyl diphosphate = a 2-acyl-4-prenylphloroglucinol + diphosphate.
dimethylallyl diphosphate + phlorisovalerophenone = 4-prenylphlorisovalerophenone + diphosphate.
2-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one + dimethylallyl diphosphate = 4-prenylphlormethylbutanophenone + diphosphate.
dimethylallyl diphosphate + phlorisobutanophenone = 4-prenylphlorisobutanophenone + diphosphate.
2',4,4',6'-tetrahydroxychalcone + dimethylallyl diphosphate = desmethylxanthohumol + diphosphate.
2-acyl-4-prenylphloroglucinol 6-prenyltransferase
The enzyme, characterized from hop (Humulus lupulus), catalyzes two successive prenylations of a 2-acyl-4-prenylphloroglucinol during the synthesis of bitter acids.
Forms a complex with EC 2.5.1.136 which catalyzes the initial prenylation of the substrates.
a 2-acyl-4-prenylphloroglucinol + dimethylallyl diphosphate = a 2-acyl-4,6-diprenylphloroglucinol + diphosphate.
a 2-acyl-4,6-diprenylphloroglucinol + dimethylallyl diphosphate = a 2-acyl-4,6,6-triprenylphloroglucinol + diphosphate.
4-prenylphlorisobutanophenone + dimethylallyl diphosphate = deoxycohumulone + diphosphate.
4-prenylphlormethylbutanophenone + dimethylallyl diphosphate = deoxyadlupulone + diphosphate.
4-prenylphlorisovalerophenone + dimethylallyl diphosphate = deoxyhumulone + diphosphate.
deoxycohumulone + dimethylallyl diphosphate = colupulone + diphosphate + H(+).
deoxyadlupulone + dimethylallyl diphosphate = adlupulone + diphosphate + H(+).
deoxyhumulone + dimethylallyl diphosphate = diphosphate + H(+) + lupulone.
The enzyme, characterized from the plant Citrus limon, is specific for geranyl diphosphate as a prenyl donor.
It also has low activity with the coumarins 5,7-dihydroxycoumarin and 5-methoxy-7-hydroxycoumarin.
(2E)-geranyl diphosphate + umbelliferone = 8-geranylumbelliferone + diphosphate.
(2E)-geranyl diphosphate + esculetin = 8-geranylesculetin + diphosphate.
umbelliferone 6-dimethylallyltransferase
The enzyme from parsley (Petroselinum crispum) is specific for umbelliferone and dimethylallyl diphosphate.
A minor product is osthenol, which is produced by transfer of the dimethylallyl group to C-8 of umbelliferone.
dimethylallyl diphosphate + umbelliferone = demethylsuberosin + diphosphate.
dimethylallyl diphosphate + umbelliferone = diphosphate + osthenol.
N-(2-amino-2-carboxyethyl)-L-glutamate synthase
L-glutamate + O-phospho-L-serine = H(+) + N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate.
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a.
In organisms that produce heme a, the enzyme forms a complex with heme a synthase.
In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o.
Isolated from the plant Solanum lycopersicum (tomato).
dimethylallyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + nerylneryl diphosphate.
pyridinium-3,5-biscarboxylic acid mononucleotide synthase
nicotinic acid adenine dinucleotide carboxylase/hydrolase
This enzyme, found in the bacterium Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor.
It carboxylates the pyridinium ring of deamido-NAD(+) and cleaves the phosphoanhydride bond to release AMP and generate pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN).
deamido-NAD(+) + hydrogencarbonate = AMP + 2 H(+) + pyridinium-3,5-dicarboxylate mononucleotide.
S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent)
In plants, the activity is catalyzed by a chloroplastic enzyme that plays an important role in chloroplast function and is essential for light-dependent redox regulation within the chloroplast.
The bacterial enzyme also catalyzes the activity of EC 2.5.1.47.
O-acetyl-L-serine + thiosulfate = acetate + H(+) + S-sulfo-L-cysteine.
phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
This bacterial enzyme, which is associated with the membrane, catalyzes the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the prospective N-terminal cysteine of a prolipoprotein, the first step in the formation of mature triacylated lipoproteins.
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate.
3-geranyl-3-[(Z)-2-isocyanoethenyl]indole synthase
(2E)-geranyl diphosphate + 3-[(Z)-2-isocyanoethenyl]-1H-indole = 3-geranyl-3-[(Z)-2-isocyanoethenyl]-1H-indole + diphosphate.
5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase
The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria.
FO is also produced by some cyanobacteria and eukaryotes.
The enzyme, which forms a complex with EC 4.3.1.32 is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to initiate the reaction.
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine.
The enzyme, characterized from the green microalga Botryococcus braunii race L, in involved in biosynthesis of (14E,18E)-lycopadiene.
In vitro, the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyze the condensation of two different substrate molecules, forming chimeric products.
However, the use of these alternative substrates is not significant in vivo.
2 (2E,6E,10E)-geranylgeranyl diphosphate + H(+) + NADPH = all-trans-lycopaoctaene + 2 diphosphate + NADP(+).
H(+) + NADPH + 2 phytyl diphosphate = (14E,18E)-lycopadiene + 2 diphosphate + NADP(+).
lycopene elongase/hydratase (flavuxanthin-forming)
The enzyme, characterized from the bacterium Corynebacterium glutamicum, is bifunctional.
It catalyzes the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2, as well as the hydroxylation of the new isoprene unit.
The enzyme acts at both ends of the substrate, forming the C50 carotenoid flavuxanthin via the C45 intermediate nonaflavuxanthin.
A + all-trans-lycopene + dimethylallyl diphosphate + H2O = AH2 + diphosphate + nonaflavuxanthin.
A + dimethylallyl diphosphate + H2O + nonaflavuxanthin = AH2 + diphosphate + flavuxanthin.
lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming)
The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, is bifunctional.
It catalyzes the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule.
The enzyme acts at both ends of the substrate, and combined with the action of EC 1.3.99.37, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin.
all-trans-lycopene + dimethylallyl diphosphate + H2O = dihydroisopentenyldehydrorhodopin + diphosphate.
dimethylallyl diphosphate + H2O + isopentenyldehydrorhodopin = dihydrobisanhydrobacterioruberin + diphosphate.
This mammalian enzyme, which is cytosolic, can bind internalized alkylcobalamins and process them to cob(I)alamin using the thiolate of glutathione for nucleophilic displacement.
The product remains bound to the protein, and, following its oxidation to cob(II)alamin, is transferred by the enzyme, together with its interacting partner MMADHC, directly to downstream enzymes involved in adenosylcobalamin and methylcobalamin biosynthesis.
In addition to its dealkylase function, the enzyme also catalyze an entirely different decyanase reaction with cyanocobalamin (cf. EC 1.16.1.6).
an R-cob(III)alamin + apo-[alkylcobalamin reductase] + glutathione = an S-substituted glutathione + cob(I)alamin-[alkylcobalamin reductase] + H(+).
apo-[alkylcobalamin reductase] + glutathione + methylcob(III)alamin = cob(I)alamin-[alkylcobalamin reductase] + H(+) + S-methyl glutathione.
adenosylcob(III)alamin + apo-[alkylcobalamin reductase] + glutathione = cob(I)alamin-[alkylcobalamin reductase] + H(+) + S-adenosylglutathione.
The enzyme, characterized from the bacterium Staphylococcus aureus, participates in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.
D-histidine + S-adenosyl-L-methionine = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + S-methyl-5'-thioadenosine.
The enzyme, characterized from the bacterial pathogen Mycobacterium tuberculosis, produces 1-tuberculosinyladenosine, an unusual terpene nucleoside that acts as a phagolysosome disruptor by neutralizing the pH, resulting in swelling of the lysosome and obliteration of its multilamellar structure.
adenosine + H(+) + tuberculosinyl diphosphate = 1-tuberculosinyladenosine + diphosphate.
H2O + tuberculosinyl diphosphate = diphosphate + tuberculosinol.
H2O + tuberculosinyl diphosphate = (13R)-edaxadiene + diphosphate.
H2O + tuberculosinyl diphosphate = (13S)-edaxadiene + diphosphate.
glycerol-1-phosphate heptaprenyltransferase
Part of the pathway in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales.
all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate.
Also acts on L-tyrosine, L-phenylalanine and L-tryptophan.
This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate.
2-aminobutanoate acts slowly instead of alanine.
2-oxoglutarate + L-alanine = L-glutamate + pyruvate.
2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-glutamate.
2-oxoglutarate + glycine = glyoxylate + L-glutamate.
L-phenylalanine can act instead of L-tyrosine.
The mitochondrial enzyme may be identical with EC 2.6.1.1.
The three isoenzymic forms are interconverted by EC 3.4.22.32 and EC 3.4.22.33.
The enzyme can also catalyze the final step in the methionine-salvage pathway of Klebsiella pneumoniae.
2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate.
2-oxoglutarate + L-phenylalanine = 3-phenylpyruvate + L-glutamate.
Differs from EC 2.6.1.42 in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine.
2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate.
kynurenine--oxoglutarate aminotransferase
The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate.
2-oxoglutarate + 3-hydroxy-L-kynurenine = H2O + L-glutamate + xanthurenate.
2,5-diaminoglutarate can act instead of diaminopentanoate.
2-oxoglutarate + L-ornithine = 5-amino-2-oxopentanoate + L-glutamate.
imidazolylacetolphosphate aminotransferase
2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
Also acts on L-ornithine and N(2)-succinyl-L-ornithine.
2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde.
a 2-oxocarboxylate + L-alanine = an L-alpha-amino acid + pyruvate.
ornithine--alpha-ketoglutarate aminotransferase
ornithine--ketoglutarate aminotransferase
a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-glutamate 5-semialdehyde.
2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-semialdehyde.
a 2-oxocarboxylate + L-asparagine = 2-oxosuccinamate + an L-alpha-amino acid.
2-oxoglutarate + L-asparagine = 2-oxosuccinamate + L-glutamate.
L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine.
glutamine--fructose-6-phosphate transaminase (isomerizing)
glucosamine-6-phosphate isomerase (glutamine-forming)
L-glutamine-D-fructose-6-phosphate amidotransferase
Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate.
succinyldiaminopimelate aminotransferase
2-oxoglutarate + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate.
Omega-amino acid--pyruvate aminotransferase
3-oxopropanoate + L-alanine = beta-alanine + pyruvate.
4-aminobutyrate--2-oxoglutarate transaminase
beta-alanine--oxoglutarate aminotransferase
Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate. cf. EC 2.6.1.120.
2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde.
The enzyme from thermophilic Bacillus species acts on many D-amino acids with D-alanine and D-2-aminobutyrate as the best amino donors.
It can similarly use any of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and 2-oxobutyrate among the best.
The enzyme from some other sources has a broader specificity.
2-oxoglutarate + D-alanine = D-glutamate + pyruvate.
(S)-3-amino-2-methylpropionate transaminase
(S)-3-amino-2-methylpropionate aminotransferase
beta-aminoisobutyrate-alpha-ketoglutarate transaminase
Also acts on beta-alanine and other omega-amino acids having carbon chains between 2 and 5.
The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
The enzyme participates in a degradation pathway of trans-4-hydroxy-L-proline, a compound that contributes to the stability of the collagen triple helix.
Oxaloacetate can replace 2-oxoglutarate.
This enzyme may be identical with EC 2.6.1.1.
(4S)-4-hydroxy-L-glutamate + 2-oxoglutarate = (4R)-4-hydroxy-2-oxoglutarate + L-glutamate.
Also acts on 3,5-dichloro-, 3,5-dibromo- and 3-iodo-L-tyrosine, thyroxine and triiodothyronine.
2-oxoglutarate + 3,5-diiodo-L-tyrosine = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + L-glutamate.
Acts on monoiodotyrosine, diiodotyrosine, triiodothyronine, thyroxine and dinitrotyrosine (unlike EC 2.6.1.24, which does not act on dinitrotyrosine).
Pyruvate or oxaloacetate can act as acceptor.
2-oxoglutarate + 3,3',5-triiodo-L-thyronine = 3,5,3'-triiodothyropyruvate + L-glutamate.
Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids.
2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-glutamate.
tryptophan--phenylpyruvate aminotransferase
Valine, leucine and isoleucine can replace tryptophan as amino donor.
3-phenylpyruvate + L-tryptophan = indole-3-pyruvate + L-phenylalanine.
2-oxoglutarate + an alkane-alpha,omega-diamine = an omega-aminoaldehyde + L-glutamate.
pyridoxamine + pyruvate = L-alanine + pyridoxal.
Pyridoxamine--oxaloacetate aminotransferase
oxaloacetate + pyridoxamine = L-aspartate + pyridoxal.
valine--3-methyl-2-oxovalerate transaminase
valine--3-methyl-2-oxovalerate aminotransferase
(S)-3-methyl-2-oxopentanoate + L-valine = 3-methyl-2-oxobutanoate + L-isoleucine.
dTDP-4-amino-4,6-dideoxy-D-glucose transaminase
dTDP-4-amino-4,6-dideoxy-D-glucose aminotransferase
TDP-4-keto-6-deoxy-D-glucose transaminase
thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase
thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase
2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate.
UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase
UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose transaminase
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase
The enzyme is involved in biosynthesis of UDP-N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species and O-linked glycosylation of certain L-serine residues in Neisseria species.
2-oxoglutarate + UDP-N-acetylbacillosamine = L-glutamate + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.
glycine + oxaloacetate = glyoxylate + L-aspartate.
The product, (S)-2-amino-6-oxohexanoate, is converted into the intramolecularly dehydrated form, 1-piperideine 6-carboxylate.
2-oxoglutarate + L-lysine = (S)-2-amino-6-oxohexanoate + L-glutamate.
2-aminoethylphosphonate--pyruvate transaminase
(2-aminoethyl)phosphonate--pyruvate aminotransferase
(2-aminoethyl)phosphonic acid aminotransferase
2-aminoethylphosphonate aminotransferase
2-aminoethylphosphonate--pyruvate aminotransferase
2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
(2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde.
2-oxoglutarate + L-histidine = 3-(imidazol-5-yl)pyruvate + L-glutamate.
2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate.
(R)-3-amino-2-methylpropionate--pyruvate transaminase
(R)-3-amino-2-methylpropionate--pyruvate aminotransferase
(R)-3-amino-2-methylpropionate transaminase
beta-aminoisobutyrate-pyruvate aminotransferase
beta-aminoisobutyrate--pyruvate aminotransferase
beta-aminoisobutyrate--pyruvate transaminase
D-3-aminoisobutyrate-pyruvate aminotransferase
D-3-aminoisobutyrate-pyruvate transaminase
D-3-aminoisobutyrate--pyruvate transaminase
D-beta-aminoisobutyrate:pyruvate aminotransferase
The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.22, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine.
D-methionine + pyruvate = 4-methylsulfanyl-2-oxobutanoate + L-alanine.
branched-chain amino acid aminotransferase
2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate.
2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate.
5-aminolevulinate + pyruvate = 4,5-dioxopentanoate + L-alanine.
With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate.
A second component also catalyzes the reaction of EC 2.6.1.51.
glyoxylate + L-alanine = glycine + pyruvate.
glyoxylate + L-serine = 3-hydroxypyruvate + glycine.
diaminobutyrate--pyruvate aminotransferase
L-2,4-diaminobutanoate + pyruvate = L-alanine + L-aspartate 4-semialdehyde.
L-alanine + oxomalonate = aminomalonate + pyruvate.
2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-glutamate.
2-oxoglutarate + L-dopa = 3-(3,4-dihydroxyphenyl)pyruvate + L-glutamate.
glutamine--scyllo-inosose aminotransferase
L-glutamine + scyllo-inosose = 1-amino-1-deoxy-scyllo-inositol + 2-oxoglutaramate.
The liver enzyme may be identical with EC 2.6.1.44.
L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.
hydroxypyruvic phosphate--glutamic transaminase
phosphohydroxypyruvic--glutamic transaminase
This enzyme catalyzes the second step in the phosphorylated pathway of serine biosynthesis and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli.
Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis.
Non-phosphorylated forms of serine and threonine are not substrates.
The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine.
2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate.
2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate.
Also acts, more slowly, on pyridoxamine.
2-oxoglutarate + pyridoxamine 5'-phosphate = D-glutamate + pyridoxal 5'-phosphate.
taurine--alpha-ketoglutarate aminotransferase
Also acts on D,L-3-amino-isobutanoate, beta-alanine and 3-aminopropanesulfonate.
Involved in the microbial utilization of beta-alanine.
2-oxoglutarate + taurine = L-glutamate + sulfoacetaldehyde.
1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase
1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol aminotransferase
L-Glutamate and L-glutamine can also act as amino donors.
1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol + pyruvate = 1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol + L-alanine.
L-methionine can also act as donor, more slowly.
Controlled proteolysis converts the enzyme to EC 2.6.1.1.
2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate.
2-oxoglutarate + L-methionine = 4-methylsulfanyl-2-oxobutanoate + L-glutamate.
phenylalanine(histidine) aminotransferase
L-Histidine and L-tyrosine can act instead of L-phenylalanine; in the reverse reaction, L-methionine, L-serine and L-glutamine can replace L-alanine.
L-phenylalanine + pyruvate = 3-phenylpyruvate + L-alanine.
dTDP-4-amino-4,6-dideoxygalactose transaminase
dTDP-4-amino-4,6-dideoxygalactose aminotransferase
2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate.
aromatic-amino-acid--glyoxylate transaminase
aromatic-amino-acid--glyoxylate aminotransferase
Phenylalanine, kynurenine, tyrosine and histidine can act as amino donors.
Glyoxylate, pyruvate and hydroxypyruvate can act as amino acceptors.
an aromatic L-alpha-amino acid + glyoxylate = an aromatic oxo-acid + glycine.
adenosylmethionine--8-amino-7-oxononanoate transaminase
7,8-diamino-pelargonic acid aminotransferase
Adenosylmethionine--8-amino-7-oxononanoate aminotransferase
S-adenosylhomocysteine can also act as donor.
(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate.
This enzyme, characterized from animals, belongs to a family of aminotransferases some members of which can use other amino acceptors (cf. EC 2.6.1.7).
The products, 4-(2-aminophenyl)-2,4-dioxobutanoate and 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate, are converted to kynurenate and xanthurenate, respectively, by spontaneous reactions.
glyoxylate + L-kynurenine = glycine + H2O + kynurenate.
3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O + xanthurenate.
glutamine--phenylpyruvate aminotransferase
L-methionine, L-histidine and L-tyrosine can act as donors.
Has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15).
3-phenylpyruvate + L-glutamine = 2-oxoglutaramate + L-phenylalanine.
N(6)-acetyl-beta-lysine aminotransferase
2-oxoglutarate + 6-acetamido-3-aminohexanoate = 6-acetamido-3-oxohexanoate + L-glutamate.
L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine.
Also acts on L-leucine and, more slowly, on L-isoleucine, L-2-aminopentanoate and L-aspartate.
2-oxoglutarate + L-2-aminohexanoate = 2-oxohexanoate + L-glutamate.
aspartate--phenylpyruvate aminotransferase
The enzyme from Pseudomonas putida also acts on 4-hydroxyphenylpyruvate and, more slowly, on L-glutamate and L-histidine.
3-phenylpyruvate + L-aspartate = L-phenylalanine + oxaloacetate.
L-lysine + pyruvate = (S)-2-amino-6-oxohexanoate + L-alanine.
D-4-hydroxyphenylglycine aminotransferase
2-oxoglutarate + D-4-hydroxyphenylglycine = 4-hydroxyphenylglyoxylate + L-glutamate.
glyoxylate + L-methionine = 4-methylsulfanyl-2-oxobutanoate + glycine.
A number of D-amino acids, including D-alanine, D-aspartate and D-methionine can also act as amino-group donors.
Although this enzyme acts on several free D-amino acids, it differs from EC 2.6.1.21 in that it can use cephalosporin C as an amino donor.
(7R)-7-(5-carboxy-5-oxopentanamido)deacetylcephalosporanate + D-glutamate = 2-oxoglutarate + cephalosporin C.
A number of cysteine conjugates can also act.
2-oxoglutarate + S-(4-bromophenyl)-L-cysteine = 3-((4-bromophenyl)sulfanyl)-2-oxopropanoate + L-glutamate.
diaminobutyrate--2-oxoglutarate transaminase
diaminobutyrate--2-oxoglutarate aminotransferase
Differs from EC 2.6.1.46, which has pyruvate as the amino-group acceptor.
This is the first enzyme in the ectoine biosynthesis pathway, the other enzymes involved being EC 2.3.1.178 and EC 4.2.1.108.
2-oxoglutarate + L-2,4-diaminobutanoate = L-aspartate 4-semialdehyde + L-glutamate.
The enzyme from Bilophila wadsworthia catalyzes a reversible reaction that starts an anaerobic taurine degradation pathway.
beta-alanine is also a significant amino group donor.
The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyzes to sulfite and acetaldehyde.
Unlike EC 2.6.1.55, 2-oxoglutarate cannot serve as an acceptor for the amino group.
pyruvate + taurine = L-alanine + sulfoacetaldehyde.
hypotaurine + pyruvate = 2-sulfinoacetaldehyde + L-alanine.
Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79).
L-arogenate + oxaloacetate = L-aspartate + prephenate.
Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78).
The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate.
2-oxoglutarate + L-arogenate = L-glutamate + prephenate.
They secrete both the nicotianamine and the transaminated product into the soil around them.
Both compounds chelate Fe(2+) and Fe(3+); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
N(2)-succinylornithine 5-aminotransferase
Also acts on N(2)-acetyl-L-ornithine and L-ornithine, but more slowly.
In Pseudomonas aeruginosa, the arginine-inducible succinylornithine transaminase, EC 2.6.1.11 and EC 2.6.1.13 activities are catalyzed by the same enzyme, but this is not the case in all species.
This is the third enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine.
2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde.
putrescine-alpha-ketoglutarate transaminase
The enzymatic part of the reaction produces 4-aminobutanal that spontaneously cyclizes to form 1-pyrroline, which is a substrate for EC 1.2.1.19.
Cadaverine and spermidine can also act as substrates.
Forms part of the arginine catabolism pathway.
2-oxoglutarate + putrescine = 4-aminobutanal + L-glutamate.
2-oxoglutarate + putrescine = 1-pyrroline + H2O + L-glutamate.
In vivo, the reaction occurs in the opposite direction to that shown above.
This is one of the final steps in the lysine biosynthesis pathway of plants (ranging from mosses to flowering plants).
Meso-diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates.
2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate.
It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate.
While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly.
Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor.
This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa.
This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked.
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine.
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB).
In the absence of PabA and glutamine (but in the presence of Mg(2+)), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate.
PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB.
In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38 to form 4-aminobenzoate. cf. EC 2.6.1.123.
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate.
In contrast to most anthranilate-synthase I (ASI) homologs, this enzyme is not inhibited by tryptophan.
In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumor antibiotic C-1027.
In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity.
(2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine.
UDP-4-amino-4-deoxy-L-arabinose aminotransferase
UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase
UDP-4-amino-4-deoxy-L-arabinose aminomutase
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
2-oxoglutarate + UDP-4-amino-4-deoxy-beta-L-arabinose = L-glutamate + UDP-beta-L-threo-pentopyranos-4-ulose.
The enzyme is most active with L-methionine.
It participates in the L-methionine salvage pathway from S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis.
The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective.
The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates.
a 2-oxocarboxylate + L-methionine = 4-methylsulfanyl-2-oxobutanoate + an L-alpha-amino acid.
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose transaminase
dTDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase
dTDP-3-keto-6-deoxy-D-glucose 3-aminotransferase
TDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase
TDP-3-keto-6-deoxy-D-glucose 3-aminotransferase
The enzyme is involved in biosynthesis of D-mycaminose.
2-oxoglutarate + dTDP-3-amino-3,6-dideoxy-alpha-D-glucose = dTDP-3-dehydro-6-deoxy-alpha-D-glucose + L-glutamate.
dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase
TDP-3-dehydro-6-deoxy-D-galactose 3-aminotransferase
TDP-3-keto-6-deoxy-D-galactose 3-aminotransferase
The enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose.
2-oxoglutarate + dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose = dTDP-3-dehydro-6-deoxy-alpha-D-galactose + L-glutamate.
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase
UDP-4-dehydro-6-deoxy-D-glucose transaminase
UDP-beta-L-threo-pentapyranos-4-ulose transaminase
The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP.
The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.
Cf. EC 2.6.1.34, which catalyzes a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
2-oxoglutarate + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine = L-glutamate + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose.
glutamate--6'-dehydroparomamine aminotransferase
The reaction occurs in vivo in the opposite direction.
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin B, butirosin, neomycin and ribostamycin.
Works in combination with EC 1.1.3.43 to replace the 6'-hydroxy group of paromamine with an amino group.
The enzyme from the bacterium Streptomyces kanamyceticus can also catalyze EC 2.6.1.94, which leads to production of kanamycin A.
The enzyme from the bacterium Streptomyces fradiae can also catalyze EC 2.6.1.95, leading to production of neomycin C.
2-oxoglutarate + neamine = 6'-oxoparomamine + L-glutamate.
2'-deamino-2'-hydroxyneamine transaminase
Involved in the biosynthetic pathway of kanamycin A and kanamycin D.
The enzyme, characterized from the bacterium Streptomyces kanamyceticus, can also catalyze EC 2.6.1.93.
2'-deamino-2'-hydroxyneamine + 2-oxoglutarate = 2'-deamino-2'-hydroxy-6'-dehydroparomamine + L-glutamate.
Works in combination with EC 1.1.3.44 to replace the 6'''-hydroxy group of 6'''-deamino-6'''-hydroxyneomycin C with an amino group.
The enzyme, characterized from the bacterium Streptomyces fradiae, can also catalyze EC 2.6.1.93.
2-oxoglutarate + neomycin C = 6'''-deamino-6'''-oxoneomycin C + L-glutamate.
gamma-aminobutyric acid pyruvate transaminase
The enzyme is found in plants that do not have the 2-oxoglutarate dependent enzyme (cf. EC 2.6.1.19).
The reaction with pyruvate is reversible while the reaction with glyoxylate only takes place in the forward direction.
4-aminobutanoate + pyruvate = L-alanine + succinate semialdehyde.
4-aminobutanoate + glyoxylate = glycine + succinate semialdehyde.
In Euryarchaeota the reaction is catalyzed by ArcS.
In Crenarchaeota, which do not have an ArcS homolog, the reaction is catalyzed either by a homolog of EC 6.3.4.20 that includes a glutaminase domain (cf. EC 3.5.1.2), or by a homolog of EC 1.7.1.13.
The enzyme from the Euryarchaeon Methanocaldococcus jannaschii can also use arginine and ammonium as amino donors.
7-cyano-7-carbaguanosine(15) in tRNA + H2O + L-glutamine = archaeosine(15) in tRNA + L-glutamate.
UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the previous enzyme in the pathway, EC 1.1.1.335.
L-glutamate + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate = 2-oxoglutarate + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate.
This plant enzyme, along with EC 1.14.13.168, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.
L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine.
L-glutamine:2-deoxy-scyllo-inosose aminotransferase
2-deoxy-L-scyllo-inosose + L-glutamine = 2-deoxy-scyllo-inosamine + 2-oxoglutaramate.
L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
3-amino-2,3-dideoxy-scyllo-inosose + L-glutamine = 2-deoxystreptamine + 2-oxoglutaramate.
D-perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria.
The enzyme catalyzes the final step in GDP-perosamine synthesis.
2-oxoglutarate + GDP-alpha-D-perosamine = GDP-4-dehydro-alpha-D-rhamnose + L-glutamate.
(S)-3,5-dihydroxyphenylglycine transaminase
The enzyme from the bacterium Amycolatopsis orientalis catalyzes the reaction in the reverse direction as part of the biosynthesis of the (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin.
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + L-glutamate.
3-dehydro-glucose-6-phosphate--glutamate transaminase
3-oxo-glucose-6-phosphate:glutamate aminotransferase
3-dehydro-D-glucose 6-phosphate + L-glutamate = 2-oxoglutarate + D-kanosamine 6-phosphate.
lysine--8-amino-7-oxononanoate transaminase
Participates in the pathway for biotin biosynthesis.
The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyzes an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62).
(8S)-8-amino-7-oxononanoate + L-lysine = (7R,8S)-7,8-diammoniononanoate + (S)-2-amino-6-oxohexanoate.
dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminase
The enzyme is involved in the biosynthesis of dTDP-alpha-D-desosamine, a sugar found in several bacterial macrolide antibiotics including erythromycin, megalomicin A, mycinamicin II, and oleandomycin.
2-oxoglutarate + dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose = dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucose + L-glutamate.
Isolated from the bacterium Streptomyces hygroscopicus NRRL3085.
It is involved in the biosynthesis of the glycopeptide antibiotic mannopeptimycin.
(2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-phenylbutanoate + L-glutamate.
(5-formylfuran-3-yl)methyl phosphate transaminase
[5-(hydroxymethyl)furan-3-yl]methyl phosphate transaminase
The enzyme, characterized from the archaebacterium Methanocaldococcus jannaschii, participates in the biosynthesis of the cofactor methanofuran.
4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + L-alanine = [5-(aminomethyl)-3-furyl]methyl phosphate + pyruvate.
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase
The enzyme, characterized from the bacterium Shewanella oneidensis, forms 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus.
2-oxoglutarate + 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate = 3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + L-glutamate.
dTDP-4-dehydro-2,3,6-trideoxy-D-glucose 4-aminotransferase
TDP-4-keto-2,3,6-trideoxy-D-glucose 4-aminotransferase
The enzyme, isolated from the bacterium Saccharopolyspora spinosa, participates in the biosynthesis of forosamine.
2-oxoglutarate + dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-erythro-hexopyranose = dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + L-glutamate.
The enzyme, found in bacteria, is part of a L-lysine degradation pathway.
The enzyme is also active with other beta-amino compounds such as 3-amino-5-methylhexanoyl-CoA and 3-amino-3-phenylpropanoyl-CoA.
(3S)-3-aminobutanoyl-CoA + 2-oxoglutarate = acetoacetyl-CoA + L-glutamate.
(S)-ureidoglycine--glyoxylate transaminase
(S)-ureidoglycine--glyoxylate aminotransferase
The protein, found in bacteria, can use other amino-group acceptors, but is specific for (S)-ureidoglycine.
(S)-2-ureidoglycine + glyoxylate = glycine + N-carbamoyl-2-oxoglycine.
The enzyme, studied in the bacterium Pseudomonas aeruginosa, participates in a putrescine degradation pathway.
putrescine + pyruvate = 4-aminobutanal + L-alanine.
8-demethyl-8-aminoriboflavin-5'-phosphate synthase
The enzyme, characterized from the bacterium Streptomyces davawensis, has the activities of an oxidoreductase, a decarboxylase, and an aminotransferase.
Its combined actions result in the replacement of a methyl substituent of one of the aromatic rings of FMN by an amino group, a step in the biosynthetic pathway of roseoflavin.
The reaction requires thiamine for completion.
3 A + FMN + H2O + L-glutamate + O2 = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5'-phosphate + 3 AH2 + CO2 + H(+).
5-hydroxydodecatetraenal 1-aminotransferase
The enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), participates in the biosynthesis of coelimycin P1, where it catalyzes the amination of (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal.
L-glutamate can also serve as the amino group donor with lower efficiency.
(2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol + pyruvate = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + L-alanine.
The enzyme, characterized from the bacterium Arthrobacter sp. KI72, participates in the degradation of nylon-6.
Glyoxylate can serve as an alternative amino group acceptor with similar efficiency.
2-oxoglutarate + 6-aminohexanoate = 6-oxohexanoate + L-glutamate.
L-glutamine--4-(methylsulfanyl)-2-oxobutanoate aminotransferase
The enzyme, found in both prokaryotes and eukaryotes, catalyzes the last reaction in a methionine salvage pathway.
In mammals this activity is catalyzed by the multifunctional glutamine transaminase K (cf. EC 2.6.1.64).
4-methylsulfanyl-2-oxobutanoate + L-glutamine = 2-oxoglutaramate + L-methionine.
[amino group carrier protein]-gamma-(L-lysyl)-L-glutamate aminotransferase
The enzyme participates in an L-lysine biosynthesis pathway in certain species of archaea and bacteria.
2-oxoglutarate + [amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate.
The enzyme participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum sp.
In vivo it has only been assayed in the reverse direction, where the preferred amino group acceptors were found to be pyruvate and oxaloacetate.
L-alanine + vanillin = pyruvate + vanillylamine.
Acetaldehyde can act instead of acetone; D-glucose oxime can act instead of pyruvate oxime.
2-(hydroxyimino)propanoate + acetone = acetone oxime + pyruvate.
The purine residue is transferred on to the apurinic site forming a normal glycosylic bond.
dATP reacts at sites of the double-stranded depurinated DNA that lack adenine, and dGTP at sites that lack guanine.
dATP + depurinated DNA = deoxyribose triphosphate + DNA.
dGTP + depurinated DNA = deoxyribose triphosphate + DNA.
1-Deoxy-D-xylulose cannot replace 1-deoxy-D-xylulose 5-phosphate as a substrate.
1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate.
The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species.
hydroxyurea + O-acetyl-L-serine = acetate + H(+) + O-ureido-L-serine.
Transferring phosphorus-containing groups
Phosphotransferases with an alcohol group as acceptor
D-glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act as acceptors.
ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+).
ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+).
ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+).
ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+).
ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+).
A group of enzymes found in invertebrates and microorganisms highly specific for glucose.
D-sorbose, D-agatose and 5-dehydro-D-fructose also act as acceptors.
ATP + beta-D-fructose = ADP + beta-D-fructose 1-phosphate + H(+).
ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate.
Part of the Leloir pathway for galactose metabolism.
The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-alpha-D-galactosamine.
alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+).
The enzyme is specific for glucosamine and has only a minor activity with D-glucose.
Two unrelated enzymes with this activityn have been described.
One type was studied in the bacterium Vibrio cholerae, where it participates in a chitin degradation pathway.
The other type has been described from actinobacteria, where it is involved in the incorporation of environmental glucosamine into antibiotic biosynthesis pathways.
alpha-D-glucose 1-phosphate + ATP = ADP + alpha-D-glucose 1,6-bisphosphate + H(+).
The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate.
D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors.
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+).
ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+).
2-dehydro-D-gluconate + ATP = 6-phospho-2-dehydro-D-gluconate + ADP + H(+).
ATP + sedoheptulose = ADP + D-sedoheptulose 7-phosphate + H(+).
2-Deoxy-D-ribose can also act as acceptor.
ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+).
Ribitol and L-arabinitol can also act as acceptors.
ATP + L-ribulose = ADP + H(+) + L-ribulose 5-phosphate.
ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+).
ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+).
ATP + D-ribose 5-phosphate = ADP + alpha-D-ribose 1,5-bisphosphate + H(+).
ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+).
2-Aminoadenosine can also act as acceptor.
The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.114, EC 2.7.1.118 and EC 2.7.4.9.
ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide D-ribonucleotide + H(+).
3'-dephospho-CoA + ATP = ADP + CoA + H(+).
The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP.
This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.
adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+).
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates.
While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2.
In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP.
erythritol kinase (D-erythritol 4-phosphate-forming)
The enzyme has been characterized from the bacterium Propionibacterium acidipropionici (previously known as Propionibacterium pentosaceum).
ATP + erythritol = ADP + D-erythritol 4-phosphate + H(+).
ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+).
ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+).
Glycerone and L-glyceraldehyde can act as acceptors.
UTP (and, in the case of the Saccharomyces cerevisiae enzyme, ITP and GTP) can act as donors.
ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate.
(R)-glycerate + ATP = (2R)-3-phosphoglycerate + ADP + H(+).
Ethanolamine and its methyl and ethyl derivatives can also act as acceptors.
ATP + choline = ADP + H(+) + phosphocholine.
(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+).
(R)-pantetheine + ATP = (R)-4'-phosphopantetheine + ADP + H(+).
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate.
ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate.
ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate.
CTP, GTP and UTP can also act as donors.
(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+).
ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine.
UTP, GTP, CTP, ITP and dATP can also act as donors.
Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate.
GTP + pyruvate = GDP + H(+) + phosphoenolpyruvate.
pyruvate + UTP = H(+) + phosphoenolpyruvate + UDP.
CTP + pyruvate = CDP + H(+) + phosphoenolpyruvate.
ITP + pyruvate = H(+) + IDP + phosphoenolpyruvate.
dATP + pyruvate = dADP + H(+) + phosphoenolpyruvate.
2 D-glucopyranose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate.
alpha-D-glucose 1-phosphate + riboflavin = D-glucose + FMN.
ATP + D-glucuronate = 1-phospho-alpha-D-glucuronate + ADP + H(+).
ATP + D-galacturonate = 1-phospho-alpha-D-galacturonate + ADP + H(+).
The enzyme shows no activity with 2-dehydro-3-deoxy-D-galactonate.
2-dehydro-3-deoxy-D-gluconate + ATP = 2-dehydro-3-deoxy-6-phospho-D-gluconate + ADP + H(+).
ATP + L-arabinose = ADP + beta-L-arabinose 1-phosphate + H(+).
The enzyme, found in prokaryotes and eukaryotes, phosphorylates both uridine and cytidine to their monophosphate forms.
The enzyme from Escherichia coli prefers GTP to ATP.
The human enzyme also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs.
4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+).
5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+).
ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate.
ATP:6-deoxy-L-galactose 1-phosphotransferase
Forms part of a salvage pathway for reutilization of L-fucose.
Can also phosphorylate D-arabinose, but more slowly.
ATP + L-fucose = ADP + beta-L-fucose 1-phosphate + H(+).
ATP + L-xylulose = ADP + H(+) + L-xylulose 5-phosphate.
ATP + D-arabinose = ADP + D-arabinose 5-phosphate + H(+).
ATP + D-allose = ADP + D-allose 6-phosphate + H(+).
ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+).
2-dehydro-3-deoxy-D-galactonate + ATP = 2-dehydro-3-deoxy-6-phospho-D-galactonate + ADP + H(+).
The bacterial enzyme also acts on D-glucose.
ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-glucosamine 6-phosphate.
Acts on the acetyl and glycolyl derivatives.
an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine 6-phosphate + H(+).
ATP + N-acetyl-D-mannosamine = ADP + H(+) + N-acetyl-D-mannosamine 6-phosphate.
acyl-phosphate--hexose phosphotransferase
Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 or O-6.
an acyl phosphate + D-hexose = a carboxylate + D-hexose phosphate + H(+).
phosphoramidate--hexose phosphotransferase
Activity is observed with several hexoses; of these glucose is the best substrate and the product from it is alpha-D-glucose 1-phosphate.
The phosphoramidate donor can be replaced by N-phosphoglycine and by an N-phosphohistidine.
D-hexose + H(+) + phosphoramidate = alpha-D-hexose 1-phosphate + NH4(+).
polyphosphate--glucose phosphotransferase
Requires a neutral salt, e.g. KCl, for maximum activity.
[phosphate](n) + D-glucose = [phosphate](n-1) + D-glucose 6-phosphate + H(+).
ATP + myo-inositol = 1D-myo-inositol 3-phosphate + ADP + H(+).
Also acts on streptamine, 2-deoxystreptamine and 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol.
1-amino-1-deoxy-scyllo-inositol + ATP = 1-amino-1-deoxy-scyllo-inositol 4-phosphate + ADP + H(+).
ATP + di-trans,octa-cis-undecaprenol = ADP + di-trans,octa-cis-undecaprenyl phosphate + H(+).
all-trans-undecaprenol + ATP = ADP + all-trans-undecaprenyl phosphate + H(+).
phosphatidylinositol kinase (phosphorylating)
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+).
1-phosphatidylinositol-4-phosphate 5-kinase
phosphatidylinositol-4-phosphate 5-kinase
This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent.
The last of these reactions occurs in vivo and is physiologically relevant.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+).
ATP + shikimate = 3-phosphoshikimate + ADP + H(+).
Dihydrostreptomycin, streptidine and 2-deoxystreptidine can act as acceptors.
ATP + streptomycin = ADP + H(+) + streptomycin 6-phosphate.
Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.
2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a ribonucleoside 5'-diphosphate + dCMP + H(+).
2'-deoxycytidine + UTP = dCMP + H(+) + UDP.
2'-deoxycytidine + ATP = ADP + dCMP + H(+).
Deoxyguanosine can also act as acceptor.
2'-deoxyadenosine + ATP = ADP + dAMP + H(+).
Phenyl phosphate and nucleoside 3'-phosphates can act as donors, although not so well as nucleoside 5'-phosphates.
Nucleosides as well as 2'-deoxyribonucleosides can act as acceptors.
a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a 2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside.
Also acts on 5'-dephospho-RNA 3'-mononucleotides.
a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + ADP + H(+).
a 5'-end dephospho-ribonucleoside-RNA + ATP = a 5'-end 5'-monophospho-ribonucleoside-RNA + ADP + H(+).
diphosphate--glycerol phosphotransferase
pyrophosphate--glycerol phosphotransferase
diphosphate + glycerol = glycerol 1-phosphate + H(+) + phosphate.
pyrophosphate--serine phosphotransferase
diphosphate + L-serine = H(+) + O-phospho-L-serine + phosphate.
Both the natural 5-hydroxy-L-lysine and its 5-epimer act as acceptors.
(5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine + GDP + H(+).
ATP + ethanolamine = ADP + H(+) + phosphoethanolamine.
ATP + pseudouridine = ADP + H(+) + psi-UMP.
ATP + O-alkylglycerone = 1-O-alkylglycerone 3-phosphate + ADP + H(+).
Phosphorylates a number of beta-D-glucosides.
GTP, CTP, ITP and UTP can also act as donors.
ATP + D-cellobiose = 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + ADP + H(+).
CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity).
Also phosphorylates dihydrostreptomycin, 3'-deoxydihydrostreptomycin and their 6-phosphates.
ATP + streptomycin = ADP + H(+) + streptomycin 3''-phosphate.
dihydrostreptomycin-6-phosphate 3'alpha-kinase
3'-Deoxydihydrostreptomycin 6-phosphate can also act as acceptor.
ATP + dihydrostreptomycin 6-phosphate = ADP + dihydrostreptomycin 3'alpha,6-bisphosphate + H(+).
ATP + thiamine = ADP + H(+) + thiamine phosphate.
diphosphate--fructose-6-phosphate 1-phosphotransferase
diphosphate-dependent 6-phosphofructose-1-kinase
pyrophosphate-dependent 6-phosphofructose-1-kinase
pyrophosphate--fructose 6-phosphate 1-phosphotransferase
beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate.
The enzyme is involved in the production of sphingolipid metabolites.
It phosphorylates various sphingoid long-chain bases, such as sphingosine, D-erythro-dihydrosphingosine (sphinganine), phytosphingosine (4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-threo-dihydrosphingosine and L-threo-dihydrosphingosine.
The exact substrate range depends on the species.
a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+).
ATP + sphinganine = ADP + H(+) + sphinganine 1-phosphate.
ATP + sphing-4-enine = ADP + H(+) + sphing-4-enine 1-phosphate.
(4R)-hydroxysphinganine + ATP = (4R)-hydroxysphinganine 1-phosphate + ADP + H(+).
5-dehydro-2-deoxy-D-gluconate + ATP = 6-phospho-5-dehydro-2-deoxy-D-gluconate + ADP + H(+).
1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate + ADP + H(+).
a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate.
Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A.
An enzyme from Pseudomonas aeruginosa also acts on butirosin.
ATP + kanamycin A = ADP + H(+) + kanamycin 3'-phosphate.
5-(methylsulfanyl)-D-ribose + ATP = ADP + H(+) + S-methyl-5-thio-alpha-D-ribose 1-phosphate.
ATP + keto-D-tagatose = ADP + H(+) + keto-D-tagatose 6-phosphate.
Also acts, more slowly, on D-hamamelitol.
ATP + D-hamamelose = ADP + D-hamamelose 2'-phosphate + H(+).
A serine residue in the peptide antibiotics acts as phosphate-acceptor.
ATP + viomycin = ADP + H(+) + O-phosphoviomycin.
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+).
alpha-D-glucose 6-phosphate can act as acceptor, forming alpha-D-glucose 1,6-bisphosphate.
(2R)-3-phospho-glyceroyl phosphate + alpha-D-glucose 1-phosphate = (2R)-3-phosphoglycerate + alpha-D-glucose 1,6-bisphosphate + H(+).
(2R)-3-phospho-glyceroyl phosphate + alpha-D-glucose 6-phosphate = (2R)-3-phosphoglycerate + alpha-D-glucose 1,6-bisphosphate + H(+).
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol.
Activity is stimulated by certain phospholipids.
In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger.
a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+).
CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP + H(+).
2'-deoxyguanosine + ATP = ADP + dGMP + H(+).
The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.21, EC 2.7.1.128 and EC 2.7.4.9.
The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyzes this reaction as well as those of EC 2.7.1.21, EC 2.7.1.114 and EC 2.7.4.9.
Phosphorylates the antibiotics hygromycin B, 1-N-hygromycin B and destomycin, but not hygromycin B2, at the 7''-hydroxy group in the destomic acid ring.
ATP + hygromycin B = 7''-O-phosphohygromycin B + ADP + H(+).
phosphoenolpyruvate--glycerone phosphotransferase
dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate.
ATP + xylitol = ADP + H(+) + xylitol 5-phosphate.
1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+).
Involved with EC 2.3.1.129 and 2.4.1.182 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.
ATP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate} = ADP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate}.
ATP + lipid A disaccharide (E. coli) = ADP + H(+) + lipid IVA (E. coli).
a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+).
1D-myo-inositol-tetrakisphosphate 1-kinase
This enzyme also phosphorylates Ins(1,3,4)P3 on O-5 and O-6.
The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP.
It can also catalyze an isomerization between Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP.
The enzymes from animals and plants also have the activity of EC 2.7.1.159.
1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+).
Erythromycin, spiramycin and some other macrolide antibiotics can also act as acceptors.
ATP + oleandomycin = ADP + H(+) + oleandomycin 2'-O-phosphate.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).
an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+).
1D-myo-inositol-tetrakisphosphate 5-kinase
The enzyme from plants and yeast can also use Ins(1,2,3,4,6)P5 as a substrate.
1D-myo-inositol 1,3,4,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+).
glycerol-3-phosphate--glucose phosphotransferase
Involved in the anaerobic metabolism of sugars in the bloodstream of trypanosomes.
D-glucose + sn-glycerol 3-phosphate = D-glucose 6-phosphate + glycerol.
pyrophosphate-dependent nucleoside kinase
The enzyme from the Acholeplasma class of Mollicutes catalyzes the conversion of adenosine, guanosine and inosine to AMP, GMP and IMP.
ATP cannot substitute for diphosphate as a substrate.
diphosphate + a purine nucleoside = phosphate + a purine mononucleotide.
ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate + H(+).
multisubstrate deoxyribonucleoside kinase
The enzyme from embryonic cells of the fruit fly Drosophila melanogaster differs from other 2'-deoxyribonucleoside kinases (EC 2.7.1.76 and EC 2.7.1.113) in its broad specificity for all four common 2'-deoxyribonucleosides.
a 2'-deoxyribonucleoside + ATP = a 2'-deoxyribonucleoside 5'-phosphate + ADP + H(+).
ADP can be replaced by GDP, ATP and GTP, to a limited extent.
ADP + beta-D-fructose 6-phosphate = AMP + beta-D-fructose 1,6-bisphosphate + H(+).
The enzyme, characterized from a number of hyperthermophilic archaeal species, is highly specific for ADP.
No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.
ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+).
ADP + D-glucosamine = AMP + D-glucosamine 6-phosphate + H(+).
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.
4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+).
1-phosphatidylinositol-5-phosphate 4-kinase
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+).
1-phosphatidylinositol-3-phosphate 5-kinase
phosphatidylinositol 3-phosphate 5-kinase
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+).
This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown.
The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively.
Yeast produces InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158.
1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+).
phosphatidylinositol-4,5-bisphosphate 3-kinase
This enzyme also catalyzes the phosphorylation of PtdIns4P to PtdIns(3,4)P2, and of PtdIns to PtdIns3P.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).
phosphatidylinositol-4-phosphate 3-kinase
C2-domain-containing phosphoinositide 3-kinase
This enzyme also phosphorylates PtdIns to PtdIns3P.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+).
adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase
AdoCbi kinase/AdoCbi-phosphate guanylyltransferase
In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl).
CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole.
The second branch of the nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by CobU.
The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalyzed by CobS (EC 2.7.8.26), to yield adenosylcobalamin.
CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62) activities.
However, both activities are not required at all times.
The kinase activity has been proposed to function only when S.typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin.
adenosylcob(III)inamide + GTP = adenosylcob(III)inamide phosphate + GDP + H(+).
adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+).
N-acetylgalactosamine (GalNAc)-1-phosphate kinase
The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose.
ATP + N-acetyl-alpha-D-galactosamine = ADP + H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate.
inositol 1,3,4,5,6-pentakisphosphate 2-kinase
The enzyme can also use Ins(1,4,5,6)P4 and Ins(1,4,5)P3 as substrate.
Inositol hexakisphosphate (phytate) accumulates in storage protein bodies during seed development and, when hydrolyzed, releases stored nutrients to the developing seedling before the plant is capable of absorbing nutrients from its environment.
1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+).
In humans, this enzyme, along with EC 2.7.1.127, EC 2.7.1.140 and EC 2.7.1.158 is involved in the production of inositol hexakisphosphate (InsP6).
InsP6 is involved in many cellular processes, including mRNA export from the nucleus.
Yeast do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 and EC 2.7.1.158.
The enzymes from animals and plants also have the activity of EC 2.7.1.134.
1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+).
1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + H(+).
Catalyzes the final step of tRNA splicing in the yeast Saccharomyces cerevisiae.
The reaction takes place in two steps: in the first step, the 2'-phosphate on the RNA substrate is ADP-ribosylated, causing the relase of nicotinamide and the formation of the reaction intermediate, ADP-ribosylated tRNA.
In the second step, dephosphorylated (mature) tRNA is formed along with ADP ribose 1'',2''-cyclic phosphate.
Highly specific for oligonucleotide substrates bearing an internal 2'-phosphate.
Oligonucleotides with only a terminal 5'- or 3'-phosphate are not substrates.
2'-phospho-[ligated tRNA] + NAD(+) = ADP-beta-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide.
This archaeal enzyme differs from EC 2.7.1.26 in using CTP as the donor nucleotide.
UTP, but not ATP or GTP, can also act as a phosphate donor but it is at least an order of magnitude less efficient than CTP.
N-acetylgalactosamine/N-acetylglucosamine 1-kinase
Involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum.
Differs from EC 2.7.1.157 as it can phosphorylate both N-acetylgalactosamine and N-acetylglucosamine at similar rates.
Also has some activity with N-acetyl-D-mannosamine, D-talose and D-mannose as substrate.
ATP can be replaced by GTP or ITP but with decreased enzyme activity.
ATP + N-acetyl-D-hexosamine = ADP + H(+) + N-acetyl-alpha-D-hexosamine 1-phosphate.
ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate.
Phosphorylates the antibiotic hygromycin B.
Whereas the enzyme from Streptomyces hygroscopicus (EC 2.7.1.119) catalyzes the formation of 7''-O-phosphohygromycin B, this enzyme, found in Escherichia coli carrying a plasmid conferring resistance to hygromycin-B, forms 4-O-phosphohygromycin B.
ATP + hygromycin B = 4-O-phosphohygromycin B + ADP + H(+).
In archaea and eukarya selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNA(Sec) kinase (PSTK) phosphorylates the endogenous L-seryl-tRNA(Sec) to O-phospho-L-seryl-tRNA(Sec), and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNA(Sec) by EC 2.9.1.2.
ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L-seryl-tRNA(Sec).
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea.
In Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assaimilation I (serine pathway).
In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation.
(R)-glycerate + ATP = (2R)-2-phosphoglycerate + ADP + H(+).
The enzyme phosphorylates the 4-OH position of KDO in (KDO)-lipid IVA.
alpha-Kdo-(2->6)-lipid IVA + ATP = 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+).
D-glycero-beta-D-manno-heptose-7-phosphate kinase
D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase
glycero-manno-heptose 7-phosphate kinase
The bifunctional protein hldE includes D-glycero-beta-D-manno-heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70).
The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria.
The enzyme selectively produces D-glycero-beta-D-manno-heptose 1,7-bisphosphate.
ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+).
D-glycero-alpha-D-manno-heptose-7-phosphate kinase
The enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein in Gram-positive bacteria.
The enzyme is specific for the alpha-anomer.
ATP + D-glycero-alpha-D-manno-heptose 7-phosphate = ADP + D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H(+).
The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein.
In bacteria and eukaryotes this conversion is performed by condensation with beta-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively).
In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with beta-alanine.
(R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+).
This enzyme, along with EC 4.2.1.126, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria.
The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling.
The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the alpha- and beta-anomers.
1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate.
Nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications.
Key early intermediates in this process are fructosamines, such as [protein]-N(6)-D-fructosyl-L-lysine.
Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins.
The phosphorylation destablilizes the [protein]-N(6)-D-fructosyl-L-lysine adduct and leads to its spontaneous decomposition.
ATP + N(6)-(D-fructosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-fructosyl)-L-lysyl-[protein].
This enzyme plays a role in freeing proteins from ribulosamines or psicosamines, which might arise from the reaction of amines with glucose and/or glycolytic intermediates.
This role is shared by EC 2.7.1.171, which has, in addition, the unique capacity to phosphorylate fructosamines.
The plant enzyme also phosphorylates [protein]-N(6)-D-erythrulosyl-L-lysine.
No activity with [protein]-N(6)-D-fructosyl-L-lysine.
ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysyl-[protein].
ATP + N(6)-(D-psicosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-psicosyl)-L-lysyl-[protein].
ATP + N(6)-(D-erythrulosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-erythrulosyl)-L-lysyl-[protein].
The enzyme from yeast and human also has the activity of EC 2.7.1.22.
ATP + beta-D-ribosylnicotinate = ADP + H(+) + nicotinate beta-D-ribonucleotide.
Unlike the diacylglycerol kinases from bacteria, plants, and animals (cf. EC 2.7.1.107), the enzyme from Saccharomyces cerevisiae utilizes CTP.
The enzyme can also use dCTP, but not ATP, GTP or UTP.
a 1,2-diacyl-sn-glycerol + CTP = a 1,2-diacyl-sn-glycero-3-phosphate + CDP + H(+).
ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+).
Toxic component of a toxin-antitoxin (TA) module.
The phosphorylation of UDP-N-acetyl-alpha-D-glucosamine results in the inhibition of EC 2.5.1.7, which is then blocked.
Phosphorylation is inhibited by cognate epsilon antitoxin.
ATP + UDP-N-acetyl-alpha-D-glucosamine = ADP + H(+) + UDP-N-acetyl-alpha-D-glucosamine 3'-phosphate.
The enzyme is involved in the de novo synthesis of adenosylcobalamin.
It is specific for ATP and free L-threonine.
In the bacterium Salmonella enterica the activity with CTP, GTP, or UTP is 6, 11, and 3% of the activity with ATP.
ATP + L-threonine = ADP + H(+) + O-phospho-L-threonine.
The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway.
It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency.
The enzyme from the bacterium Amycolatopsis mediterranei is specific for kanosamine.
ATP + kanosamine = ADP + D-kanosamine 6-phosphate + H(+).
The enzyme catalyzes the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1.
FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+).
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
The dual kinase/methylase WbdD also catalyzes the methylation of 3-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (Cf. EC 2.1.1.294).
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + ATP = 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + ADP + H(+).
The enzyme is found in plants and photosynthetic algae and is involved in phytol salvage.
It can use UTP as an alternative phosphate donor with lower activity.
CTP + phytol = CDP + H(+) + phytyl phosphate.
In humans this phosphorylated trisaccharide is attached to an L-threonine residue of alpha-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains, and is important for its activity.
3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-Thr-[protein] + ATP = 3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + ADP + H(+).
3-O-(N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-seryl-[protein] + ATP = 3-O-(N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-6-O-phospho-alpha-D-mannosyl)-L-seryl-[protein] + ADP + H(+).
6-deoxy-6-sulfo-D-fructose + ATP = 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+).
Mevalonate 3-kinase and EC 2.7.1.186 act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum.
Mevalonate 3-kinase is different from EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea.
(R)-mevalonate + ATP = (R)-3-phosphomevalonate + ADP + H(+).
(R)-3-phosphomevalonate + ATP = (R)-3,5-bisphosphomevalonate + ADP + H(+).
The enzyme, characterized from the bacterium Actinoplanes sp. SE50/110, is specific for acarbose.
acarbose + ATP = acarbose 7(IV)-phosphate + ADP + H(+).
The enzyme, characterized from the bacterium Actinoplanes sp. SE50/110, is involved in the biosynthesis of the oligosaccharide acarbose.
2-epi-5-epi-valiolone + ATP = 2-epi-5-epi-valiolone 7-phosphate + ADP + H(+).
(S)-4,5-dihydroxypentane-2,3-dione + ATP = (2S)-2-hydroxy-3,4-dioxopentyl phosphate + ADP + H(+).
This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin.
In most, but not all, cases the phosphorylation confers resistance against the antibiotic.
Some forms of the enzyme use ATP as a phosphate donor in appreciable amount.
The enzyme is often found as a bifunctional enzyme that also catalyzes 6'-aminoglycoside N-acetyltransferase activity.
The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
a gentamycin + GTP = a gentamycin 2''-phosphate + GDP + H(+).
protein-N(pi)-phosphohistidine--D-mannose phosphotransferase
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS).
The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it.
The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9.
Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency.
The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannose 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--N-acetylmuramate phosphotransferase
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-muramate(out) = L-histidyl-[protein] + N-acetyl-beta-D-muramate 6-phosphate(in).
protein-N(pi)-phosphohistidine--N-acetyl-D-glucosamine phosphotransferase
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) = L-histidyl-[protein] + N-acetyl-D-glucosamine 6-phosphate(in).
protein-N(pi)-phosphohistidine--L-ascorbate phosphotransferase
L-ascorbate(out) + N(pros)-phospho-L-histidyl-[protein] = L-ascorbate 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--2-O-alpha-mannosyl-D-glycerate phosphotransferase
2-O-alpha-mannosyl-D-glycerate PTS permease
(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] = (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--N,N'-diacetylchitobiose phosphotransferase
N(pros)-phospho-L-histidyl-[protein] + N,N'-diacetylchitobiose(out) = diacetylchitobiose-6'-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-mannitol phosphotransferase
The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate--protein phosphotransferase).
D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannitol 1-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-sorbitol phosphotransferase
D-sorbitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-sorbitol 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-glucose phosphotransferase
D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-glucose 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--galactitol phosphotransferase
galactitol(out) + N(pros)-phospho-L-histidyl-[protein] = galactitol 1-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--trehalose phosphotransferase
alpha,alpha-trehalose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha,alpha-trehalose 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-fructose phosphotransferase
The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9.
The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9.
D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-fructose 1-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-glucosaminate phosphotransferase
2-amino-2-deoxy-D-gluconate PTS permease
2-amino-2-deoxy-D-gluconate(out) + N(pros)-phospho-L-histidyl-[protein] = 2-amino-2-deoxy-D-gluconate 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-galactose phosphotransferase
D-galactose(out) + N(pros)-phospho-L-histidyl-[protein] = D-galactose 6-phosphate(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--D-cellobiose phosphotransferase
D-cellobiose(out) + N(pros)-phospho-L-histidyl-[protein] = 6-phospho-beta-D-glucosyl-(1->4)-D-glucose(in) + L-histidyl-[protein].
protein-N(pi)-phosphohistidine--L-sorbose phosphotransferase
keto-L-sorbose(out) + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + L-sorbose 1-phosphate(in).
protein-N(pi)-phosphohistidine--lactose phosphotransferase
lactose(out) + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + lactose 6-phosphate(in).
protein-N(pi)-phosphohistidine--maltose phosphotransferase
D-maltose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha-maltose 6'-phosphate(in) + L-histidyl-[protein].
The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of L-threitol.
ATP + L-erythrulose = ADP + H(+) + L-erythrulose 1-phosphate.
The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of erythritol and D-threitol.
ATP + D-erythrulose = ADP + D-erythrulose 4-phosphate + H(+).
protein-N(pi)-phosphohistidine--sucrose phosphotransferase
N(pros)-phospho-L-histidyl-[protein](out) + sucrose = L-histidyl-[protein] + sucrose 6(G)-phosphate(in).
alpha-D-ribose-1-phosphate 5-kinase (ADP)
The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in an archaeal pathway for nucleoside degradation.
ADP + alpha-D-ribose 1-phosphate = alpha-D-ribose 1,5-bisphosphate + AMP + H(+).
The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in a pathway for nucleoside degradation.
The enzyme can also act on deoxycytidine and uridine, but unlike EC 2.7.1.48 it is most active with cytidine.
The enzyme, characterized from the bacterium Streptomyces hygroscopicus var. jinggangensis, is involved in the biosynthesis of the antifungal agent validamycin A.
ATP + valienone = ADP + H(+) + valienone 7-phosphate.
ATP + validone = ADP + H(+) + validone 7-phosphate.
erythritol kinase (D-erythritol 1-phosphate-forming)
ATP + erythritol = ADP + D-erythritol 1-phosphate + H(+).
The enzyme, found in plants and animals, can also use other nucleotide triphosphates as phosphate donor, albeit less efficiently.
The plant enzyme can also use geraniol and geranylgeraniol as substrates with lower activity, but not farnesyl phosphate (cf. EC 2.7.4.32).
(2E,6E)-farnesol + CTP = (2E,6E)-farnesyl phosphate + CDP + H(+).
(2E,6E)-farnesol + ATP = (2E,6E)-farnesyl phosphate + ADP + H(+).
(2E)-geraniol + ATP = (2E)-geranyl phosphate + ADP + H(+).
(2E,6E,10E)-geranylgeraniol + ATP = (2E,6E,10E)-geranylgeranyl phosphate + ADP + H(+).
The enzyme, characterized from bacteria, is involved in D-erythronate and L-threonate catabolism.
3-dehydro-L-erythronate + ATP = 3-dehydro-4-O-phospho-L-erythronate + ADP + H(+).
3-dehydro-D-erythronate + ATP = 3-dehydro-4-O-phospho-D-erythronate + ADP + H(+).
The enzyme, characterized from the bacterium Escherichia coli, has very little activity with fructose.
ATP + N(6)-(D-fructosyl)-L-lysine = ADP + H(+) + N(6)-(6-phospho-D-fructosyl)-L-lysine.
ATP + D-threonate = 4-O-phospho-D-threonate + ADP + H(+).
ATP + D-erythronate = 4-phospho-D-erythronate + ADP + H(+).
The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
ATP + N-acetyl-D-muramate = ADP + H(+) + N-acetyl-alpha-D-muramate 1-phosphate.
Also acts on 4-hydroxy-L-tryptophan in vitro.
4-hydroxytryptamine + ATP = 4-hydoxytryptamine 4-phosphate + ADP + H(+).
The enzyme, characterized from the bacterium Salmonella enterica, can phosphorylate exogeneously-provided 5-amino-1-(beta-D-ribosyl)imidazole to form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important intermediate in the production of both purine mononucleotides and the hydroxymethyl pyrimidine moiety of thiamine.
5-amino-1-(beta-D-ribosyl)imidazole + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+).
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium’s capsular polysaccharides.
ATP + cytidine 5'-diphosphoramidate = ADP + cytidine 3'-phospho-5'-diphosphoramidate + H(+).
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of L-2,3-diaminopropanoate, which is used by that organism as a precursor for the biosynthesis of the siderophore staphyloferrin B.
ATP + L-serine = ADP + H(+) + O-phospho-L-serine.
The enzyme, characterized in the hyperthermophilic archaeon Thermococcus kodakarensis, participates in L-cysteine biosynthesis.
ADP + L-serine = AMP + H(+) + O-phospho-L-serine.
The enzyme, characterized from yeast, attaches a phosphoinositol headgroup to alpha-hydroxyphytoceramides, generating a very-long-chain inositol phospho-alpha hydroxyphytoceramide (IPC), the simplest of the three complex sphingolipids produced by yeast.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an N-(2R-hydroxy-very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base = a 1,2-diacyl-sn-glycerol + a 1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base.
mannosyl-inositol-phosphoceramide inositolphosphotransferase
This enzyme catalyzes the ultimate reaction in the yeast sphingolipid biosynthesis pathway.
It transfers a second phosphoinositol group to mannosyl-inositol-phospho-alpha-hydroxyphytoceramide (MIPC), forming the final and most abundant yeast sphingolipid, mannosyl-diphosphoinositol-ceramide (MIP2C).
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an alpha-D-mannosyl-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base = a 1,2-diacyl-sn-glycerol + an alpha-D-mannosyl-6-(1D-myo-inositol phospho)-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base.
The enzyme, characterized from bacteria, is much more active with 2-deoxy-D-ribose than with D-ribose.
2-deoxy-D-ribose + ATP = 2-deoxy-D-ribose 5-phosphate + ADP + H(+).
The enzyme, found in some bacterial species, inactivates the antibiotic amicoumacin A by phosphorylating it, conferring resistance on the bacteria.
amicoumacin A + ATP = ADP + amicoumacin A 2-phosphate + H(+).
Stereospecificity of the product, 3-oxoisoapionate 4-phosphate, has not been determined.
3-oxoisoapionate + ATP = 3-oxoisoapionate 4-phosphate + ADP + H(+).
The enzyme, found in yeast and fungi, requires a magnesium ion.
ATP + H2O + levoglucosan = ADP + D-glucose 6-phosphate + H(+).
apulose + ATP = ADP + apulose 4-phosphate + H(+).
Phosphotransferases with a carboxy group as acceptor
While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly.
Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8.
Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate.
The enzyme catalyzes the reversible conversion of carbamoyl phosphate and ADP to ATP and carbamate, which hydrolyzes to ammonia and hydrogen carbonate.
The physiological role of the enzyme is to generate ATP.
ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate + H(+) + H2O.
(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP.
The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3.
This is also the case for two of the four isoenzymes in Arabidopsis thaliana.
The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction.
ATP + L-aspartate = 4-phospho-L-aspartate + ADP.
The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14).
ATP + butanoate = ADP + butanoyl phosphate.
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate.
(2R)-3-phosphoglycerate + GTP = (2R)-3-phospho-glyceroyl phosphate + GDP.
The product rapidly cyclizes to 5-oxoproline and phosphate.
ATP + L-glutamate = ADP + L-glutamyl 5-phosphate.
acetate + diphosphate = acetyl phosphate + phosphate.
3-methylbutanoate, 2-methylbutanoate, pentanoate, butanoate, and propanoate can also act as acceptors (cf. EC 2.7.2.7).
2-methylpropanoate + ATP = 2-methylpropanoyl phosphate + ADP.
Both propanoate and acetate can act as a substrate.
Involved in the anaerobic degradation of L-threonine in bacteria.
Both this enzyme and EC 2.7.2.1 play important roles in the production of propanoate.
ATP + propanoate = ADP + propanoyl phosphate.
The enzyme, found in a number of methanogenic archaeal genera, is involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant.
Activity is stimulated by potassium ions.
(2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate + ADP + H(+).
[amino-group carrier protein]-L-2-aminoadipate 6-kinase
The enzyme participates in an L-lysine biosynthetic pathway in certain species of bacteria and archaea.
[amino-group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine + ATP = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + ADP.
The enzyme is a dimeric complex consisting of an ATP-binding protein (FakA) and a fatty acid-binding protein (FakB).
The first step in the reaction is the binding of FakB (with a bound fatty acid) to FakA.
The fatty acid bound to FakB is then phosphorylated by FakA, and the fatty acyl phosphate-bound FakB is released from the complex.
In the presence of an exchangeable fatty acid pool in the cell membrane, the fatty acy phosphate bound to FakB exchanges with a fatty acid to regenerate the substrate for FakA.
The system is widespread in Gram-positive bacteria, with most strains possessing a single FakA protein along with multiple FakB subunits that differ in their specificity toward fatty acid substrates.
a fatty acid + ATP = a fatty acyl monophosphate + ADP.
Phosphotransferases with a nitrogenous group as acceptor
ATP + guanidinoacetate = ADP + H(+) + phosphoguanidinoacetate.
N-Ethylglycocyamine can also act as acceptor.
ATP + creatine = ADP + H(+) + N-phosphocreatine.
ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine.
ATP + taurocyamine = ADP + H(+) + N-phosphotaurocyamine.
Also acts on methylated lombricines such as thalassemine; the specificity varies with the source species.
ATP + L-lombricine = ADP + H(+) + N-phospho-L-lombricine.
Also acts, more slowly, on taurocyamine.
ATP + hypotaurocyamine = ADP + H(+) + N(omega)-phosphohypotaurocyamine.
Has a little activity on taurocyamine, lombricine and phosphotaurocyamine.
ATP + guanidinoethyl methyl phosphate = ADP + H(+) + N'-phosphoguanidinoethyl methylphosphate.
In the reverse direction, N-phosphoglycine and N-phosphohistidine can also act as phosphate donors, and ADP, dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate acceptors (in decreasing order of activity).
ATP + NH4(+) = ADP + 2 H(+) + phosphoramidate.
phosphoenolpyruvate--protein phosphotransferase
enzyme I of the phosphotransferase system
phosphoenolpyruvate--protein phosphatase
phosphoenolpyruvate sugar phosphotransferase enzyme I
phosphopyruvate--protein factor phosphotransferase
phosphopyruvate--protein phosphotransferase
Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport.
A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme.
L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate.
L-arginine can act as acceptor, more slowly.
agmatine + ATP = ADP + 2 H(+) + N(4)-phosphoagmatine.
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
ATP + H2O + L-glutamine = AMP + 2 H(+) + N(5)-phospho-L-glutamine + phosphate.
Phosphotransferases with a phosphate group as acceptor
The enzyme is responsible for the synthesis of most of the cellular polyphosphate, using the terminal phosphate of ATP as substrate.
[phosphate](n) + ATP = [phosphate](n+1) + ADP.
(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate + ADP.
Inorganic triphosphate can also act as donor.
Other nucleoside triphosphates can act instead of ATP.
a ribonucleoside 5'-phosphate + ATP = a ribonucleoside 5'-diphosphate + ADP.
nucleoside 5'-diphosphate phosphotransferase
Many nucleoside diphosphates can act as acceptors.
Many ribo- and deoxyribonucleoside triphosphates can act as donors.
a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP.
a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP.
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP.
nucleoside-triphosphate--adenylate kinase
Many nucleoside triphosphates can act as donors.
a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP.
a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'-deoxyribonucleoside 5'-diphosphate + ADP.
uridine monophosphate-cytidine monophosphate phosphotransferase
This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22.
ATP + thiamine diphosphate = ADP + thiamine triphosphate.
ATP + thiamine phosphate = ADP + thiamine diphosphate.
3-phosphoglyceroyl-phosphate--polyphosphate phosphotransferase
(2R)-3-phospho-glyceroyl phosphate + [phosphate](n) = (2R)-3-phosphoglycerate + [phosphate](n+1).
(2E,6E)-farnesyl diphosphate + ATP = (2E,6E)-farnesyl triphosphate + ADP.
5-methyldeoxycytidine-5'-phosphate kinase
The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m(5)dCMP into m(5)dCDP and then into m(5)dCTP.
5-methyldeoxycytidine 5'-phosphate + ATP = 5-methyldeoxycytidine diphosphate + ADP.
dolichyl-diphosphate--polyphosphate phosphotransferase
[phosphate](n) + a dolichyl diphosphate = [phosphate](n+1) + a dolichyl phosphate.
Three mammalian isoforms are known to exist.
1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ADP.
1-diphospho-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP.
Strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme EC 2.7.4.14 for the same purpose.
Subject of feedback regulation, being inhibited by UTP and activated by GTP.
This enzyme, found in NAD suppression mutants of Escherichia coli, synthesizes 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) without the participation of EC 2.7.6.1.
Ribose, ribose 1-phosphate and ribose 5-phosphate are not substrates, and GTP cannot act as a phosphate donor.
alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP.
diphosphoinositol-pentakisphosphate 1-kinase
diphosphoinositol-pentakisphosphate 1/3-kinase
diphosphoinositol pentakisphosphate kinase
diphosphoinositol-pentakisphosphate kinase
This enzyme is activated by osmotic shock.
Ins(1,3,4,5,6)P5, 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates.
The enzyme specifically phosphorylates the 1-position of the substrates.
1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP.
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP.
The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor.
Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22.
The enzyme phosphorylates dCMP nearly as well as it does CMP.
The enzyme is involved in the mevalonate pathway in Archaea.
The activity has also been identified in the plant Mentha piperita (peppermint).
It is strictly specific for ATP but can use other phosphate acceptors such as prenyl phosphate, geranyl phosphate, or fosfomycin.
ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate.
([Pyruvate, phosphate dikinase] phosphate) phosphotransferase
bifunctional dikinase regulatory protein
pyruvate, phosphate dikinase regulatory protein
The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyzes the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32.
H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase] + phosphate = diphosphate + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase].
([Pyruvate, water dikinase] phosphate) phosphotransferase
The enzyme from the bacterium Escherichia coli is bifunctional and catalyzes both the phosphorylation and dephosphorylation of pyruvate, water dikinase (EC 2.7.9.2), cf. EC 2.7.11.33.
[pyruvate, water dikinase]-phosphate + H(+) + phosphate = [pyruvate, water dikinase] + diphosphate.
In vitro the enzyme can use diacylglycerol 3-diphosphate as the phosphate donor.
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + di-trans,octa-cis-undecaprenyl diphosphate = (Kdo)2-lipid A 1-diphosphate + di-trans,octa-cis-undecaprenyl phosphate.
[5-(aminomethyl)furan-3-yl]methyl phosphate kinase
[5-(aminomethyl)-3-furyl]methyl phosphate + ATP = [5-(aminomethyl)furan-3-yl]methyl diphosphate + ADP.
The enzyme, found in plants and animals, is specific for CTP as phosphate donor.
It does not use farnesol as substrate (cf. EC 2.7.1.216).
(2E,6E)-farnesyl phosphate + CTP = (2E,6E)-farnesyl diphosphate + CDP.
The enzyme, characterized from the bacteria Acinetobacter johnsonii and Pseudomonas aeruginosa, transfers a phosphate group from polyphosphates to nucleotide monophosphates.
The highest activity is achieved with AMP, but the enzyme can also phosphorylate GMP, dAMP, dGMP, IMP, and XMP.
The reverse reactions were not detected.
[phosphate](n) + ADP = [phosphate](n+1) + AMP.
Polyphosphate kinase 2, characterized from the bacterium Pseudomonas aeruginosa, uses inorganic polyphosphate as a donor to convert GDP to GTP.
The enzyme can also act on ADP (cf. EC 2.7.4.1), but with lower activity.
The enzyme has only a trivial activity in the opposite direction (synthesizing polyphosphate from GTP).
The GTP that is produced is believed to be consumed by EC 2.7.7.13.
[phosphate](n) + GTP = [phosphate](n+1) + GDP.
Phosphotransferases with regeneration of donors, apparently catalyzing intramolecular transfers
ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+).
ATP + thiamine = AMP + H(+) + thiamine diphosphate.
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
6-hydroxymethyl-7,8-dihydropterin diphosphokinase
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
7,8-dihydro-6-hydroxymethylpterin diphosphokinase
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase
The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria).
The enzyme from the bacterium Streptococcus pneumoniae also harbors the activity of EC 4.1.2.25, the enzyme from the plant Arabidopsis thaliana harbors the activity of EC 2.5.1.15, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities.
6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+).
Acts on the 5'-mono-, di- and triphosphate derivatives of purine nucleosides.
a nucleoside 5'-phosphate + ATP = a 5'-phosphonucleoside 3'-diphosphate + AMP + H(+).
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
nicotinamide-nucleotide adenylyltransferase
adenosine triphosphate-nicotinamide mononucleotide transadenylase
diphosphopyridine nucleotide pyrophosphorylase
nicotinamide adenine dinucleotide pyrophosphorylase
nicotinamide mononucleotide adenylyltransferase
Nicotinate nucleotide can also act as acceptor.
ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+).
Highly specific for ATP as phosphate donor.
While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.
pantetheine-phosphate adenylyltransferase
The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157.
(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate.
ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate.
ADP + H(+) + sulfate = adenosine 5'-phosphosulfate + phosphate.
RNA nucleotidyltransferase (DNA-directed)
Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized.
a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).
DNA nucleotidyltransferase (DNA-directed)
Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
Requires a primer which may be DNA or RNA.
a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1).
polyribonucleotide nucleotidyltransferase
ADP, IDP, GDP, UDP and CDP can act as donors.
phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n).
UTP--glucose-1-phosphate uridylyltransferase
alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose.
UTP--hexose-1-phosphate uridylyltransferase
galactose-1-phosphate uridylyltransferase
alpha-D-glucose 1-phosphate can also act as acceptor, more slowly.
alpha-D-galactose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-galactose.
UTP--xylose-1-phosphate uridylyltransferase
alpha-D-xylose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-xylose.
UDP-glucose--hexose-1-phosphate uridylyltransferase
alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose.
GTP-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose.
ethanolamine-phosphate cytidylyltransferase
CTP:phosphoethanolamine cytidylyltransferase
CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate.
CTP + H(+) + phosphocholine = CDP-choline + diphosphate.
nicotinate-nucleotide adenylyltransferase
ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate.
Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time.
The primer, depending on the source of the enzyme, may be an RNA or DNA fragment or oligo(A) bearing a 3'-OH terminal group.
ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide.
mannose-1-phosphate guanylyltransferase (GDP)
alpha-D-mannose 1-phosphate + GDP + H(+) = GDP-alpha-D-mannose + phosphate.
N-acetylglucosamine-1-phosphate uridyltransferase
UDP-N-acetylglucosamine pyrophosphorylase
The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157.
The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate.
H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
glucose-1-phosphate thymidylyltransferase
alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose.
alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate.
nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase
GTP:alpha-D-hexose-1-phosphate guanylyltransferase
guanosine diphosphohexose pyrophosphorylase
hexose 1-phosphate nucleotidyltransferase
NTP:hexose-1-phosphate nucleotidyltransferase
nucleoside diphosphohexose pyrophosphorylase
nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase
In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar.
nucleoside triphosphate + alpha-D-aldose 1-phosphate = diphosphate + NDP-hexose.
beta-L-fucose 1-phosphate + GTP + H(+) = diphosphate + GDP-beta-L-fucose.
terminal deoxyribonucleotidyltransferase
galactose-1-phosphate thymidylyltransferase
alpha-D-galactose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-D-galactose.
glucose-1-phosphate cytidylyltransferase
alpha-D-glucose 1-phosphate + CTP + H(+) = CDP-D-glucose + diphosphate.
Also acts, more slowly, on D-mannose 1-phosphate.
alpha-D-glucose 1-phosphate + GTP + H(+) = diphosphate + GDP-D-glucose.
The enzyme, characterized from the single-celled alga Euglena gracilis, catalyzes an irreversible reaction in the direction of ADP formation.
ADP + D-ribose 5-phosphate + H(+) = ADP-D-ribose + phosphate.
ADP + alpha-D-aldose 1-phosphate = phosphate + ADP-aldose.
aldose-1-phosphate nucleotidyltransferase
sugar-1-phosphate nucleotidyltransferase
The enzyme works on a variety of alpha-D-aldose 1-phosphates and beta-L-aldose 1-phosphates (which have the same anomeric configuration as the former).
NDP + alpha-D-aldose 1-phosphate = phosphate + NDP-aldose.
3-deoxy-manno-octulosonate cytidylyltransferase
CMP-2-keto-3-deoxyoctulosonic acid synthetase
CMP-3-deoxy-D-manno-octulosonate diphosphorylase
CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase
3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate.
glycerol-3-phosphate cytidylyltransferase
CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate.
D-ribitol-5-phosphate cytidylyltransferase
CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate.
a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate.
[glutamine synthetase] adenylyltransferase
[glutamate--ammonia-ligase] adenylyltransferase
glutamate-ammonia-ligase adenylyltransferase
glutamine-synthetase adenylyltransferase
This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2.
The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89).
The two activities are present on separate domains.
[glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate.
Acts on N-acetyl- and N-glycolyl- derivatives.
an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate + diphosphate.
glucuronate-1-phosphate uridylyltransferase
1-phospho-alpha-D-glucuronate + H(+) + UTP = diphosphate + UDP-alpha-D-glucuronate.
guanosine-triphosphate guanylyltransferase
Also acts, more slowly, on GDP to form P(1),P(3)-bis(5'-guanosyl) triphosphate.
2 GTP + H(+) = diphosphate + P(1),P(4)-bis(5'-guanosyl) tetraphosphate.
2''-aminoglycoside nucleotidyltransferase
ATP, dATP, CTP, ITP and GTP can act as donors.
Kanamycin, tobramycin and sisomicin can also act as acceptors.
The nucleotidyl residue is transferred to the 2-hydroxy group of the 3-amino-3-deoxy-D-glucose moiety in the antibiotic.
nucleoside triphosphate + gentamicin = diphosphate + 2''-nucleotidylgentamicin.
ATP + streptomycin = 3''-O-adenylylstreptomycin + diphosphate.
RNA nucleotidyltransferase (RNA-directed)
Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
DNA nucleotidyltransferase (RNA-directed)
Catalyzes RNA-template-directed extension of the 3'-end of a DNA strand by one deoxynucleotide at a time.
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74.
a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate.
adenylylsulfate--ammonia adenylyltransferase
adenosine 5'-phosphosulfate + NH4(+) = adenosine 5'-phosphoramidate + 2 H(+) + sulfate.
Requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide.
bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming)
diadenosine 5',5'''-P(1),P(4)-tetraphosphate phosphorylase
diadenosinetetraphosphate alphabeta-phosphorylase
GTP and adenosine tetraphosphate can also act as adenylyl acceptors.
ADP + ATP + H(+) = P(1),P(4)-bis(5'-adenosyl) tetraphosphate + phosphate.
Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus in tRNA and nucleoside diphosphate.
phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n).
N-methylphosphoethanolamine cytidylyltransferase
CTP + H(+) + N-methylethanolamine phosphate = CDP-N-methylethanolamine + diphosphate.
The enzyme uridylylates and de-uridylylates the small trimeric protein PII.
[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate.
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
4-diphosphocytidyl-2-C-methyl-D-erythritol synthase
ATP or UTP can replace CTP, but both are less effective.
2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate.
citrate lyase holo-[acyl-carrier protein] synthase
2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase
The gamma-subunit of EC 4.1.3.6 serves as an acyl-carrier protein (ACP) and contains the prosthetic group 2'-(5-triphosphoribosyl)-3'-dephospho-CoA.
Synthesis and attachment of the prosthetic group requires the concerted action of this enzyme and EC 2.4.2.52.
In the enzyme from Escherichia coli, the prosthetic group is attached to serine-14 of the ACP via a phosphodiester bond.
2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-[citrate lyase ACP] = diphosphate + holo-[citrate lyase ACP].
adenosylcobinamide-phosphate guanylyltransferase
The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU.
The guanylyltransferase reaction is a two-stage reaction with formation of a CobU-GMP intermediate.
adenosylcob(III)inamide phosphate + GTP + H(+) = adenosylcob(III)inamide-GDP + diphosphate.
UTP-monosaccharide-1-phosphate uridylyltransferase
The reaction can occur in either direction and it has been postulated that MgUTP and Mg-diphosphate are the actual substrates.
Catalyzes the formation of UDP-Glc, UDP-Gal, UDP-GlcA, UDP-L-Ara and UDP-Xyl, showing broad substrate specificity toward monosaccharide 1-phosphates.
Mannose 1-phosphate, L-fucose 1-phosphate and glucose 6-phosphate are not substrates and UTP cannot be replaced by other nucleotide triphosphates.
a monosaccharide 1-phosphate + H(+) + UTP = a UDP-monosaccharide + diphosphate.
Can be activated by BeF3, a phosphoryl mimic, which results in dimerization.
Dimerization is required but is not sufficient for diguanylate-cyclase activity.
Cyclic di-3',5'-guanylate is an intracellular signaling molecule that controls motility and adhesion in bacterial cells; it was first identified as having a positive allosteric effect on EC 2.4.1.12.
malonate decarboxylase holo-[acyl-carrier protein] synthase
The delta subunit of malonate decarboxylase serves as an an acyl-carrier protein (ACP) and contains the prosthetic group 2'-(5-triphosphoribosyl)-3'-dephospho-CoA.
Two reactions are involved in the production of the holo-ACP form of this enzyme.
The first reaction is catalyzed by EC 2.4.2.52.
The resulting prosthetic group is then attached to the ACP subunit via a phosphodiester linkage to a serine residue, thus forming the holo form of the enzyme, in a manner analogous to that of EC 2.7.7.61.
2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-[malonate decarboxylase ACP] = diphosphate + holo-[malonate decarboxylase ACP].
CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase
CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol synthase
Catalyzes one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycero-1-phosphate backbone rather than an sn-glycero-3-phosphate backbone as is found in bacteria and eukaryotes.
2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP + H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate.
This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor, in all methanogenic archaea.
(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate.
GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase
This plant enzyme catalyzes the conversion of GDP-beta-L-galactose and GDP-alpha-D-glucose to beta-L-galactose 1-phosphate and alpha-D-glucose 1-phosphate, respectively.
The enzyme can use inorganic phosphate as the cosubstrate, but several hexose 1-phosphates, including alpha-D-mannose 1-phosphate, alpha-D-glucose 1-phosphate, and alpha-D-galactose 1-phosphate, are better guanylyl acceptors.
The enzyme's activity on GDP-beta-L-galactose is crucial for the biosynthesis of L-ascorbate.
alpha-D-mannose 1-phosphate + GDP-beta-L-galactose = beta-L-galactose 1-phosphate + GDP-alpha-D-mannose.
alpha-D-mannose 1-phosphate + GDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + GDP-alpha-D-mannose.
GDP-beta-L-galactose + phosphate = beta-L-galactose 1-phosphate + GDP + H(+).
alpha-D-glucose 1-phosphate + GDP-beta-L-galactose = beta-L-galactose 1-phosphate + GDP-alpha-D-glucose.
GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + GDP + H(+).
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
D-glycero-D-manno-heptose-1beta-phosphate adenylyltransferase
The bifunctional protein hldE includes D-glycero-beta-D-manno-heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.1.167).
ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate.
D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase
The enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein in some Gram-positive bacteria.
D-glycero-alpha-D-manno-heptose 1-phosphate + GTP + H(+) = diphosphate + GDP-D-glycero-alpha-D-manno-heptose.
ribonucleic cytidylic cytidylic adenylic pyrophosphorylase
transfer ribonucleic adenylyl (cytidylyl) transferase
The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence.
The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms.
Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition.
a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate.
sulfur carrier protein ThiS adenylyltransferase
The enzyme catalyzes the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
The enzyme shows significant structural similarity to ubiquitin-activating enzyme.
In Escherichia coli, but not in Bacillus subtilis, the enzyme forms a cross link from Cys-184 to the ThiS carboxy terminus (the position that is also thiolated) via an acyldisulfide.
[sulfur-carrier protein ThiS]-C-terminal Gly-Gly + ATP + H(+) = [sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + diphosphate.
1L-myo-inositol 1-phosphate cytidylyltransferase
L-myo-inositol-1-phosphate cytidylyltransferase
In many organisms this activity is catalyzed by a bifunctional enzyme.
The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 is absolutely specific for CTP and 1L-myo-inositol 1-phosphate.
The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol + diphosphate.
Catalyzes the activation of molybdopterin for molybdenum insertion.
In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes EC 2.10.1.1.
ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate.
molybdenum cofactor cytidylyltransferase
Catalyzes the cytidylation of the molybdenum cofactor.
This modification occurs only in prokaryotes.
CTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin cytosine dinucleotide.
Catalyzes the guanylation of the molybdenum cofactor.
GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide.
The enzyme may be involved in prevention of misincorporation of glucose in place of mannose residues into glycoconjugates i.e. to remove accidentally produced GDP-alpha-D-glucose.
Activities with GDP-L-galactose, GDP-D-mannose and UDP-D-glucose are all less than 3% that with GDP-D-glucose.
In eukarya an additional guanosine residue is added post-transcriptionally to the 5'-end of tRNA(His) molecules.
The addition occurs opposite a universally conserved adenosine(73) and is thus the result of a non-templated 3'-5' addition reaction.
The additional guanosine residue is an important determinant for aminoacylation by EC 6.1.1.21.
The enzyme requires a divalent cation for activity.
ATP activation is not required when the substrate contains a 5'-triphosphate (ppp-tRNA(His)).
a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate + H(+).
molybdopterin-synthase adenylyltransferase
Adenylates the C-terminus of the small subunit of the molybdopterin synthase.
This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit.
The reaction occurs in prokaryotes and eukaryotes.
In the human, the reaction is catalyzed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate.
CTP + pseudaminate = CMP-pseudaminate + diphosphate.
CMP-N,N'-diacetyllegionaminic acid synthase
Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni.
Involved in biosynthesis of legionaminic acid, a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates which may include lipopolysaccharide (LPS), capsular polysaccharide, pili and flagella.
CTP + N,N-diacetyllegionaminate = CMP-N,N-diacetyllegionaminate + diphosphate.
UDP-N-acetylgalactosamine diphosphorylase
The enzyme from plants and animals also has activity toward N-acetyl-alpha-D-glucosamine 1-phosphate (cf. EC 2.7.7.23).
H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-galactosamine.
The enzyme is activated by binding to double-stranded RNA.
The resulting product binds to and activates RNase L, which subsequently degrades the RNA.
Oligoadenylates of chain lengths 2, 4 and 5 are also produced.
The dimer does not have any known biological activity.
3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate.
Cyclic di-3',5'-adenylate is a bioactive molecule produced by some bacteria and archaea, which may function as a secondary signaling molecule.
The intracellular bacterial pathogen Listeria monocytogenes secretes it into the host's cytosol, where it triggers a cytosolic pathway of innate immunity.
Cyclic Gp(2'-5')Ap(3'-5') is a signaling molecule in mammalian cells that triggers the production of type I interferons and other cytokines.
ATP + GTP = 2',3'-cGAMP + 2 diphosphate.
The enzyme is involved in the synthesis of N(6)-threonylcarbamoyladenosine(37) in tRNAs with the anticodon NNU, i.e. tRNA(Ile), tRNA(Thr), tRNA(Asn), tRNA(Lys), tRNA(Ser) and tRNA(Arg).
ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate.
The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses and lyssaviruses) is specific for mRNAs with sequences starting with AACA.
a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate.
[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2.
The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42).
[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.
8-amino-3,8-dideoxy-manno-octulosonate cytidylyltransferase
The enzyme, characterized from the bacterium Shewanella oneidensis MR-1, acts on the 8-aminated from of 3-deoxy-alpha-D-manno-octulosonate (Kdo).
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate + CTP = CMP-8-amino-3,8-dideoxy-alpha-D-manno-oct-2-ulosonate + diphosphate.
valienol-1-phosphate guanylyltransferase
The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, is involved in the biosynthesis of the antifungal agent validamycin A.
GTP + H(+) + valienol 1-phosphate = diphosphate + GDP-valienol.
3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase
The enzyme is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate (Kdn).
3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + CTP = CMP-beta-3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + diphosphate.
The enzyme, characterized from the bacterium Streptomyces viridochromogenes, participates in the biosynthesis of the herbicide antibiotic bialaphos.
The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine.
Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2.
CTP + phosphonoformate = CMP-5'-phosphonoformate + diphosphate.
diphosphate--ADP-D-ribose adenylyltransferase
The human enzyme produces ATP in nuclei in situations of high energy demand, such as chromatin remodeling.
The reaction is dependent on the presence of diphosphate.
In its absence the enzyme catalyzes the reaction of EC 3.6.1.13.
ATP + D-ribose 5-phosphate + H(+) = ADP-D-ribose + diphosphate.
3-hydroxy-4-methylanthranilate adenylyltransferase
The enzyme, characterized from the bacteria Streptomyces anulatus and Streptosporangium sibiricum, activates 3-hydroxy-4-methylanthranilate, a precursor of actinomycin antibiotics and the antitumor antibiotic sibiromycin, to an adenylate form, so it can be loaded onto a dedicated aryl-carrier protein.
3-hydroxy-4-methylanthranilate + ATP + H(+) = 3-hydroxy-4-methylanthranilyl-5'-AMP + diphosphate.
N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase
H(+) + N-acetyl-alpha-D-muramate 1-phosphate + UDP = phosphate + UDP-N-acetyl-alpha-D-muramate.
The enzyme catalyzes the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea, by catalyzing the ATP-dependent formation of a SAMP adenylate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage.
The product of this activity can accept a sulfur atom to form a thiocarboxylate moiety that acts as a sulfur carrier involved in thiolation of tRNA and other metabolites such as molybdopterin.
Alternatively, the enzyme can also catalyze the transfer of SAMP from its activated form to an internal cysteine residue, leading to a process termed SAMPylation (see EC 6.2.1.55).
[small archaeal modifier protein]-C-terminal Gly-Gly + ATP + H(+) = [small archaeal modifier protein]-C-terminal Gly-Gly-AMP + diphosphate.
The enzyme catalyzes the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase.
The latter also have a second primase system (EC 2.7.7.102).
ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
The enzyme, which is found in eukaryota and archaea, catalyzes the synthesis of short RNA or DNA sequences which are used as primers for EC 2.7.7.7.
ssDNA + n dNTP = ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate.
L-glutamine-phosphate cytidylyltransferase
CTP + H(+) + N(5)-phospho-L-glutamine = diphosphate + N(5)-(cytidine 5'-diphosphoramidyl)-L-glutamine.
2-hydroxyethylphosphonate cytidylyltransferase
The enzyme also is active as EC 5.4.2.9.
2-hydroxyethylphosphonate + CTP = cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + diphosphate.
This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor, in mycobacteria.
GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine.
3-phospho-D-glycerate guanylyltransferase
The enzyme, characterized from the Gram-negative bacterium Paraburkholderia rhizoxinica, participates in the biosynthesis of 3PG-factor 420.
The enzyme can also accept 2-phospho-L-lactate and phosphoenolpyruvate, but activity is much higher with 3-phospho-D-glycerate.
(2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-diphospho-5'-guanosine + diphosphate.
The enzyme, commonly referred to as AMPylase, transfers an adenylyl (adenosine 5'-phosphate) group from ATP to L-serine, L-threonine, and L-tyrosine residues in its target protein substrates.
AMPylation is found in both prokaryotes and eukaryotes.
In bacteria AMPylases are abundant enzymes that either regulate the function of endogenous bacterial proteins or are translocated into host cells to hijack host cell signaling processes.
Metazoans AMPylases are either enzymes containing a conserved Fic domain that primarily modify the ER-resident chaperone BiP, or mitochondrial selenocysteine-containing proteins (SelO) involved in redox signaling.
ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein].
ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate.
ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate.
The enzyme from Legionella also functions as EC 2.7.7.n1.
GTP + L-tyrosyl-[protein] = diphosphate + O-(5'-guanylyl)-L-tyrosyl-[protein].
Transferases for other substituted phosphate groups
a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CMP + H(+).
1-O-(1Z-alkenyl)-2-acyl-sn-glycerol + CDP-ethanolamine = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + CMP + H(+).
diacylglycerol cholinephosphotransferase
1-alkyl-2-acetylglycerol cholinephosphotransferase
alkylacylglycerol cholinephosphotransferase
phosphorylcholine--glyceride transferase
1-alkyl-2-acylglycerol can act as acceptor.
a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+).
1-O-alkyl-2-acyl-sn-glycerol + CDP-choline = 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + CMP + H(+).
a 1-O-alkyl-2-acetyl-sn-glycerol + CDP-choline = a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + CMP + H(+).
an N-acylsphing-4-enine + CDP-choline = a sphingomyelin + CMP + H(+).
CDP-ethanolamine + L-serine = CMP + H(+) + L-serine-phosphoethanolamine.
CDP-diacylglycerol--glycerol-3-phosphate 1-phosphatidyltransferase
3-phosphatidyl-1'-glycerol-3'-phosphate synthase
glycerophosphate phosphatidyltransferase
The enzyme catalyzes the committed step in the biosynthesis of acidic phospholipids known by the common names phophatidylglycerols and cardiolipins.
a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+).
undecaprenyl-phosphate galactose phosphotransferase
poly(isoprenol)-phosphate galactosephosphotransferase
di-trans,octa-cis-undecaprenyl phosphate + UDP-alpha-D-galactose = alpha-D-galactosyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP.
acyl carrier protein holoprotein (holo-ACP) synthetase
alphaaminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active.
The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain.
The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes.
Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.
apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP].
CDP-diacylglycerol--serine O-phosphatidyltransferase
CDP-diglycerine-serine O-phosphatidyltransferase
a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+).
GDP-mannose + (phosphomannan)n = GMP + (phosphomannan)n+1.
CDP-choline + sphing-4-enine = CMP + H(+) + sphing-4-enine-phosphocholine.
CDP-diacylglycerol--inositol 3-phosphatidyltransferase
CDP-diacylglycerol--inositol phosphatidyltransferase
a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+).
teichoic acid poly(glycerol phosphate) polymerase
This enzyme adds 30-50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44.
4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CDP-glycerol = 4-O-{[(2R)-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl undecaprenyl diphosphate + n CMP + n H(+).
phosphoacetylmuramoylpentapeptide translocase
phospho-N-acetylmuramoyl pentapeptide translocase
phospho-NAc-muramoyl-pentapeptide translocase (UMP)
UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla:undecaprenylphosphate transferase
UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid alcohol transferase
UDP-MurNAc-pentapeptide phosphotransferase
In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-center.
di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + UMP.
di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP.
Involved in the biosynthesis of poly ribitol phosphate teichoic acids in the cell wall of the bacterium Staphylococcus aureus.
This enzyme adds around 40 ribitol units to the linker molecule.
4-O-[di(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CDP-L-ribitol = 4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CMP + n H(+).
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
N-acetylglucosamine-1-phosphate transferase
a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP.
UDP-N-acetylglucosamine--lysosomal-enzyme N-acetylglucosaminephosphotransferase
Some other glycoproteins with high-mannose can act as acceptors, but much more slowly than lysosomal enzymes.
N(4)-[alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + UMP.
UDP-galactose--UDP-N-acetylglucosamine galactose phosphotransferase
N-Acetylglucosamine end-groups in glycoproteins can also act as acceptors.
UDP-alpha-D-galactose + UDP-N-acetyl-alpha-D-glucosamine = H(+) + UDP-N-acetyl-6-(alpha-D-galactose-1-phospho)-alpha-D-glucosamine + UMP.
UDP-glucose--glycoprotein glucose phosphotransferase
Penultimate mannose residues on oligomannose type glycoproteins can act as acceptors.
alpha-D-mannose derivative + UDP-alpha-D-glucose = 6-(alpha-D-glucose-1-phospho)-alpha-D-mannosyl derivative + H(+) + UMP.
phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase
1,2-beta- and 1,6-beta-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors.
phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose.
membrane-oligosaccharide glycerophosphotransferase
beta-linked glucose residues in simple glucosides, such as gentiobiose, can act as acceptors.
In the presence of low concentrations of acceptor, free cyclic 1,2-phosphoglycerol is formed.
Transfer of a glycerophospho group from one membrane-derived oligosaccharide to another.
1-alkenyl-2-acylglycerol choline phosphotransferase
1-O-(1Z-alkenyl)-2-acyl-sn-glycerol + CDP-choline = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CMP + H(+).
carboxyvinyl-carboxyphosphonate phosphorylmutase
carboxyphosphonoenolpyruvate phosphonomutase
Catalyzes the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos.
1-carboxyvinyl carboxyphosphonate + H(+) = 3-(hydrohydroxyphosphoryl)pyruvate + CO2.
CDP-diglyceride-choline O-phosphatidyltransferase
a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+).
adenosylcobinamide-GDP ribazoletransferase
The second branch of the nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU.
CobS catalyzes the final step in adenosylcobalamin biosynthesis, which is the condensation of AdoCbi-GDP with alpha-ribazole to yield adenosylcobalamin.
adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+).
adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+).
phosphatidylcholine:ceramide cholinephosphotransferase
The reaction can occur in both directions.
Occupies a central position in sphingolipid and glycerophospholipid metabolism.
Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signaling in a variety of mammalian cell types.
Unlike EC 2.7.8.3 CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin.
a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin.
This enzyme is involved in the biosynthesis of factor 420, a redox-active cofactor, in methanogenic archaea and certain bacteria.
The specific reaction catalyzed in vivo is determined by the availability of substrate, which in turn is determined by the enzyme present in the organism - EC 2.7.7.68, EC 2.7.7.105, or EC 2.7.7.106.
(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0.
7,8-didemethyl-8-hydroxy-5-deazariboflavin + enolpyruvoyl-2-diphospho-5'-guanosine = dehydro coenzyme F420-0 + GMP + H(+).
3-[(R)-glyceryl]-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized 3PG-factor420-0.
L-serine-phosphatidylethanolamine phosphatidyltransferase
This mammalian enzyme catalyzes an exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine.
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine.
undecaprenyl-phosphate glucose phosphotransferase
undecaprenylphosphate glucosylphosphate transferase
The enzyme is involved in biosynthesis of xanthan.
di-trans,octa-cis-undecaprenyl phosphate + UDP-alpha-D-glucose = alpha-D-glucosyl di-trans,octa-cis-undecaprenyl diphosphate + UMP.
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose xylosylphosphotransferase
The enzyme is specific for mannose as an acceptor but is flexible as to the structural context of the mannosyl disaccharide.
3-alpha-D-mannopyranosyl-alpha-D-mannopyranose + UDP-alpha-D-xylose = 3-O-(6-O-alpha-D-xylosylphospho-alpha-D-mannopyranosyl)-alpha-D-mannopyranose + H(+) + UMP.
UDP-N-acetylglucosamine--undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
This enzyme catalyzes the synthesis of N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components.
The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 and of teichoic acid in certain Gram-positive bacteria.
di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP.
CDP-L-myo-inositol myo-inositolphosphotransferase
The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-1L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors.
The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+).
UDP-N-acetylglucosamine--decaprenyl-phosphate N-acetylglucosaminephosphotransferase
UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase
Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis.
This enzyme catalyzes the synthesis of monotrans,octacis-decaprenyl-N-acetyl-alpha-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components.
trans,octa-cis-decaprenyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-1-diphospho-trans,octa-cis-decaprenol + UMP.
undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase
tri-trans,hepta-cis-undecaprenyl phosphate + UDP-N,N'-diacetylbacillosamine = N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UMP.
alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase
Isolated from the bacterium Escherichia coli.
ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate.
Isolated from the archaeon Methanothermobacter thermautotrophicus.
CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + L-serine = archaetidylserine + CMP + H(+).
CDP-2,3-bis-O-(phytanyl)-sn-glycerol + L-serine = 2,3-bis-O-phytanyl-sn-glycero-3-phospho-L-serine + CMP + H(+).
The enzyme is involved in biosynthesis of archaetidyl-myo-inositol, a compound essential for glycolipid biosynthesis in archaea.
1D-myo-inositol 3-phosphate + CDP-2,3-bis-O-(phytanyl)-sn-glycerol = CMP + H(+) + saturated 1-archaetidyl-1D-myo-inositol 3-phosphate.
UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-acetylgalactosaminephosphotransferase
The enzyme catalyzes a step in the assembly of the repeating-unit of the O-antigen of the Gram-negative bacterium Aeromonas hydrophila AH-3.
The enzyme shows no activity with UDP-N-acetyl-alpha-D-glucosamine (Cf. EC 2.7.8.33).
di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-galactosamine = N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP.
The eukaryotic enzyme is involved in the biosynthesis of the mitochondrial phospholipid cardiolipin.
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-diacyl-sn-glycerol = a cardiolipin + CMP + H(+).
Kdo2-lipid A phosphoethanolamine 7''-transferase
The enzyme has been characterized from the bacterium Escherichia coli.
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A = 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + a 1,2-diacyl-sn-glycerol.
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA = 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + a 1,2-diacyl-sn-glycerol.
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups.
It will also act on lipid IVA and Kdo2-lipid A.
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H(+) + lipid A (E. coli) = a 1,2-diacyl-sn-glycerol + lipid A hexaacyl 1-(2-aminoethyl diphosphate).
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H(+) + lipid A (E. coli) = a 1,2-diacyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate) (E. coli).
a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H(+) + lipid A hexaacyl 1-(2-aminoethyl diphosphate) = a 1,2-diacyl-sn-glycerol + lipid A 1,4'-bis(2-aminoethyl diphosphate).
teichoic acid glycerol-phosphate primase
This enzyme adds the first glycerol unit to the disaccharide linker of the teichoic acid.
CDP-glycerol + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate = 4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CMP + H(+).
teichoic acid glycerol-phosphate transferase
Involved in the biosynthesis of teichoic acid linkage units in the cell walls of some bacteria such as Staphylococcus aureus.
This enzyme adds a second glycerol unit to the disaccharide linker of the teichoic acid.
4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CDP-glycerol = 4-O-[di(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CMP + H(+).
Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23.
This enzyme adds the first ribitol unit to the disaccharide linker of the teichoic acid.
4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CDP-L-ribitol = 4-O-[1-D-ribitylphospho-(2R)-1-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CMP + H(+).
teichoic acid ribitol-phosphate polymerase
This enzyme adds the 25-35 ribitol units to the linker molecule.
4-O-[1-D-ribitylphospho-(2R)-1-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CDP-L-ribitol = 4-O-[(D-ribitylphospho)(n)-D-ribitylphospho-(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CMP + n H(+).
an N-acylsphing-4-enine + CDP-ethanolamine = an N-acylsphing-4-enine 1-phosphoethanolamine + CMP + H(+).
an N-acyl-sphingoid base + CDP-ethanolamine = an N-acyl-sphingoid 1-phosphoethanolamine + CMP + H(+).
Phosphotransferases with paired acceptors
ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate.
ATP + L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] + phosphate = AMP + diphosphate + H(+) + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase].
N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] + pyruvate = L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] + phosphoenolpyruvate.
ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate.
ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate + selenophosphate.
ATP appears to be the only phosphate donor.
No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate.
The protein phosphorylates glucans exclusively at O-6 of glucosyl residues.
The protein phosphorylates itself with the beta-phosphate of ATP, which is then transferred to the glucan.
[(1->4)-alpha-D-glucosyl](n) + n ATP + n H2O = [(1->4)-6-phospho-alpha-D-glucosyl](n) + n AMP + 2n H(+) + n phosphate.
The enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4; there is no activity with unphosphorylated glucans.
It transfers the beta-phosphate of ATP to the phosphoglucan, whereas the gamma-phosphate is transferred to water.
In contrast to EC 2.7.9.4, which phosphorylates the glucose groups in glucans predominantly on O-6, this enzyme phosphorylates glucose groups in phosphorylated starch predominantly on O-3.
[(1->4)-6-phospho-alpha-D-glucosyl](n) + n ATP + n H2O = [(1->4)-3,6-bisphospho-alpha-D-glucosyl](n) + n AMP + 2n H(+) + n phosphate.
The enzyme, characterized from a diverse collection of Gram-positive bacteria, inactivates the antibiotic rifampicin by phosphorylating it at position 21.
The enzyme comprises three domains: two substrate-binding domains (ATP-grasp and rifampicin-binding domains) and a smaller phosphate-carrying L-histidine swivel domain that transits between the spatially distinct substrate-binding sites during catalysis.
ATP + H2O + rifampicin = 21-phosphorifampicin + AMP + 2 H(+) + phosphate.
The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].
Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain.
In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families.
non-specific serine/threonine protein kinase
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein].
[pyruvate dehydrogenase (acetyl-transferring)] kinase
pyruvate dehydrogenase kinase (phosphorylating)
Has no activating compound but is specific for its substrate.
A mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals.
ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit].
hydroxymethylglutaryl coenzyme A reductase kinase kinase
Activated by AMP and is specific for its substrate.
Phosphorylates and activates EC 2.7.11.31 which has been inactivated by EC 3.1.3.16.
ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase] = ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase].
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase
branched-chain 2-oxo acid dehydrogenase kinase
branched-chain alpha-ketoacid dehydrogenase kinase
branched-chain keto acid dehydrogenase kinase
branched-chain oxo acid dehydrogenase kinase (phosphorylating)
A mitochondrial enzyme associated with the branched-chain 2-oxoacid dehydrogenase complex.
ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase].
[isocitrate dehydrogenase (NADP(+))] kinase
isocitrate dehydrogenase kinase/phosphatase
isocitrate dehydrogenase kinase (phosphorylating)
Phosphorylates and inactivates EC 1.1.1.42.
ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[isocitrate dehydrogenase].
pheochromocytoma tyrosine hydroxylase-associated kinase
tyrosine 3-monooxygenase kinase (phosphorylating)
Has no activating compound but is specific for its substrate, with which it copurifies.
Activates EC 1.14.16.2 by phosphorylation.
ATP + L-seryl-[tyrosine-3-monooxygenase] = ADP + H(+) + O-phospho-L-seryl-[tyrosine-3-monooxygenase].
calmodulin-dependent myosin heavy chain kinase
The enzyme from Dictyostelium sp. (slime molds) brings about phosphorylation of the heavy chains of Dictyostelium myosin, inhibiting the actin-activated ATPase activity of the myosin.
One threonine residue in each heavy chain acts as acceptor.
While the enzyme from some species is activated by actin, in other cases Ca(2+)/calmodulin are required for activity.
ATP + L-threonyl-[myosin heavy-chain] = ADP + H(+) + O-phospho-L-threonyl-[myosin heavy-chain].
This enzyme is activated during Fas-mediated apoptosis.
Following Fas ligation, the enzyme, which is constitutively phosphorylated, is dephosphorylated, and it is the dephosphorylated form that causes phosphorylation of TIA-1, a nuclear RNA-binding protein.
Phosphorylation of TIA-1 precedes the onset of DNA fragmentation.
ATP + L-seryl-[Fas-activated protein] = ADP + H(+) + O-phospho-L-seryl-[Fas-activated protein].
ATP + L-threonyl-[Fas-activated protein] = ADP + H(+) + O-phospho-L-threonyl-[Fas-activated protein].
[Goodpasture-antigen-binding protein] kinase
Goodpasture antigen-binding protein kinase
This serine/threonine kinase specifically binds to and phosphorylates the N-terminal region of the human Goodpasture antigen, which is located on the alpha3 chain of collagen IV and is involved in autoimmune disease.
ATP + L-seryl-[Goodpasture antigen-binding protein] = ADP + H(+) + O-phospho-L-seryl-[Goodpasture antigen-binding protein].
ATP + L-threonyl-[Goodpasture antigen-binding protein] = ADP + H(+) + O-phospho-L-threonyl-[Goodpasture antigen-binding protein].
Phosphorylates IkappaB proteins at specific serine residues, which marks them for destruction via the ubiquitination pathway.
Subsequent degradation of the IkappaB complex (IKK) activates NF-kappaB, a translation factor that plays an important role in inflammation, immunity, cell proliferation and apoptosis.
If the serine residues are replaced by threonine residues, the activity of the enzyme is decreased considerably.
ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein].
This eukaryotic enzyme recognizes the sequence -Arg-Arg-X-Ser*/Thr*-Hpo, where * indicates the phosphorylated residue and Hpo indicates a hydrophobic residue.
The inactive holoenzyme is a heterotetramer composed of two regulatory (R) subunits and two catalytic (C) subunits.
Each R subunit occludes the active site of a C subunit and contains two binding sites for 3',5'-cyclic-AMP (cAMP).
Binding of cAMP activates the enzyme by causing conformational changes that release two free monomeric C subunits from a dimer of the R subunits, i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C.
Activity requires phosphorylation of a conserved Thr in the activation loop (T-loop) sequence (Thr(198) in human Calpha; Thr(224) in budding yeast Tpk2), installed by auto-phosphorylation or by the 3-phosphoinositide-dependent protein kinase-1 (PDPK1).
Certain R2C2 combinations can be localized to particular subcellular regions by their association with diverse species of 'A Kinase-Anchoring Proteins' (AKAPs).
The enzyme has been characterized from many organisms. Humans have three C units (Calpha, Cbeta, and Cgamma) encoded by the paralogous genes PRKACA, PRKACB and PRKACG, respectively, and four R subunits (R1alpha, RIbeta, RIIalpha and RIIbeta), encoded by PKRAR1A, PKRAR1B, PKRAR2A and PKRAR2B, respectively. Yeast (Saccharomyces cerevisiae) has three C subunits (Tpk1, Tpk2, and Tpk3) encoded by the paralogous genes TPK1, TPK2 and TPK3, respectively, and a single R subunit (Bcy1) encoded by the BCY1 gene.
Some validated substrates of the enzyme include cAMP-response element-binding protein (CREB), phosphorylase kinase alpha subunit (PHKA), and tyrosine 3-monooxygenase (TH) in mammals; Adr1, Whi3, Nej1, and Pyk1 in yeast.
3':5'-cyclic GMP-dependent protein kinase
guanosine 3':5'-cyclic monophosphate-dependent protein kinase
cGMP is required to activate this enzyme.
The enzyme occurs as a dimer in higher eukaryotes.
The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites.
This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates.
The enzyme also has two allosteric cGMP-binding sites (sites A and B).
Binding of cGMP causes a conformational change that is associated with activation of the kinase.
calcium/phospholipid dependent protein kinase
A family of serine- and threonine-specific protein kinases that depend on lipids for activity.
They can be activated by calcium but have a requirement for the second messenger diacylglycerol.
Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signaling pathways.
Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters.
Acts on the bleached or activated form of rhodopsin.
Also phosphorylates the beta-adrenergic receptor, but more slowly.
Does not act on casein, histones or phosphovitin.
Inhibited by Zn(2+) and digitonin (cf. EC 2.7.11.15 and EC 2.7.11.16).
ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-[rhodopsin].
ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-threonyl-[rhodopsin].
beta-adrenergic-receptor kinase (phosphorylating)
beta-adrenergic receptor-specific kinase
Acts on the agonist-occupied form of the receptor; also phosphorylates rhodopsin, but more slowly.
Inhibited by Zn(2+) and digitonin but is unaffected by cyclic-AMP (cf. EC 2.7.11.14 and EC 2.7.11.16).
[beta-adrenergic receptor] + ATP = [beta-adrenergic receptor]-phosphate + ADP + H(+).
All members of this enzyme subfamily possess a highly conserved binding site for 1-phosphatidylinositol 4,5-bisphosphate.
[G-protein-coupled receptor] + ATP = [G-protein-coupled receptor]-phosphate + ADP + H(+).
calcium/calmodulin-dependent protein kinase
Ca(2+)/calmodulin-dependent microtubule-associated protein 2 kinase
Ca(2+)/calmodulin-dependent protein kinase 1
Ca(2+)/calmodulin-dependent protein kinase II
Ca(2+)/calmodulin-dependent protein kinase IV
Ca(2+)/calmodulin-dependent protein kinase kinase
Ca(2+)/calmodulin-dependent protein kinase kinase beta
calcium/calmodulin-dependent protein kinase type II
A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule-associated tau protein.
Not identical with EC 2.7.11.18 or EC 2.7.11.26.
calcium/calmodulin-dependent myosin light chain kinase
myosin light-chain kinase (phosphorylating)
The 20 kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, more slowly.
ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain].
ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-phospho-L-threonyl-[myosin light chain].
The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b.
For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase.
The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b.
The gamma subunit of the tetrameric alphabetagammadelta enzyme is the catalytic subunit.
2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
Can also be phosphorylated by the catalytic subunit of EC 2.7.11.11.
Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca(2+).
[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+).
The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation.
The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein.
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin.
It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
Appears to be distinct from other protein phosphokinases.
Brings about multiple phosphorylation of the unique C-terminal repeat domain of the largest subunit of eukaryotic EC 2.7.7.6.
Does not phosphorylate casein, phosvitin or histone.
[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase].
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2 is necessary for enzyme activation.
Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline.
A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY).
Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation.
Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury.
mitogen-activated protein kinase kinase kinase
MLK-like mitogen-activated protein triple kinase
This enzyme phosphorylates and activates its downstream protein kinase, EC 2.7.12.2, but requires MAPKKKK for activation.
Some members of this family can be activated by p21-activated kinases (PAK/STE20) or Ras.
While c-Raf and c-Mos activate the classical MAPK/ERK pathway, MEKK1 and MEKK2 preferentially activate the c-Jun N-terminal protein kinase(JNK)/stress-activated protein kinase (SAPK) pathway.
Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease.
ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein].
ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein].
acetyl-CoA carboxylase kinase (AMP-activated)
acetyl-CoA carboxylase kinase (cAMP-independent)
acetyl coenzyme A carboxylase kinase (phosphorylating)
Phosphorylates and inactivates EC 6.4.1.2, which can be dephosphorylated and reactivated by EC 3.1.3.17.
More active toward the dimeric form of acetyl-CoA carboxylase than the polymeric form.
ATP + L-seryl-[acetyl-CoA carboxylase] = ADP + H(+) + O-phospho-L-seryl-[acetyl-CoA carboxylase].
Phosphorylates casein equally well, and histone and phosvitin to a lesser extent.
ATP + [tropomyosin] = ADP + [tropomyosin] phosphate.
[low-density-lipoprotein receptor] kinase
low-density-lipoprotein receptor kinase (phosphorylating)
Phosphorylates the last serine residue (Ser-833) in the cytoplasmic domain of the low-density lipoprotein receptor.
Casein can also act as a substrate but with lower affinity.
ATP + L-seryl-[low-density-lipoprotein receptor] = ADP + H(+) + O-phospho-L-seryl-[low-density-lipoprotein receptor].
receptor protein serine/threonine kinase
receptor serine/threonine protein kinase
receptor type II serine/threonine protein kinase
receptor type I serine/threonine protein kinase
The transforming growth factor beta (TGF-beta) family of cytokines regulates cell proliferation, differentiation, recognition and death.
Signaling occurs by the binding of ligand to the type II receptor, which is the constitutively active kinase.
Bound TGF-beta is then recognized by receptor I, which is phosphorylated and can propagate the signal to downstream substrates.
ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein].
ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein].
[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase
[hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase
3-hydroxy-3-methylglutaryl-CoA reductase kinase
3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
hydroxymethylglutaryl-CoA reductase kinase
hydroxymethylglutaryl coenzyme A reductase kinase
hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating)
EC 1.1.1.34 is inactivated by the phosphorylation of the enzyme protein.
Can also phosphorylate EC 6.4.1.2 and EC 3.1.1.79.
Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase.
ATP + L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] = ADP + H(+) + O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase].
The enzyme from the plants Zea mays (maize) and Arabidopsis is bifunctional and catalyzes both the phosphorylation and dephosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.4.27.
The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates an active site histidine.
ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase].
The enzyme from the bacterium Escherichia coli is bifunctional and catalyzes both the phosphorylation and dephosphorylation of EC 2.7.9.2; cf. EC 2.7.4.28.
The enzyme is specific for a reaction intermediate form of EC 2.7.9.2, where it phosphorylates an active site histidine.
It has no activity toward EC 2.7.9.1, (cf. EC 2.7.11.32).
[pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+).
Dual-specificity kinases (those acting on Ser/Thr and Tyr residues)
This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
A dual-specific protein kinase and requires mitogen-activated protein kinase kinase kinase (MAPKKK) for activation.
It is required for activation of EC 2.7.11.24.
Phosphorylation of MEK1 by Raf involves phosphorylation of two serine residues.
A number of histones can act as acceptor.
ATP + L-histidyl-[protein] = ADP + H(+) + N(pros)-phospho-L-histidyl-[protein].
ATP + L-histidyl-[protein] = ADP + H(+) + N(tele)-phospho-L-histidyl-[protein].
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine).
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
The enzyme, characterized from Gram-positive bacteria, is involved in the regulation of the bacterial stress response.
ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein].
triphosphate--protein phosphotransferase
pyrophosphate-protein phosphotransferase
This enzyme was originally thought to use diphosphate as substrate but this has since been disproved.
The activity is observed as the second part of a biphasic reaction after depletion of ATP.
Tripolyphosphate is a contaminant of [gamma-(32)P]ATP.
triphosphate + [microsomal-membrane protein] = diphosphate + [microsomal-membrane protein] phosphate.
A few other sulfur compounds can act as donors.
hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate.
The enzyme catalyzes a transsulfuration reaction from 3-mercaptopyruvate to an internal cysteine residue.
In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide.
The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate.
glutathione-dependent thiosulfate reductase
The primary product is glutathione hydrodisulfide, which reacts with glutathione to give glutathione disulfide and sulfide.
2 glutathione + thiosulfate = glutathione disulfide + 2 H(+) + hydrogen sulfide + sulfite.
The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide.
The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP.
The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA.
The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.
[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme from Chlorella shows very little activity toward monothiols such as glutathione and cysteine (cf. EC 2.8.1.3).
The enzyme probably transfers the sulfur atom onto one thiol group to form -S-S(-), and sulfide is spontaneously expelled from this by reaction with the other thiol group.
dithioerythritol + thiosulfate = cis-1,2-dithiane-4,5-diol + 2 H(+) + hydrogen sulfide + sulfite.
The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster.
In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and 4,5-secobiotin.
Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-S hydrogen atom from 4,5-secobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring.
The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover.
In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis.
(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin].
The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors.
The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin).
In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine.
This enzyme catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C6 and C8 of a pendant octanoyl chain.
It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur center.
The enzyme contains two [4Fe-4S] clusters.
The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C6 and C8, respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster.
Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins.
Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein.
An alternative lipoylation pathway involves EC 6.3.1.20, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs).
[[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin].
Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide.
The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes.
In prokaryotes the reaction is catalyzed by two enzymes: EC 2.8.1.7, which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.
AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdopterin.
Part of the pathway for thiamine biosynthesis.
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O.
molybdopterin synthase sulfurtransferase
The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC 2.8.1.12.
In the human, the reaction is catalyzed by the rhodanese-like C-terminal domain (cf. EC 2.8.1.1) of the MOCS3 protein, a bifunctional protein that also contains EC 2.7.7.80 at the N-terminal domain.
[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase].
Catalyzes the synthesis of molybdopterin from cyclic pyranopterin phosphate.
Two sulfur atoms are transferred to cyclic pyranopterin phosphate in order to form the characteristic ene-dithiol group found in the molybdenum cofactor.
Molybdopterin synthase consists of two large subunits forming a central dimer and two small subunits (molybdopterin-synthase sulfur-carrier proteins) that are thiocarboxylated at the C-terminus by EC 2.8.1.11, molybdopterin synthase sulfurtransferase.
2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin.
The enzyme, found in bacteria, catalyzes formation of the 2-thiouridine modification in the wobble position of tRNA(Gln), tRNA(Lys) and tRNA(Glu).
AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein].
tRNA-5-taurinomethyluridine 2-sulfurtransferase
The enzyme, found in mitochondria, catalyzes formation of 5-taurinomethyl-2-thiouridine in the wobble position of mitochondrial tRNA(Gln), tRNA(Lys) and tRNA(Glu).
5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein].
tRNA-5-methyluridine(54) 2-sulfurtransferase
The enzyme, found in thermophilic bacteria such as Thermus thermophilus and archaea such as Pyrococcus horikoshii, modifies the ribothymidine (5-methyluridine) residue at position 54 of tRNAs.
5-methyluridine(54) in tRNA + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + ATP + H2O = 5-methyl-2-thiouridine(54) in tRNA + [TtuB sulfur-carrier protein]-C-terminal Gly-Gly + AMP + diphosphate + 2 H(+).
L-aspartate semialdehyde sulfurtransferase
The enzyme, characterized from the archaeon Methanosarcina acetivorans, participates in an L-methionine biosysnthetic pathway found in most of the methanogenic archaea.
3 H(+) + hydrogen sulfide + L-aspartate 4-semialdehyde + reduced 2[4Fe-4S]-[ferredoxin] = H2O + L-homocysteine + oxidized 2[4Fe-4S]-[ferredoxin].
A number of aromatic compounds can act as acceptors.
Organic hydroxylamines are not substrates (cf. EC 2.8.2.9).
3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+).
Primary and secondary alcohols, including aliphatic alcohols, ascorbate, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15).
3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+).
A large number of primary and secondary amines can act as acceptors, including aniline, 2-naphthylamine, cyclohexylamine and octylamine.
3'-phosphoadenylyl sulfate + a primary amine = a sulfamate + adenosine 3',5'-bisphosphate + 2 H(+).
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate + H(+).
The sulfation is at the 4-position of N-acetylgalactosamine residues of chondroitin.
n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+).
3'-phosphoadenylyl sulfate + choline = adenosine 3',5'-bisphosphate + choline sulfate + H(+).
UDP-N-acetylgalactosamine-4-sulfate sulfotransferase
3'-phosphoadenylyl sulfate + UDP-N-acetyl-alpha-D-galactosamine 4-sulfate = adenosine 3',5'-bisphosphate + H(+) + UDP-N-acetyl-alpha-D-galactosamine 4,6-bissulfate.
[heparan sulfate]-glucosamine N-sulfotransferase
3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase
3'-phosphoadenylyl-sulfate:N-desulfoheparin N-sulfotransferase
3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase
glucosaminyl N-deacetylase/N-sulfotransferase
heparan sulfate N-deacetylase/N-sulfotransferase
The enzyme also catalyzes the sulfation of chondroitin 4-sulfate and dermatan sulfate, but to a much more limited extent.
3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n).
Phenols and organic hydroxylamines can act as acceptors (cf. EC 2.8.2.1).
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + H(+) + L-tyrosine methyl ester 4-sulfate.
The product may be identical with Watasenia luciferin.
3'-phosphoadenylyl sulfate + coelenterazine h = adenosine 3',5'-bisphosphate + H(+) + luciferyl sulfate.
Also acts on lactosylceramide and monogalactosylalkylacylglycerol.
3'-phosphoadenylyl sulfate + a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine = adenosine 3',5'-bisphosphate + H(+) + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine.
3'-phosphoadenylyl sulfate + a 1-O-alkyl-2-acyl-3-O-(beta-D-galactosyl)-sn-glycerol = a 1-O-alkyl-2-acyl-3-(beta-D-3-sulfogalactosyl)-sn-glycerol + adenosine 3',5'-bisphosphate + H(+).
3'-phosphoadenylyl sulfate + beta-D-galactosyl-(1<->1)-sphing-4-enine = 6-O-sulfo-beta-D-galactosyl-(1<->1)-sphing-4-enine + adenosine 3',5'-bisphosphate + H(+).
bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase
bile salt:3'phosphoadenosine-5'-phosphosulfate:sulfotransferase
The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species.
This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase.
In addition to the 5beta-bile acid glycolithocholate, deoxycholate, 3beta-hydroxy-5-cholenoate and dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) also act as substrates (see also EC 2.8.2.2 and EC 2.8.2.34).
3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + H(+) + sulfoglycolithocholate.
3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + H(+) + taurolithocholate 3-sulfate.
Broad specificity resembling EC 2.8.2.2, but also acts on estrone.
3'-phosphoadenylyl sulfate + a phenolic steroid = a phenolic steroid 3-O-sulfate + adenosine 3',5'-bisphosphate + H(+).
Also acts on dithiols; substrates include glutathione, dithioerythritol and 2,3-bis(sulfanyl)propan-1-ol.
3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + H(+) + S-alkyl thiosulfate.
The sulfation is at the 6-position of N-acetylgalactosamine residues of chondroitin.
n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+).
3'-phosphoadenylyl sulfate + cortisol = adenosine 3',5'-bisphosphate + cortisol 21-sulfate + H(+).
triglucosylalkylacylglycerol sulfotransferase
3'-phosphoadenylyl sulfate + alpha-D-glucosyl-(1->6)-alpha-D-glucosyl-(1->6)-alpha-D-glucosyl-(1->3)-1-alkyl-2-acylglycerol = 6-sulfo-alpha-D-glucosyl-(1->6)-alpha-D-glucosyl-(1->6)-alpha-D-glucosyl-(1->3)-1-alkyl-2-acylglycerol + adenosine 3',5'-bisphosphate + H(+).
The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors.
3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein].
Sulfation takes place at the 6-position of galactosyl and N-acetylglucosaminyl residues in keratan, a proteoglycan.
Not identical with EC 2.8.2.5, EC 2.8.2.6 or EC 2.8.2.17.
3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate.
Hydroxy groups of tyrosine residues in peptides such as angiotensin can act as acceptors.
Does not act on 3'-phosphoadenylyl sulfate or adenosine 3',5'-bisphosphate.
a phenol + an aryl sulfate = a phenol + an aryl sulfate.
[heparan sulfate]-glucosamine 3-sulfotransferase 1
3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase
heparan sulfate D-glucosaminyl 3-O-sulfotransferase
heparin-glucosamine 3-O-sulfotransferase
This enzyme differs from EC 2.8.2.29 and EC 2.8.2.30 by being the most selective for a precursor of the antithrombin-binding site.
It has a minimal acceptor sequence of: -> GlcNAc6S->GlcA-> GlcN2S*+-6S->IdoA2S->GlcN2S->.
It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites.
These precursors are variants of the consensus sequence: -> Glc(N2S>NAc)+-6S->GlcA->GlcN2S*+-6S->GlcA>IdoA+-2S-> Glc(N2S/NAc)+-6S->.
If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA.
3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+).
aromatic desulfoglucosinolate sulfotransferase
PAPS-desulfoglucosinolate sulfotransferase
This enzyme, characterized from cruciferous plants, catalyzes the last step in the biosynthesis of tryptophan- and phenylalanine-derived glucosinolates.
(Z)-desulfoglucotropeolin + 3'-phosphoadenylyl sulfate = (Z)-glucotropeolin + adenosine 3',5'-bisphosphate + H(+).
(Z)-indolylmethyl desulfoglucosinolate + 3'-phosphoadenylyl sulfate = (Z)-glucobrassicin + adenosine 3',5'-bisphosphate + H(+).
Also acts on some other flavonol aglycones.
3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + H(+) + quercetin 3-sulfate.
3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + H(+) + quercetin 3,3'-bissulfate.
3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + H(+) + quercetin 3,4'-bissulfate.
quercetin-3,3'-bissulfate 7-sulfotransferase
Quercetin 3,4'-bissulfate can also act as acceptor.
3'-phosphoadenylyl sulfate + quercetin 3,3'-bissulfate = adenosine 3',5'-bisphosphate + H(+) + quercetin 3,3',7-trissulfate.
[heparan sulfate]-glucosamine 3-sulfotransferase 2
heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2
This enzyme sulfates the residues marked with an asterisk in sequences containing at least ->IdoA2S->GlcN*-> or ->GlcA2S->GlcN*->.
Preference for GlcN2S versus unmodified GlcN has not yet been established.
Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant.
This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 prefers GlcA or IdoA, whereas EC 2.8.2.30 prefers IdoA2S.
[heparan sulfate]-glucosamine 3-sulfotransferase 3
heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3
Two major substrates contain the tetrasaccharides: -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN*-> and -> undetermined 2-sulfo-uronic acid->GlcN2S->IdoA2S->GlcN6S*-> with modification of the N-unsubstituted glucosamine residue (shown with an asterisk).
Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded.
The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells.
There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes.
The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases.
It is inefficient at modifying precursors of the antithrombin binding site (in contrast to EC 2.8.2.23) and it does not modify glucosamine preceded by GlcA2S (unlike EC 2.8.2.29).
The enzyme from the lamprey Petromyzon marinus can also use the corresponding 3-ketone as a substrate.
It is stereoselective (5alpha-cholane) and regioselective, exhibiting a preference for an hydroxy group at C-24.
The enzyme is inactive when allocholic acid, which has a carboxy group at C-24, is used as a substrate.
3'-phosphoadenylyl sulfate + 5alpha-cholane-3alpha,7alpha,12alpha,24-tetrol = 3alpha,7alpha,12alpha-trihydroxy-5alpha-cholan-24-yl sulfate + adenosine 3',5'-bisphosphate + H(+).
The enzyme from the shark Heterodontus portusjacksoni is able to sulfate the C27 bile salts 5beta-scymnol (the natural bile salt) and 5alpha-cyprinol (the carp bile salt).
Enzyme activity is activated by Mg(2+) but inhibited by the product 5beta-scymnol sulfate.
3'-phosphoadenylyl sulfate + 5beta-scymnol = 5beta-scymnol sulfate + adenosine 3',5'-bisphosphate + H(+).
N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
The enzyme from human transfers sulfate to position 6 of both internal residues and non-reducing terminal GalNAc 4-sulfate residues of chondroitin sulfate.
Oligosaccharides derived from chondroitin sulfate also serve as acceptors but chondroitin sulfate E, keratan sulfate and heparan sulfate do not.
Differs from EC 2.8.2.17 in being able to use both chondroitin and dermatan as effective substrates.
n 3'-phosphoadenylyl sulfate + dermatan 4'-sulfate = n adenosine 3',5'-bisphosphate + dermatan 4',6'-bissulfate + n H(+).
n 3'-phosphoadenylyl sulfate + chondroitin 4'-sulfate = n adenosine 3',5'-bisphosphate + chondroitin 4',6'-bissulfate + n H(+).
Specifically sulfates glycochenodeoxycholate at the 7alpha-position (see also EC 2.8.2.14).
The monohydroxy bile acids glycolithocholate, chenodeoxycholate and ursodeoxycholate act as inhibitors.
3'-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate + H(+).
dermatan N-acetylgalactosamine 4-O-sulfotransferase
dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase
The sulfation takes place at the 4-position of N-acetylgalactosamine residues of dermatan.
D4ST-1 shows a strong preference in vitro for sulfate transfer to IdoUAalpha(1,3)GalNAcbeta(1,4) that is flanked by GlcUAbeta(1,3)GalNAcbeta(1,4) as compared with IdoUAalpha(1,3)GalNAcbeta(1,4) flanked by IdoUAalpha(1,3)GalNAcbeta(1,4).
n 3'-phosphoadenylyl sulfate + dermatan = n adenosine 3',5'-bisphosphate + dermatan 4'-sulfate + n H(+).
The enzyme from the bacterium Streptomyces toyocaensis catalyzes the final step in the biosynthesis of the glycopeptide antibiotic A47934, a naturally occurring antibiotic of the vancomycin group.
3'-phosphoadenylyl sulfate + desulfo-A47934 = A47934 + adenosine 3',5'-bisphosphate + H(+).
The sulfation of trehalose in the bacterium Mycobacterium tuberculosis is required for the biosynthesis of sulfolipid-1.
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-sulfo-alpha,alpha-trehalose + adenosine 3',5'-bisphosphate + H(+).
aliphatic desulfoglucosinolate sulfotransferase
The enzyme catalyzes the last step in the biosynthesis of aliphatic glucosinolate core structures.
3'-phosphoadenylyl sulfate + an aliphatic (Z)-desulfo-glucosinolate = a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate S-glucoside + adenosine 3',5'-bisphosphate + H(+).
The enzyme, charaterized from the plant Arabidopsis thaliana, also acts on 11-hydroxyjasmonate.
3'-phosphoadenylyl sulfate + a 12-hydroxyjasmonate = a 12-sulfojasmonate + adenosine 3',5'-bisphosphate + H(+).
3'-phosphoadenylyl sulfate + an 11-hydroxyjasmonate = adenosine 3',5'-bisphosphate + an 11-sulfojasmonate + H(+).
omega-hydroxy-beta-dihydromenaquinone-9 sulfotransferase
The enzyme catalyzes the last step in the production of omega-sulfo-beta-dihydromenaquinone-9 by members of the Mycobacterium tuberculosis complex.
3'-phosphoadenylyl sulfate + omega-hydroxy-beta-dihydromenaquinone-9 = adenosine 3',5'-bisphosphate + H(+) + omega-sulfo-beta-dihydromenaquinone-9.
The enzyme is involved in the metabolism of the hormone thyroxine.
3'-phosphoadenylyl sulfate + thyroxine = adenosine 3',5'-bisphosphate + H(+) + thyroxine sulfate.
Butanoate and lactate can also act as acceptors.
acetyl-CoA + propanoate = acetate + propanoyl-CoA.
oxalate + succinyl-CoA = oxalyl-CoA + succinate.
The enzyme from Pseudomonas ovalis also catalyzes the reaction of EC 4.1.1.9.
acetyl-CoA + malonate = acetate + malonyl-CoA.
Acetoacetate or, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptor.
Malonyl-CoA can act instead of succinyl-CoA.
a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate.
acetoacetate + succinyl-CoA = acetoacetyl-CoA + succinate.
beta-ketoadipate:succinyl-CoA transferase
The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate.
3-oxoadipate + succinyl-CoA = 3-oxoadipyl-CoA + succinate.
The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism.
The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue.
Unlike EC 2.8.3.9, this enzyme exhibits maximal activity using acetate as the CoA acceptor.
Substrate range depends on the specific enzyme.
Typical substrates include butanoyl-CoA and pentanoyl-CoA.
acetate + an acyl-CoA = a carboxylate + acetyl-CoA.
Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C2 to C6 monocarboxylic acids.
acetoacetate + butanoyl-CoA = acetoacetyl-CoA + butanoate.
Also catalyzes the transfer of thioacyl carrier protein from its acetyl thioester to citrate.
acetyl-CoA + citrate = (3S)-citryl-CoA + acetate.
Also catalyzes the transfer of thioacyl carrier protein from its acetyl thioester to citramalate.
acetyl-CoA + citramalate = (3S)-citramalyl-CoA + acetate.
Glutarate, (R)-2-hydroxyglutarate, propenoate and propanoate, but not (Z)-glutaconate, can also act as acceptors.
acetyl-CoA + trans-glutaconate = (2E)-glutaconyl-CoA + acetate.
succinate--hydroxymethylglutarate CoA-transferase
Malonyl-CoA can also act as donor, more slowly.
3-hydroxy-3-methylglutarate + succinyl-CoA = (3S)-hydroxy-3-methylglutaryl-CoA + succinate.
3-hydroxy-3-methylglutarate + malonyl-CoA = (3S)-hydroxy-3-methylglutaryl-CoA + malonate.
Propanoyl-CoA, acetyl-CoA, butanoyl-CoA and some other acyl-CoAs can act as substrates, more slowly than 5-hydroxypentanoyl-CoA.
5-hydroxypentanoate + acetyl-CoA = 5-hydroxy-pentanoyl-CoA + acetate.
succinyl-CoA:(R)-benzylsuccinate CoA-transferase
Involved in anaerobic catabolism of toluene and is a strictly toluene-induced enzyme that catalyzes the reversible regio- and enantio-selective synthesis of (R)-2-benzylsuccinyl-CoA.
The enzyme from Thauera aromatica is inactive when (R)-benzylsuccinate is replaced by (S)-benzylsuccinate.
(R)-2-benzylsuccinate + succinyl-CoA = (R)-2-benzylsuccinyl-CoA + succinate.
The enzyme from Oxalobacter formigenes can also catalyze the transfer of CoA from formyl-CoA to succinate.
formyl-CoA + oxalate = formate + oxalyl-CoA.
formyl-CoA + succinate = formate + succinyl-CoA.
3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase
It forms a complex with (R)-3-(aryl)lactoyl-CoA dehydratase.
(E)-cinnamoyl-CoA + (R)-3-phenyllactate = (E)-cinnamate + (R)-3-phenyllactoyl-CoA.
(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + (E)-4-coumaroyl-CoA = (E)-4-coumarate + (R)-3-(4-hydroxyphenyl)lactoyl-CoA.
(E)-3-(indol-3-yl)acryloyl-CoA + (R)-3-(indol-3-yl)lactate = (E)-3-(indol-3-yl)acrylate + (R)-3-(indol-3-yl)lactoyl-CoA.
In some bacteria the enzyme catalyzes the conversion of acetate to acetyl-CoA as part of a modified tricarboxylic acid (TCA) cycle.
In other organisms it converts acetyl-CoA to acetate during fermentation.
In some organisms the enzyme also catalyzes the activity of EC 2.8.3.27.
acetate + succinyl-CoA = acetyl-CoA + succinate.
The enzymes characterized from the bacteria Escherichia coli and Acetobacter aceti can also use formyl-CoA and oxalate (EC 2.8.3.16) or formyl-CoA and acetate, with significantly reduced specific activities.
acetyl-CoA + oxalate = acetate + oxalyl-CoA.
succinyl-CoA--D-citramalate CoA-transferase
The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency.
(3R)-citramalate + succinyl-CoA = (3R)-citramalyl-CoA + succinate.
(R)-malate + succinyl-CoA = (R)-malyl-CoA + succinate.
The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli.
It has similar activity with both substrates.
(R)-carnitine + crotonobetainyl-CoA = (R)-carnitinyl-CoA + crotonobetaine.
(R)-carnitine + gamma-butyrobetainyl-CoA = (R)-carnitinyl-CoA + 4-(trimethylamino)butanoate.
The enzyme, purified from the bacterium Chloroflexus aurantiacus, can also accept itaconate as acceptor, with lower efficiency.
It is part of the 3-hydroxypropanoate cycle for carbon assimilation.
(S)-malate + succinyl-CoA = (S)-malyl-CoA + succinate.
(3S)-citramalate + succinyl-CoA = (3S)-citramalyl-CoA + succinate.
itaconate + succinyl-CoA = itaconyl-CoA + succinate.
The enzyme, isolated from the bacterium Acetobacterium woodii, catalyzes an energy-saving CoA loop for caffeate activation.
In addition to caffeate, the enzyme can utilize 4-coumarate or ferulate as CoA acceptor.
(E)-caffeate + hydrocaffeoyl-CoA = (E)-caffeoyl-CoA + 3-(3,4-dihydroxyphenyl)propanoate.
(R)-2-hydroxy-4-methylpentanoate CoA-transferase
The enzyme, characterized from the bacterium Peptoclostridium difficile, participates in an L-leucine fermentation pathway.
The reaction proceeds via formation of a covalent anhydride intermediate between a conserved aspartate residue and the acyl group of the CoA thioester substrate.
(R)-2-hydroxy-4-methylpentanoate + 4-methylpentanoyl-CoA = (R)-2-hydroxy-4-methylpentanoyl-CoA + 4-methylpentanoate.
The enzyme, characterized from the gut bacterium Clostridium scindens, catalyzes the last step in bile acid 7alpha-dehydroxylation, the removal of the CoA moiety from the products.
By using a transferase rather than hydrolase, the bacteria conserve the thioester bond energy, saving ATP molecules.
The enzyme has a broad substrate specificity and can use multiple acceptors, including allocholate, ursodeoxycholate, and beta-muricholate.
cholate + lithocholoyl-CoA = choloyl-CoA + lithocholate.
cholate + deoxycholoyl-CoA = choloyl-CoA + deoxycholate.
The enzyme participates in the methylaspartate cycle, an anaplerotic pathway that operates in some members of the haloarchaea and forms malate from acetyl-CoA.
mesaconate + succinyl-CoA = 2-methylfumaryl-CoA + succinate.
This enzyme catalyzes the final step in methanogenesis, the biological production of methane.
This important anaerobic process is carried out only by methanogenic archaea.
The enzyme can also function in reverse, for anaerobic oxidation of methane.
The enzyme requires the hydroporphinoid nickel complex coenzyme F430.
Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates.
The sulfide sulfur can be replaced by selenium but not by oxygen.
coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane.
The product arseno-mycothiol is reduced by EC 1.20.4.3 (mycoredoxin) to arsenite and mycothiol-mycoredoxin disulfide.
Finally, a second mycothiol recycles mycoredoxin and forms mycothione.
arsenate + mycothiol = arseno-mycothiol + H2O.
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase
2-methylthio-N-6-isopentenyl adenosine synthase
This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur.
The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.
The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover.
The identity of the electron donor is not known.
[sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine.
[ribosomal protein S12] (aspartate(89)-C(3))-methylthiotransferase
[ribosomal protein S12] (aspartate-C(3))-methylthiotransferase
This bacterial enzyme binds two [4Fe-4S] clusters.
A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters.
In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge.
In the second reaction the enzyme catalyzes the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate(89) (Escherichia coli numbering).
[sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine.
AH2 + L-aspartate(89)-[ribosomal protein uS12]-methanesulfate + S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + A + H(+) + L-methionine.
[sulfur carrier]-SH + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + S-adenosyl-L-methionine = [sulfur carrier]-H + H(+) + L-aspartate(89)-[ribosomal protein uS12]-methanesulfate + S-adenosyl-L-homocysteine.
tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase
methylthio-threonylcarbamoyl-adenosine transferase B
The enzyme, which is a member of the S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes superfamily, binds two [4Fe-4S] clusters as well as the transferred sulfur.
[sulfur carrier]-SH + AH2 + N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine.
S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent)
The enzyme, which has been characterized from the bacterium Mycobacterium tuberculosis, has no activity with O-acetyl-L-serine.
O-phospho-L-serine + thiosulfate = phosphate + S-sulfo-L-cysteine.
It catalyzes two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of an L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue.
2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein].
2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-sulfodisulfanyl)-L-cysteinyl-[SoxY protein].
cysteinyl-tRNA(Sec)-selenium transferase
cysteinyl-tRNA(Sel)-selenium transferase
Recognizes specifically tRNA(Sec)-species.
Binding of tRNA(Sec) also occurs in the absence of the seryl group.
2-Aminoacryloyl-tRNA, bound to the enzyme as an imine with the pyridoxal phosphate, is an intermediate in the reaction.
Since the selenium atom replaces oxygen in serine, the product may also be referred to as L-selenoseryl-tRNA(Sel).
The abbreviation Sel has also been used for selenocysteine but Sec is preferred.
H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate.
O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase
O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase
O-phosphoseryl-tRNA(Sec) selenium transferase
In archaea and eukarya selenocysteine formation is achieved by a two-step process: EC 2.7.1.164 phosphorylates the endogenous L-seryl-tRNA(Sec) to O-phospho-L-seryl-tRNA(Sec), and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNA(Sec) by Sep-tRNA:Sec-tRNA synthase.
H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + 2 phosphate.
This bacterial enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates.
The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA.
(2E)-geranyl diphosphate + 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + H2O + selenophosphate = (2E)-thiogeraniol + 5-methylaminomethyl-2-selenouridine(34) in tRNA + diphosphate + phosphate.
Transferring molybdenum- or tungsten-containing groups
Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors
Catalyzes the insertion of molybdenum into the ene-dithiol group of molybdopterin.
In eukaryotes this reaction is catalyzed by the N-terminal domain of a fusion protein whose C-terminal domain catalyzes EC 2.7.7.75.
adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin.
Wide specificity; also hydrolyzes vitamin A esters.
The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4 and EC 3.5.1.13.
a carboxylic ester + H2O = a carboxylate + an alcohol + H(+).
It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases.
The natural substrates of the paraoxonases are lactones, with (+-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate.
a phenyl acetate + H2O = a phenol + acetate + H(+).
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria.
It hydrolyzes triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids.
The enzyme is highly soluble in water and acts at the surface of oil droplets.
Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site.
The lid opens when the enzyme contacts an oil-water interface (interfacial activation).
The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+).
Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position.
a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).
1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).
a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine.
an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+).
acetylcholine + H2O = acetate + choline + H(+).
Acts on a variety of choline esters and a few other compounds.
an acylcholine + H2O = a carboxylate + choline + H(+).
Also acts on cocaine and other tropine esters.
atropine + H2O = H(+) + tropate + tropine.
[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol.
A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols.
a sterol ester + H2O = a fatty acid + a sterol + H(+).
a cholesterol ester + H2O = a fatty acid + cholesterol + H(+).
Chlorophyllase has been found in higher plants, diatoms, and in the green algae Chlorella.
Forms part of the chlorophyll degradation pathway and is thought to take part in de-greening processes such as fruit ripening, leaf senescence and flowering, as well as in the turnover and homeostasis of chlorophyll.
Acts preferentially on chlorophyll a but will also accept chlorophyll b and pheophytins as substrates.
Ethylene and methyl jasmonate, which are known to accelerate senescence in many species, can enhance the activity of the hormone-inducible form of this enzyme.
a chlorophyll + H2O = a chlorophyllide + H(+) + phytol.
chlorophyll a + H2O = chlorophyllide a + H(+) + phytol.
H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate.
Acts on a wide range of hexono-1,5-lactones.
D-glucono-1,5-lactone + H2O = D-gluconate + H(+).
D-glucurono-6,2-lactone + H2O = D-glucuronate + H(+).
Also hydrolyzes ester links in other tannins.
digallate + H2O = 2 3,4,5-trihydroxybenzoate + H(+).
(3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+).
Hydrolyzes glycerol monoesters of long-chain fatty acids.
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O = 3-oxoadipate + H(+).
Specific for 1,4-lactones with 4-8 carbon atoms.
Does not hydrolyze simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone.
a 1,4-lactone + H2O = a 4-hydroxyacid + H(+).
D-galactono-1,4-lactone + H2O = D-galactonate + H(+).
D-xylono-1,4-lactone 5-phosphate + H2O = 5-phospho-D-xylonate + H(+).
H2O + L-arabino-1,4-lactone 5-phosphate = 5-phospho-L-arabinonate + H(+).
Also acts on 2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids.
a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+).
4-pyridoxolactone + H2O = 4-pyridoxate + H(+).
Acts on higher fatty acid (C6 to C18) esters of L-carnitine.
Highest activity is with O-decanoyl-L-carnitine.
H2O + O-acyl-(R)-carnitine = (R)-carnitine + a fatty acid + H(+).
an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+).
D-arabinono-1,4-lactone + H2O = D-arabinonate + H(+).
6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+).
Has a much broader specificity than EC 3.1.1.4.
a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).
6-acetyl-D-glucose + H2O = acetate + D-glucose + H(+).
Hydrolyzes triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles (VLDL).
Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein.
The principal reaction sequence of that enzyme is triglyceride -> 1,2-diglyceride -> 2-monoglyceride.
The hepatic enzyme (LIPC) also hydrolyzes triglycerides and phospholipids present in circulating plasma lipoproteins.
Also hydrolyzes some other benzenoid 1,4-lactones.
3,4-dihydrocoumarin + H2O = 3-(2-hydroxyphenyl)propanoate + H(+).
H2O + testololactone = H(+) + testolate.
H2O + triacetate lactone = H(+) + triacetate.
actinomycin + H2O = actinomycinic monolactone.
Will only hydrolyze those substrates based on the 2,4-dihydroxy-6-methylbenzoate structure that also have a free hydroxyl ortho to the depside linkage.
H2O + o-orsellinate depside = H(+) + 2 orsellinate.
Hydrolyzes the acetyl ester bond on the 10-position of the antibiotic cephalosporin C.
cephalosporin C + H2O = acetate + deacetylcephalosporin C + H(+).
Also acts, more slowly, on isochlorogenate.
chlorogenate + H2O = (E)-caffeate + H(+) + L-quinate.
Also catalyzes alpha-aminoacyl transfer to a number of amine nucleophiles.
an alpha-amino acid ester + H2O = an alcohol + an alpha-amino acid + H(+).
H2O + oxaloacetate 4-methyl ester = H(+) + methanol + oxaloacetate.
2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-2-enedioate + H(+).
Opens the A-ring-lactone of the triterpenoid deoxylimonic acid, leaving the D-ring-lactone intact.
deoxylimonoate + H2O = deoxylimononate D-ring-lactone + H(+).
1-alkyl-2-acetylglycerophosphocholine esterase
2-acetyl-1-alkylglycerophosphocholine esterase
platelet-activating factor acetylhydrolase
a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+).
Hydrolyzes the three ornithine ester bonds in fusarinine C.
Also acts on N(5)-dinitrophenyl-L-ornithine methyl ester.
H2O + N(5)-acyl-L-ornithine ester = an alcohol + H(+) + N(5)-acyl-L-ornithine.
H2O + O-sinapoylcholine = (E)-sinapate + choline + H(+).
Also acts on long-chain acylglycerol, but not diacyl- or triacylglycerols.
a wax ester + H2O = a long chain fatty alcohol + a long-chain fatty acid + H(+).
Hydrolyzes the 12-ester bond in a variety of 12,13-diacylphorbols (phorbol is a diterpenoid).
This reaction inactivates tumor promoter 12-O-tetradecanoylphorbol-13-acetate from croton oil.
H2O + phorbol 12,13-dibutanoate = butanoate + H(+) + phorbol 13-butanoate.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) + a fatty acid + H(+).
Acts on free and glycosidically-bound N-acetyl- or N-glycoloylneuraminic acid.
Acts mainly on 4-O- and 9-O-acetyl groups.
Also acts on some other O-acetyl esters, both cyclic and acyclic compounds, which are not sialic acids.
H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate.
H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate.
5-(4-acetoxybut-1-ynyl)-2,2'-bithiophene + H2O = 5-(4-hydroxy-but-1-ynyl)-2,2'-bithiophene + acetate + H(+).
The activity of the liver cytosol enzyme is highest with acetyl esters of aryl alcohols, and thioesters are also hydrolyzed.
The microsomal enzyme also hydrolyzes some other negatively charged esters.
Best substrates were esters of salicylate with long-chain alcohols.
acetylsalicylate + H2O = acetate + H(+) + salicylate.
Acts on short-chain acyl esters of 4-methylumbelliferone, but not on naphthyl, indoxyl or thiocholine esters.
4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate + H(+).
2-pyrone-4,6-dicarboxylate lactonohydrolase
The product is most likely the keto-form of 4-oxalmesaconate (shown).
It can be converted to the enol-form, 4-hydroxybuta-1,3-diene-1,2,4-trioate, either spontaneously or by EC 5.3.2.8.
2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+).
N-acetyl-D-galactosaminoglycan + H2O = D-galactosaminoglycan + acetate.
methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase
Demethylates the insect juvenile hormones, JH1 and JH3, but does not hydrolyze the analogous ethyl or isopropyl esters.
H2O + juvenile hormone I = H(+) + juvenile hormone I carboxylate + methanol.
H2O + juvenile hormone III = H(+) + juvenile hormone III carboxylate + methanol.
H2O + juvenile hormone II = H(+) + juvenile hormone II carboxylate + methanol.
Also acts on 4-nitrophenyl esters, with optimum acyl chain length C6 to C8.
bis(2-ethylhexyl)phthalate + H2O = 2-ethylhexan-1-ol + 2-ethylhexyl phthalate + H(+).
methyl-accepting chemotaxis protein methyl-esterase
[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol.
11-cis-retinyl hexadecanoate + H2O = 11-cis-retinol + H(+) + hexadecanoate.
all-trans-retinylester 11-cis isomerohydrolase
This enzyme, which operates in the retinal pigment epithelium (RPE), catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol, a key step in the regeneration of the visual chromophore in the vertebrate visual cycle.
Interaction of the enzyme with the membrane is critical for its enzymatic activity.
an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid + H(+).
all-trans-retinyl hexadecanoate + H2O = 11-cis-retinol + H(+) + hexadecanoate.
H2O + L-rhamnono-1,4-lactone = H(+) + L-rhamnonate.
5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene deacetylase
A highly specific enzyme from Tagetes patula.
5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene + H2O = 5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2'-bithiophene + acetate + H(+).
In the reverse reaction, forms ethyl esters from fatty acids and ethanol in the absence of coenzyme A or ATP.
Best substrates are unsaturated octadecanoic acids; palmitate, stearate and arachidonate also act, more slowly.
a long-chain fatty acyl ethyl ester + H2O = a long-chain fatty acid + ethanol + H(+).
D-xylono-1,4-lactone + H2O = D-xylonate + H(+).
Acts on a number of benzyl esters of substituted phenyl propanoates, and on the benzyl esters of phenylalanine and tyrosine.
benzyl cetraxate + H2O = benzyl alcohol + cetraxate + H(+).
Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates.
Differs from EC 3.1.1.34 since 1,2-diacetyl-sn-glycerols are not substrates.
a 1-O-alkyl-2-acetyl-sn-glycerol + H2O = 1-O-alkyl-sn-glycerol + acetate + H(+).
catalyzes the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol.
Does not act on acetylated mannan or pectin.
Deacetylation of xylans and xylo-oligosaccharides.
Catalyzes the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in 'natural' substrates.
p-Nitrophenol acetate and methyl ferulate are poorer substrates.
All microbial ferulate esterases are secreted into the culture medium.
They are sometimes called hemicellulase accessory enzymes, since they help xylanases and pectinases to break down plant cell wall hemicellulose.
feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Cutin, a polymeric structural component of plant cuticles, is an hydroxy fatty acid polymer, usually C16 or C18 and that contains one to three hydroxyl groups.
The enzyme from several fungal sources also hydrolyzes the p-nitrophenyl esters of hexadecanoic acid.
It is however inactive toward several esters that are substrates for non-specific esterases.
poly[(R)-hydroxyalkanoic acid] depolymerase
Reaction also occurs with esters of other short-chain-length (C1-C5) hydroxyalkanoic acids (HA).
There are two types of polymers: native (intracellular) granules are amorphous and have an intact surface layer; denatured (extracellular) granules either have no surface layer or a damaged surface layer and are partially crystalline.
[(3R)-hydroxybutanoate](n) + H2O = (R)-3-hydroxybutanoate + [(3R)-hydroxybutanoate](n-1) + H(+).
[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate dimer + [(3R)-hydroxybutanoate](n-2) + H(+).
[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate trimer + [(3R)-hydroxybutanoate](n-3) + H(+).
[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate tetramer + [(3R)-hydroxybutanoate](n-4) + H(+).
[(3R)-hydroxybutanoate](n) + H2O = (3R)-hydroxybutanoate pentamer + [(3R)-hydroxybutanoate](n-5) + H(+).
The main product after prolonged incubation is the dimer.
Besides hydrolyzing polymers of 3-hydroxyoctanoic acid, the enzyme also hydrolyzes other polymers derived from medium-chain-length (C6-C12) hydroxyalkanoic acids and copolymers of mixtures of these.
It also hydrolyzes p-nitrophenyl esters of fatty acids.
Polymers of short-chain-length hydroxyalkanoic acids such as poly[(R)-3-hydroxybutanoic acid] and poly[(R)-3-hydroxypentanoic acid] are not hydrolyzed.
Hydrolyzes the polyester poly{oxycarbonyl[(R)-2-pentylethylene]} to oligomers.
The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms.
It consists of diglucosamine, beta-D-GlcN-(1->6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue.
Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3.
The enzyme from human leukocytes detoxifies the lipid by hydrolyzing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS).
It also possesses a wide range of phospholipase and acyltransferase activities (e.g. EC 3.1.1.4, EC 3.1.1.5, EC 3.1.1.32 and EC 3.1.1.52), hydrolyzing diacylglycerol and phosphatidyl compounds, but not triacylglycerols.
It has a preference for saturated C12-C16 acyl groups.
a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+).
Following hydrolysis of this indole alkaloid ester, the carboxylic acid decarboxylates spontaneously giving the sarpagan skeleton.
Also acts on akuammidine aldehyde (the 16-epimer of polyneuridine aldehyde).
H2O + polyneuridine aldehyde = 16-epivellosimine + CO2 + methanol.
Compared with other lipases, hormone-sensitive lipase has a uniquely broad substrate specificity.
It hydrolyzes all acylglycerols (triacylglycerol, diacylglycerol and monoacylglycerol) as well as cholesteryl esters, steroid fatty acid esters, retinyl esters and p-nitrophenyl esters.
It exhibits a preference for the 1- or 3-ester bond of its acylglycerol substrate compared with the 2-ester bond.
The enzyme shows little preference for the fatty acids in the triacylglycerol, although there is some increase in activity with decreasing chain length.
The enzyme activity is increased in response to hormones that elevate intracellular levels of cAMP.
a diacylglycerol + H2O = a fatty acid + a monoacylglycerol + H(+).
a monoacylglycerol + H2O = a fatty acid + glycerol + H(+).
Responsible for the last stages in the biosynthesis of the indole alkaloid ajmaline.
Highly specific for the substrates 17-O-acetylajmaline and 17-O-acetylnorajmaline as the structurally related acetylated alkaloids vinorine, vomilenine, 1,2-dihydrovomilenine and 1,2-dihydroraucaffricine cannot act as substrates.
17-O-acetylajmaline + H2O = acetate + ajmaline + H(+).
17-O-acetylnorajmaline + H2O = acetate + H(+) + norajmaline.
quorum-quenching N-acyl-homoserine lactonase
quorum-quenching N-acyl homoserine lactone hydrolase
Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signaling and the expression of virulence genes in quorum-sensing bacteria.
N-(3-oxohexanoyl)-L-homoserine lactone, N-(3-oxododecanoyl)-L-homoserine lactone, N-butanoyl-L-homoserine lactone and N-(3-oxooctanoyl)-L-homoserine lactone can act as substrates.
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+).
Forms part of the chlorophyll degradation pathway, and is found in higher plants and in algae.
In higher plants it participates in de-greening processes such as fruit ripening, leaf senescence, and flowering.
Exists in two forms: type 1 is induced by senescence whereas type 2 is constitutively expressed.
Highly specific for pheophorbide as substrate (with a preference for pheophorbide a over pheophorbide b) as other chlorophyll derivatives such as protochlorophyllide a, pheophytin a and c, chlorophyll a and b, and chlorophyllide a cannot act as substrates.
Another enzyme, called pheophorbide demethoxycarbonylase (PDC), produces pyropheophorbide a from pheophorbide a without forming an intermediate although the precise reaction is not yet known.
H(+) + H2O + pheophorbide a = CO2 + methanol + pyropheophorbide a.
Catalyzes the ring opening of epsilon-lactones which are formed during degradation of dihydrocarveol by the Gram-positive bacterium Rhodococcus erythropolis DCL14.
Also acts on ethyl caproate, indicating that it is an esterase with a preference for lactones (internal cyclic esters).
4-isopropenyl-7-methyloxepan-2-one + H2O = 6-hydroxy-3-isopropenylheptanoate + H(+).
7-isopropyl-4-methyloxepan-2-one + H2O = 6-hydroxy-3,7-dimethyloctanoate + H(+).
(4R,7R)-4-isopropenyl-7-methyloxepan-2-one + H2O = (3R,6R)-6-hydroxy-3-isopropenylheptanoate + H(+).
(4S,7R)-4-isopropenyl-7-methyloxepan-2-one + H2O = (3S,6R)-6-hydroxy-3-isopropenylheptanoate + H(+).
(4R,7S)-7-isopropyl-4-methyloxepan-2-one + H2O = (3R,6S)-6-hydroxy-3,7-dimethyloctanoate + H(+).
Rhodococcus sp. strain MB1 and Pseudomonas maltophilia strain MB11L can utilize cocaine as sole source of carbon and energy.
cocaine + H2O = benzoate + ecgonine methyl ester + H(+).
pimeloyl-[acyl-carrier protein] methyl ester esterase
Involved in biotin biosynthesis in Gram-negative bacteria.
The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains.
Even though the enzyme can interact with coenzyme A thioesters, the in vivo role of the enzyme is to hydrolyze the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalyzed by the fatty acid elongation enzymes.
6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol.
The degradation of rhamnogalacturonan by rhamnogalacturonases depends on the removal of the acetyl esters from the substrate.
Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I.
The enzyme is involved in degradation of fumonisin B1.
fumonisin B1 + 2 H2O = (2S,3S,5R,10R,12S,14S,15R,16R)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + 2 H(+) + 2 tricarballylate.
The enzyme is involved in degradation of pyrethroid pesticides.
The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyze cis-permethrin at approximately equal rate to trans-permethrin.
The enzyme from mouse hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin.
(-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol + H(+).
The methyl ester is formed by EC 2.1.1.233.
[phosphatase 2A protein]-C-terminal L-leucine methyl ester + H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) + methanol.
all-trans-retinyl ester 13-cis isomerohydrolase
all-trans-retinyl esters, which are a storage form of vitamin A, are generated by the activity of EC 2.3.1.135.
They can be hydrolyzed to 11-cis-retinol by EC 3.1.1.64, or to 13-cis-retinol by this enzyme.
an all-trans-retinyl ester + H2O = 13-cis-retinol + a fatty acid + H(+).
2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase
This enzyme, characterized from the soil bacterium Bradyrhizobium sp. JS329, is involved in the pathway of 5-nitroanthranilate degradation.
2-oxo-3-(5-oxofuran-2-ylidene)propanoate + H2O = 3-maleylpyruvate + H(+).
The enzyme was isolated from the bacteria Hydrogenophaga intermedia and Agrobacterium radiobacter S2.
It catalyzes a step in the degradation of 4-sulfocatechol.
4-sulfomuconolactone + H2O = 2 H(+) + maleylacetate + sulfite.
mycophenolic acid acyl-glucuronide esterase
mycophenolic acid acyl-glucuronide deglucuronidase
This liver enzyme deglucuronidates mycophenolic acid O-acyl-glucuronide, a metabolite of the immunosuppressant drug mycophenolate that is thought to be immunotoxic.
H2O + mycophenolic acid O-acyl-beta-D-glucuronide = D-glucuronate + H(+) + mycophenolate.
(2S,3S)-versiconal hemiacetal acetate + H2O = (2S-3S)-versiconal hemiacetal + acetate + H(+).
(3S)-versiconol acetate + H2O = (S)-versiconol + acetate + H(+).
The enzyme is involved in the modification of the aklavinone skeleton in the biosynthesis of anthracyclines in Streptomyces species.
aclacinomycin T + H2O = 15-demethylaclacinomycin T + methanol.
The enzyme, found in all domains of life, can cleave mischarged glycyl-tRNA(Ala).
The enzyme from Escherichia coli can cleave D-tyrosyl-tRNA(Tyr), D-aspartyl-tRNA(Asp) and D-tryptophanyl-tRNA(Trp).
Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc.
a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+).
glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala).
D-phenylalanyl-tRNA(Phe) + H2O = D-phenylalanine + H(+) + tRNA(Phe).
D-aspartyl-tRNA(Asp) + H2O = D-aspartate + H(+) + tRNA(Asp).
D-tryptophanyl-tRNA(Trp) + H2O = D-tryptophan + tRNA(Trp).
D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr).
The protein is only present in eukaryotes.
diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + H(+) + methanol.
[Wnt protein] O-palmitoleoyl-L-serine hydrolase
The enzyme removes the palmitoleate modification that is introduced to specific L-serine residues in Wnt proteins by EC 2.3.1.250.
[Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + H2O = (9Z)-hexadecenoate + [Wnt protein]-L-serine + H(+).
6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O = 6-deoxy-6-sulfo-D-gluconate + H(+).
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green filamentous bacteria (Chloroflexaceae), catalyzes the first committed step in the biosynthesis of bacteriochlorophylls c, d and e, the removal of the C-13(2)-methylcarboxyl group from chlorophyllide a.
The reaction is very similar to the conversion of pheophorbide a to pyropheophorbide a during chlorophyll a degradation, which is catalyzed by EC 3.1.1.82.
chlorophyllide a + H(+) + H2O = 8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d + CO2 + methanol.
The enzyme, isolated from the bacterium Ideonella sakaiensis, also produces small amounts of terephthalate (cf. EC 3.1.1.102).
The reaction takes place on PET-film placed in solution.
(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+).
The enzyme, isolated from the bacterium Ideonella sakaiensis, has no activity with poly(ethylene terephthalate) PET (cf. EC 3.1.1.101).
4-[(2-hydroxyethoxy)carbonyl]benzoate + H2O = ethylene glycol + H(+) + terephthalate.
The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface.
The activity greatly increases methicillin resistance in MRSA strains.
[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n D-alanine.
The enzyme, characterized from Mycoplasma spp., contains a binuclear metal center with two zinc cations.
The enzyme is specific for the phosphorylated forms, and is unable to hydrolyze non-phosphorylated 1,4-lactones.
3-O-acetylpapaveroxine + H2O = acetate + H(+) + narcotine hemiacetal.
The enzyme, characterized from the bacterium Escherichia coli and from human cells, removes the acetyl group from either the 2'' or 3'' position of O-acetyl-ADP-ribose, which are formed by the action of EC 2.3.1.286.
The human enzyme can also remove ADP-D-ribose from phosphorylated double stranded DNA adducts.
3''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+).
2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+).
This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains.
Unlike EC 3.1.1.108, which acts only on enterobactin, this enzyme can also act on the C-glucosylated forms known as salmochelins.
Unlike EC 3.1.1.109, (IroD), IroE prefers apo siderophores as substrates, and is assumed to act before the siderophores are exported out of the cell.
It hydrolyzes the trilactone only once, producing linearized trimers.
enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer.
H2O + triglucosyl-enterobactin = [N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]3 + H(+).
diglucosyl-enterobactin + H2O = H(+) + N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2.
H2O + monoglucosyl-enterobactin = [N-(2,3-dihydroxybenzoyl)-L-seryl]2-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine + H(+).
The enzyme, isolated from the bacterium Escherichia coli, allows the bacterium to grow in limited iron conditions.
It can also act on enterobactin (with no complexed iron) and the aluminum(III) analog of iron(III) enterobactin.
The trimer formed is further hydrolyzed to form the dimer and the monomer.
Fe(III)-enterobactin + H(+) + 3 H2O = Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] + 2 N-(2,3-dihydroxybenzoyl)-L-serine.
The enzyme acts on iron(III)-bound enterobactin and C-glucosylated derivatives known as salmochelins.
Unlike EC 3.1.1.107, (IroE), IroD prefers iron(III)-bound siderophores as substrates, and is assumed to act after the iron-siderophore complexes are imported into the cell.
It catalyzes several hydrolytic reactions, producing a mixture of iron(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] complex and salmochelin SX.
Fe(III)-di(C-5-deoxy-beta-D-glucosyl)-enterobactin + H2O = Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+).
Fe(III)-C-5-deoxy-beta-D-glucosyl-enterobactin + H2O = Fe(III)-{di[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + H(+).
Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+) + H2O = Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2 + N-(2,3-dihydroxybenzoyl)-L-serine.
Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+) + H2O = Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine.
Fe(III)-{di[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + H(+) + H2O = Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + N-(2,3-dihydroxybenzoyl)-L-serine.
Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2 + H(+) + H2O = Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine] + N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine.
The enzyme, found in bacteria, participates in the degradation of D-xylose.
D-xylono-1,5-lactone + H2O = D-xylonate + H(+).
phosphatidylserine-specific phospholipase A1
The enzyme, which has described from mammals, is specific for phosphatidylserine and 2-lysophosphatidylserine, and does not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid or phosphatidylinositol.
a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+).
a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = a fatty acid + H(+) + sn-glycero-3-phospho-L-serine.
The enzyme, characterized from the yeast Saccharomyces cerevisiae, hydrolyzes acetate esters.
It acts preferentially on 3-methylbutyl acetate, a major determinant of sake flavor.
3-methylbutyl acetate + H2O = 3-methylbutanol + acetate + H(+).
The enzyme, characterized from Pseudomonas strains, is involved in degradation of short chain alkyl methyl ketones.
ethyl acetate + H2O = acetate + ethanol + H(+).
The enzyme, characterized from the bacterium Gordonia sp. TY-5, participates in a propane utilization pathway.
H2O + methyl acetate = acetate + H(+) + methanol.
D-apionolactone + H2O = D-apionate + H(+).
The enzyme, present in animals, is specific for the sn-1 position.
When acting on 1-acyl-2-arachidonoyl-sn-glycerol, the enzyme forms 2-arachidonoylglycerol, the most abundant endocannabinoid in the mammalian brain.
a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid + H(+).
(4-O-methyl)-D-glucuronate--lignin esterase
The enzyme occurs in microorganisms and catalyzes the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers.
a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+).
phosphatidic acid-preferring phospholipase A1
The human enzyme shows broad specificity, and has a preference for phosphatidate over other phospholipids.
Unlike EC 3.1.1.32 it is also active against phosphatidylinositol.
It is not active toward acyl groups linked at the sn-2 position.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = a 2-acyl-sn-glycero-3-phospho-D-myo-inositol + a fatty acid + H(+).
a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid + H(+).
protein-S-isoprenylcysteine alpha-carbonyl methylesterase
[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + H2O = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + H(+) + methanol.
acetyl-CoA + H2O = acetate + CoA + H(+).
Also hydrolyzes CoA thioesters of other long-chain fatty acids.
H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate.
H2O + succinyl-CoA = CoA + H(+) + succinate.
3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-methylpropanoate + CoA + H(+).
(3S)-hydroxy-3-methylglutaryl-CoA + H2O = 3-hydroxy-3-methylglutarate + CoA + H(+).
Also hydrolyzes S-acetoacetylglutathione, more slowly.
an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+).
(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione + H(+).
H2O + S-acylglutathione = a carboxylate + glutathione + H(+).
formyl-CoA + H2O = CoA + formate + H(+).
acetoacetyl-CoA + H2O = acetoacetate + CoA + H(+).
Also hydrolyzes S-acetylglutathione, more slowly.
H2O + S-formylglutathione = formate + glutathione + H(+).
H2O + S-succinylglutathione = glutathione + H(+) + succinate.
Acts on [acyl-carrier-protein] thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.
(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP].
H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate.
H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP].
acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase
In the proteobacterium Rubrivivax gelatinosus, this enzyme modulates the activity of EC 4.1.3.6 by converting it from its active acetyl form into its inactive thiol form by removal of its acetyl groups.
The activity of citrate-lyase deacetylase is itself inhibited by L-glutamate.
acetyl-[citrate lyase ACP] + H2O = acetate + H(+) + holo-[citrate lyase ACP].
(S)-methylmalonyl-CoA + H2O = CoA + H(+) + methylmalonate.
ADP-dependent short-chain-acyl-CoA hydrolase
Maximum activity is shown with propanoyl-CoA.
a short-chain fatty acyl-CoA + H2O = a short-chain fatty acid + CoA + H(+).
ADP-dependent medium-chain-acyl-CoA hydrolase
Maximum activity is shown with nonanoyl-CoA.
a medium-chain fatty acyl-CoA + H2O = a medium chain fatty acid + CoA + H(+).
Broad specificity for medium- to long-chain acyl-CoA.
Insensitive to NAD(+) (cf. EC 3.1.2.19).
a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+).
dodecanoyl-[acyl-carrier-protein] hydrolase
dodecanoyl-acyl-carrier-protein hydrolase
dodecyl-[acyl-carrier protein] hydrolase
Acts on the acyl-carrier protein thioester of C12 and, with a much lower activity, C14 fatty acids.
The derivative of oleic acid is hydrolyzed very slowly.
dodecanoyl-[ACP] + H2O = dodecanoate + H(+) + holo-[ACP].
Specific for long-chain thioesters of fatty acids.
Hydrolyzes fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA.
H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein].
this enzyme is part of the bacterial 2,4-dichlorobenzoate degradation pathway.
4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA + H(+).
This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1.
H2O + phenylglyoxylyl-CoA = CoA + H(+) + phenylglyoxylate.
chenodeoxycholoyl-coenzyme A thioesterase
Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short- and medium- to long-chain acyl-CoA's, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoA's, all of which are present in peroxisomes.
The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome.
choloyl-CoA + H2O = cholate + CoA + H(+).
chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+).
This enzyme participates in the synthesis of menaquinones, phylloquinone, as well as several plant pigments.
The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates.
1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA + H(+).
It reacts with CoA to form fluoroacetyl-CoA, which substitutes for acetyl CoA and reacts with EC 2.3.3.1 to produce fluorocitrate, a metabolite of which binds very tightly to EC 4.2.1.3 and halts the TCA cycle.
This enzyme hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance on the organisms that produce it.
It has been described in the poisonous plant Dichapetalum cymosum and the bacterium Streptomyces cattleya, both of which are fluoroacetate producers.
fluoroacetyl-CoA + H2O = CoA + fluoroacetate + H(+).
The enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24) or other CoA esters.
(S)-malyl-CoA + H2O = (S)-malate + CoA + H(+).
dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase
Dihydromonacolin L acid is synthesized while bound to an acyl-carrier protein domain of EC 2.3.1.161.
Since that enzyme lacks a thioesterase domain, release of the dihydromonacolin L acid moiety from the polyketide synthase requires this dedicated enzyme.
dihydromonacolin L-[lovastatin nonaketide synthase] + H2O = dihydromonacolin L carboxylate + H(+) + holo-[lovastatin nonaketide synthase].
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the production of the signal molecule 2-heptyl-4(1H)-quinolone (HHQ).
(2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA + H(+).
Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1).
a phosphate monoester + H2O = an alcohol + phosphate.
H2O + O-phospho-L-serine = L-serine + phosphate.
H2O + O-phospho-D-serine = D-serine + phosphate.
This enzyme catalyzes the Mg(2+)-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol.
In lipid signaling, the enzyme generates a pool of DAG to be used for protein kinase C activation.
The mammalian enzymes are known as lipins.
a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
1-O-alkyl-2-acyl-sn-glycero-3-phosphate + H2O = 1-O-alkyl-2-acyl-sn-glycerol + phosphate.
a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate.
a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + phosphate.
3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase
3'-phosphoadenylylsulfate 3'-phosphatase
Also acts on 3'-phosphoadenylylsulfate, and on the corresponding 2'-phosphates.
adenosine 3',5'-bisphosphate + H2O = AMP + phosphate.
myo-inositol-hexakisphosphate 3-phosphohydrolase
1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.
Also catalyzes potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose, or 2-deoxy-D-glucose (cf. EC 2.7.1.62, EC 2.7.1.79 and EC 3.9.1.1).
D-glucose 6-phosphate + H2O = D-glucose + phosphate.
alpha-D-glucose 6-phosphate + H2O = alpha-D-glucose + phosphate.
Also acts, more slowly, on alpha-D-galactose 1-phosphate.
alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate.
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate.
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate.
(2R)-S-methyl-3-phospho-1-thioglycerate + H2O = (2R)-S-methyl-1-thioglycerate + phosphate.
H2O + L-histidinol phosphate = L-histidinol + phosphate.
serine/threonine specific protein phosphatase
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate.
H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate.
[phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate.
2-phosphoglycolate + H2O = glycolate + phosphate.
glycerol 2-phosphate + H2O = glycerol + phosphate.
(2R)-2-phosphoglycerate + H2O = (R)-glycerate + phosphate.
The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate.
The enzyme from Saccharomyces cerevisiae also acts on propane-1,2-diol 1-phosphate, but not on a variety of other phosphate esters.
H2O + sn-glycerol 1-phosphate = glycerol + phosphate.
H2O + sn-glycerol 3-phosphate = glycerol + phosphate.
D-mannitol 1-phosphate + H2O = D-mannitol + phosphate.
Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate.
sugar phosphate + H2O = sugar + phosphate.
This is the final step in the sucrose-biosynthesis pathway.
Highly specific for sucrose 6-phosphate, with fructose 6-phosphate unable to act as a substrate.
H2O + sucrose 6(F)-phosphate = phosphate + sucrose.
myo-inositol-1(or 4)-phosphate phosphohydrolase
Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group.
It also acts on adenosine 2'-phosphate (but not the 3'- or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols.
a myo-inositol phosphate + H2O = myo-inositol + phosphate.
1D-myo-inositol 3-phosphate + H2O = myo-inositol + phosphate.
1D-myo-inositol 1-phosphate + H2O = myo-inositol + phosphate.
1D-myo-inositol 2-phosphate + H2O = myo-inositol + phosphate.
1D-myo-inositol 4-phosphate + H2O = myo-inositol + phosphate.
1D-myo-inositol 5-phosphate + H2O = myo-inositol + phosphate.
1D-myo-inositol 6-phosphate + H2O = myo-inositol + phosphate.
6-phytase (name based on 1L-numbering system and not 1D-numbering)
1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate.
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate.
3-ADP-2-phosphoglycerate + H2O = 3-ADP-glycerate + phosphate.
an N-acylneuraminate 9-phosphate + H2O = an N-acylneuraminate + phosphate.
Also hydrolyzes nucleoside 2'-, 3'- and 5'-monophosphates, but only 2'- and 3'-phosphopolynucleotides.
a 3'end (2'-deoxyribonucleotide 3'-phosphate)-DNA + H2O = a 3'-end 2'-deoxyribonucleotide-DNA + phosphate.
Does not act on nucleoside monophosphates.
Induced in Escherichia coli by T-even phages.
a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate.
a 5'-end triphospho-adenosine in mRNA + H2O = a 5'-end diphospho-adenosine in mRNA + H(+) + phosphate.
a 5'-end triphospho-guanosine in mRNA + H2O = a 5'-end diphospho-guanosine in mRNA + H(+) + phosphate.
Also catalyzes the selective removal of 3'-phosphate groups from DNA and oligodeoxyribonucleotides.
a 2'-deoxyribonucleoside 3'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate.
Acts on 5-methyl-dCMP and on TMP, but more slowly than on dTMP.
inositol 1,4,5-triphosphate 5-phosphomonoesterase
inositol triphosphate 5-phosphomonoesterase
phosphatidylinositol 4,5-bisphosphate phosphatase
phosphatidyl-inositol-bisphosphate phosphatase
phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase
type II inositol-1,4,5-trisphosphate 5-phosphatase
type II inositol polyphosphate 5-phosphatase
These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3 and/or Ins(1,3,4,5)P4.
They are a diverse family of enzymes, with differing abilities to catalyze two or more of the four reactions listed.
They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo.
All of them can use either or both of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main property that distinguishes them from EC 3.1.3.56.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate.
D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-phosphate + phosphate.
Wide specificity, but 3-phosphoglycerate is the best substrate.
(2R)-3-phosphoglycerate + H2O = (R)-glycerate + phosphate.
Also acts on dihydrostreptomycin 3'alpha,6-bisphosphate and streptidine 6-phosphate.
H2O + streptomycin 6-phosphate = phosphate + streptomycin.
1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + H2O = 1-guanidino-1-deoxy-scyllo-inositol + phosphate.
A number of other substances, including phenyl phosphate, 4-nitrophenyl sulfate, acetyl phosphate and glycerol phosphate, are not substrates.
4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) + phosphate.
[glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate.
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
A mitochondrial enzyme associated with EC 1.2.4.1 in the pyruvate dehydrogenase complex.
H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + phosphate.
Simultaneously dephosphorylates and activates EC 6.4.1.2.
Acts similarly on EC 1.1.1.88, EC 2.4.1.1 and EC 2.4.1.11, and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate.
Not identical with EC 3.1.3.17 or EC 3.1.3.43.
[acetyl-CoA carboxylase] phosphate + H2O = [acetyl-CoA carboxylase] + phosphate.
3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate.
The enzyme copurifies with EC 2.7.1.105 (cf. EC 3.1.3.54).
beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate.
[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase
Acts on the product of the reaction catalyzed by EC 2.7.11.31, simultaneously dephosphorylating and activating EC 1.1.1.34.
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O = [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate.
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.
H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate.
Simultaneously dephosphorylates and activates EC 2.7.1.40 which has been inactivated by protein kinase.
[pyruvate kinase] phosphate + H2O = [pyruvate kinase] + phosphate.
Acts, very slowly, on hexose 6-phosphates.
D-sorbitol 6-phosphate + H2O = D-sorbitol + phosphate.
a dolichyl phosphate + H2O = di-trans,poly-cis-dolichol + phosphate.
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase
branched-chain oxo-acid dehydrogenase phosphatase
A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex.
Simultaneously dephosphorylates and activates EC 1.2.4.4 which has been inactivated by phosphorylation.
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] phosphate + H2O = [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] + phosphate.
The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.31, but not myosin; the catalytic subunit acts on all three substrates.
H2O + O-phospho-L-seryl-[myosin light chain] = L-seryl-[myosin light chain] + phosphate.
H2O + O-phospho-L-threonyl-[myosin light chain] = L-threonyl-[myosin light chain] + phosphate.
beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 2-phosphate + phosphate.
Dephosphorylation activates the calmodulin- and actin-binding ability of caldesmon.
[caldesmon] phosphate + H2O = [caldesmon] + phosphate.
D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase
D-myo-inositol 1,4,5-triphosphate 5-phosphatase
D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase
inositol-1,4,5-trisphosphate 5-phosphatase
inositol 1,4,5-trisphosphate phosphatase
inositol phosphate 5-phosphomonoesterase
inositol trisphosphate phosphomonoesterase
L-myo-inositol 1,4,5-trisphosphate-monoesterase
myo-inositol-1,4,5-trisphosphate 5-phosphatase
type I inositol-polyphosphate phosphatase
This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36 by its inability to dephosphorylate inositol lipids.
1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphate.
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
Acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar Vmax for both substrates, but with a 5 times higher affinity for the bisphosphate.
Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.
1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.
Acts on sugars and polyols phosphorylated on the terminal carbon, with a preference for sugars with a D-erythro-configuration, e.g. good substrates are glucose 6-phosphate, mannose 6-phosphate, 6-phosphogluconate, erythrose 4-phosphate and xylitol 5-phosphate.
1-O-alkyl-2-acetyl-sn-glycerol 3-phosphate + H2O = a 1-O-alkyl-2-acetyl-sn-glycerol + phosphate.
Also acts, more slowly, on a wide range of other monophosphates.
H2O + phosphoenolpyruvate = phosphate + pyruvate.
multiple inositol-polyphosphate phosphatase
inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
inositol-1,3,4,5-tetrakisphosphate 3-phosphatase
inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase
inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase
inositol tetrakisphosphate phosphomonoesterase
Also acts on Ins(1,3,4,5)P4 to yield Ins(1,4,5)P3.
myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate.
2-carboxy-D-arabinitol 1-phosphate + H2O = 2-carboxy-D-arabinitol + phosphate.
D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase
phosphatidyl-3-phosphate 3-phosphohydrolase
This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3)P2 to Ins-1-P.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate.
phosphatidylinositol-3,4-bisphosphate 4-phosphatase
D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase
inositol polyphosphate 4-phosphatase type II
This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4)P3 to Ins(1,3)P2.
It also converts Ins(3,4)P2 into Ins-3-P.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate.
phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase
Does not dephosphorylate inositol 4,5-bisphosphate.
This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4,5)P4 to Ins(1,4,5)P3.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate.
Also active toward fructose 1-phosphate.
2-deoxy-D-glucose 6-phosphate + H2O = 2-deoxy-D-glucose + phosphate.
Acts with EC 2.4.1.213 to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.
2-O-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + H2O = 2-O-(alpha-D-glucopyranosyl)glycerol + phosphate.
The enzyme from Pyrococcus horikoshii is specific for alpha-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = (2R)-2-O-(alpha-D-mannosyl)-glycerate + phosphate.
(2R)-phosphosulfolactate phosphohydrolase
The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyzes a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate.
This enzyme can also hydrolyze phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations.
(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate.
The enzyme attacks the product of the above reaction more slowly to yield Ins(1,2,3)P3.
1D-myo-inositol hexakisphosphate + H2O = 1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate.
adenosylcobalamin/alpha-ribazole phosphatase
This enzyme catalyzes the last step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, characterized in Salmonella enterica.
It also participates in a salvage pathway that recycles cobinamide into adenosylcobalamin.
adenosylcob(III)alamin 5'-phosphate + H2O = adenosylcob(III)alamin + phosphate.
alpha-ribazole 5'-phosphate + H2O = alpha-ribazole + phosphate.
Specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate.
This reaction can also be carried out by EC 3.1.3.1 and EC 3.1.3.2, but these enzymes have very broad substrate specificities.
H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal.
phosphate + pyridoxamine = H2O + pyridoxamine 5'-phosphate.
H2O + pyridoxine 5'-phosphate = phosphate + pyridoxine.
phosphoethanolamine/phosphocholine phosphatase
The enzyme is highly specific for phosphoethanolamine and phosphocholine.
H2O + phosphoethanolamine = ethanolamine + phosphate.
H2O + phosphocholine = choline + phosphate.
The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10.
The best substrates for this enzyme are 10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form.
The phosphatase activity is not found in plant EC 3.3.2.10 or in mammalian EC 3.3.2.9.
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one.
The acireductone represents a branch point in the methione salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54.
5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate.
phosphatidylinositol-4,5-bisphosphate 4-phosphatase
Two pathways exist in mammalian cells to degrade 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [PtdIns(4,5)P2].
One is catalyzed by this enzyme and the other by EC 3.1.3.36, where the product is PtdIns4P.
The enzyme from human is specific for PtdIns(4,5)P2 as substrate, as it cannot use PtdIns(3,4,5)P3, PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns5P, PtdIns4P or PtdIns3P.
In humans, the enzyme is localized to late endosomal/lysosomal membranes.
It can control nuclear levels of PtdIns5P and thereby control p53-dependent apoptosis.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate.
mannosylfructose-6-phosphate phosphatase
Mannosylfructose is the major endogenous osmolyte produced by several alpha-proteobacteria in response to osmotic stress and is synthesized by the sequential action of EC 2.4.1.246 followed by this enzyme.
While mannosylfructose 6-phosphate is the physiological substrate, the enzyme can use sucrose 6-phosphate very efficiently.
The F in mannosylfructose 6(F)-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
beta-D-fructofuranosyl alpha-D-mannopyranoside 6(F)-phosphate + H2O = beta-D-fructofuranosyl alpha-D-mannopyranoside + phosphate.
This reaction is a shortcut in the Rapoport-Luebering shunt.
It bypasses the reactions of EC 5.4.2.11/EC 5.4.2.12 and directly forms 2-phospho-Dglycerate by removing the 3-phospho-group of 2,3-diphospho-Dglycerate.
The MIPP1 protein also catalyzes the reaction of EC 3.1.3.62.
(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate.
The bifunctional enzyme catalyzes the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. EC 3.1.3.4).
It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signaling role in stress response.
The phosphatase activity of the bifunctional enzyme is Mg(2+)-independent and N-ethylmaleimide-insensitive and is distinct from the Mg(2+)-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4.
The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase.
a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate.
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase
In vitro the catalytic efficiency with the beta-anomer is 100-200-fold higher than with the alpha-anomer.
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate.
D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
The in vitro catalytic efficiency of the enzyme from Bacteroides thetaiotaomicron is 6-fold higher with the alpha-anomer than with the beta-anomer.
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate.
The enzyme is highly specific for ADP-D-ribose 1''-phosphate.
Involved together with EC 3.1.4.37 in the breakdown of adenosine diphosphate ribose 1'',2''-cyclic phosphate (Appr>p), a by-product of tRNA splicing.
ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose + phosphate.
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 catalyzes the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase.
In vivo the enzyme catalyzes the dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency.
Divalent metal ions (Mg(2+), Mn(2+) or Co(2+)) stimulate activity.
(2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H2O = (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate.
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
This enzyme hydrolyzes phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways.
The enzyme also shows activity toward PtdIns(1,3,4,5)P4.
The enzyme is involved in several signal transduction pathways in the immune system leading to an adverse range of effects.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate.
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
The enzyme participates in the methionine salvage pathway in Bacillus subtilis.
In some species a single bifunctional enzyme, EC 3.1.3.77, catalyzes both this reaction and that of EC 5.3.2.5.
2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate.
5''-phosphoribostamycin + H2O = phosphate + ribostamycin.
The enzyme, characterized from the bacterium Escherichia coli, shows strict specificity toward deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates.
a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate.
The enzyme from the bacterium Enterococcus faecalis also has activity with the sucrose isomer turanose 6'-phosphate (alpha-D-glucopyranosyl-(1->3)-D-fructose 6-phosphate).
alpha-maltose 6'-phosphate + H2O = D-maltose + phosphate.
The enzyme also has low activity with N(7)-methyl-GDP, producing N(7)-methyl-GMP.
Does not accept AMP or GMP, and has low activity with UMP.
H2O + N(7)-methyl-GMP = N(7)-methylguanosine + phosphate.
D-kanosamine 6-phosphate + H2O = kanosamine + phosphate.
The enzyme from plants also has the activity of EC 3.1.3.25.
The enzymes have very low activity with D-galactose 1-phosphate (cf. EC 3.1.3.94).
beta-L-galactose 1-phosphate + H2O = L-galactose + phosphate.
The human enzyme also has the activity of EC 3.1.3.25.
The enzyme has very low activity with L-galactose 1-phosphate (cf. EC 3.1.3.93).
alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate.
phosphatidylinositol-3,5-bisphosphate 3-phosphatase
The enzyme is found in both plants and animals.
It also has the activity of EC 3.1.3.64.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate.
The enzyme, isolated from animals, dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation.
H2O + psi-UMP = phosphate + pseudouridine.
3',5'-nucleoside bisphosphate phosphatase
The enzyme, characterized from the bacterium Chromobacterium violaceum, has similar catalytic efficiencies with all the bases.
The enzyme has similar activity with ribonucleoside and 2'-deoxyribonucleoside 3',5'-bisphosphates, but shows no activity with nucleoside 2',5'-bisphosphates (cf. EC 3.1.3.7).
a ribonucleoside 3',5'-bisphosphate + H2O = a ribonucleoside 5'-phosphate + phosphate.
The enzyme, isolated from the yeast Saccharomyces cerevisiae, is highly specific for inosine 5'-phosphate, and has no detectable activity with other purine and pyrimidine nucleotides.
The enzyme participates in the thiamine biosynthesis pathway in eukaryotes and a few prokaryotes.
These organisms lack EC 2.7.4.16 and need to convert thiamine phosphate to thiamine diphosphate, the active form of the vitamin, by first removing the phosphate group, followed by diphosphorylation by EC 2.7.6.2.
H2O + thiamine phosphate = phosphate + thiamine.
validoxylamine A 7'-phosphate phosphatase
H2O + validoxylamine A 7'-phosphate = phosphate + validoxylamine A.
The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily.
Most of the isoforms have a wide substrate specificity, but isoforms specific for FMN also exist.
3-deoxy-D-glycero-D-galacto-nonulopyranosonate 9-phosphatase
2-keto-3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate-9-phosphate phosphatase
The enzyme, characterized from the bacterium Bacteroides thetaiotaomicron, is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate (Kdn).
3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate 9-phosphate + H2O = 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + phosphate.
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase
The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis.
Most forms of the enzyme has a broad substrate specificity.
5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-(D-ribitylamino)uracil + phosphate.
N-acetyl-D-muramate 6-phosphate phosphatase
H2O + N-acetyl-D-muramate 6-phosphate = N-acetyl-D-muramate + phosphate.
The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae.
The enzyme from yeast, but not from the plants, requires Mg(2+).
a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate.
This bacterial enzyme activates the antibiotic amicoumacin A by removing a phosphate group that is added by EC 2.7.1.230.
amicoumacin A 2-phosphate + H2O = amicoumacin A + phosphate.
The mammalian mitochondrial enzyme is a rhythmically expressed protein that regulates metabolism under the control of circadian clock.
It has a slight preference for NADPH over NADP(+).
The archaeal enzyme, identified in Methanocaldococcus jannaschii, is bifunctional acting as NAD kinase (EC 2.7.1.23) and NADP phosphatase with a slight preference for NADP(+) over NADPH.
5' nucleotide phosphodiesterase/alkaline phosphodiesterase I
nucleotide pyrophosphatase/phosphodiesterase I
orthophosphoric diester phosphohydrolase
Hydrolyzes both ribonucleotides and deoxyribonucleotides.
Has low activity toward polynucleotides.
A 3'-phosphate terminus on the substrate inhibits hydrolysis.
Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
Also acts on sn-glycero-3-phosphoethanolamine.
H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-glycerol 3-phosphate.
Clostridium oedematiens beta- and gamma-toxins
The bacterial enzyme also acts on sphingomyelin and phosphatidylinositol.
The enzyme from seminal plasma does not act on phosphatidylinositol.
a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine.
a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+).
a 1-acyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphate + choline + H(+).
1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphate + ethanolamine + H(+).
1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
monophosphatidylinositol phosphodiesterase
These enzymes form some of the cyclic phosphate Ins(cyclic 1,2)P(4,5)P2 as well as Ins(1,4,5)P3.
They show activity toward phosphatidylinositol, i.e., the activity of EC 4.6.1.13 in vitro at high calcium concentration.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+).
Has very little activity on phosphatidylcholine.
a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine.
serine-ethanolaminephosphate phosphodiesterase
Acts only on those phosphodiesters that have ethanolamine as a component part of the molecule.
H2O + L-serine-phosphoethanolamine = H(+) + L-serine + phosphoethanolamine.
[acyl-carrier-protein] phosphodiesterase
[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase
The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier-protein (ACP) and short-chain ACPs over the medium- and long-chain species.
Deletion of the gene encoding this enzyme abolishes ACP prosthetic-group turnover in vivo.
Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7.
H2O + holo-[ACP] = (R)-4'-phosphopantetheine + apo-[ACP] + H(+).
2',3'-cyclic-nucleotide 2'-phosphodiesterase
Also hydrolyzes 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides.
Similar reactions are carried out by EC 4.6.1.18 and EC 4.6.1.24.
a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-phosphate + H(+).
2',3'-cyclophospho-GMP + H2O = 3'-GMP + H(+).
2',3'-cyclophospho-UMP + H2O = 3'-UMP + H(+).
2',3'-cyclophospho-CMP + H2O = 3'-CMP + H(+).
2',3'-cyclophospho-AMP + H2O = 3'-AMP + H(+).
3',5'-cyclic-nucleotide phosphodiesterase
Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP.
a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+).
2',3'-cyclic-nucleotide 3'-phosphodiesterase
The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives.
An enzyme from liver acts on 2',3'-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyzes the corresponding 3',5'-cyclic phosphates, more slowly.
This latter enzyme has been called cyclic-CMP phosphodiesterase.
a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+).
2',3'-cyclophospho-AMP + H2O = adenosine 2'-phosphate + H(+).
2',3'-cyclophospho-GMP + H2O = guanosine 2'-monophosphate + H(+).
2',3'-cyclophospho-CMP + H2O = cytidine 2'-phosphate + H(+).
2',3'-cyclophospho-UMP + H2O = H(+) + uridine 2'-phosphate.
glycerophosphocholine cholinephosphodiesterase
No activity on sn-3-glycerophosphoethanolamine.
H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine.
alkylglycerophosphoethanolamine phosphodiesterase
1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-sn-glycero-3-phosphate + ethanolamine + H(+).
1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-O-(1Z-alkenyl)-sn-glycero-3-phosphate + ethanolamine + H(+).
a CMP-N-acyl-beta-neuraminate + H2O = an N-acylneuraminate + CMP + H(+).
Does not act on phosphatidylcholine, but hydrolyzes 2-lysophosphatidylcholine to choline and 2-lysophosphatidate.
a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+).
glycerol-1,2-cyclic-phosphate 2-phosphodiesterase
Acts on both stereoisomers of the substrate and also, more slowly, on 3',5'-cyclic AMP and on 2',3'-cyclic AMP.
glycerol 1,2-cyclic phosphate + H2O = glycerol 1-phosphate + H(+).
glycerophosphoinositol inositolphosphodiesterase
1,2-cyclic-inositol-phosphate phosphodiesterase
1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase
D-inositol 1,2-cyclic phosphate 2-phosphohydrolase
D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase
D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase
inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase
This enzyme also hydrolyzes Ins(cyclic 1,2)P to Ins-1-P.
H2O + sn-glycero-3-phospho-1D-myo-inositol = 1D-myo-inositol 1-phosphate + glycerol + H(+).
glycerophosphoinositol glycerophosphodiesterase
sn-glycero(3)phosphoinositol glycerophosphohydrolase
sn-glycero-3-phospho-1-inositol glycerophosphohydrolase
H2O + sn-glycero-3-phospho-1D-myo-inositol = H(+) + myo-inositol + sn-glycerol 3-phosphate.
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
alpha-N-acetylglucosaminyl phosphodiesterase
Acts on a variety of compounds in which N-acetyl-D-glucosamine is alpha-linked to a phosphate group, including the biosynthetic in intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the product of EC 2.7.8.17.
H2O + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] = H(+) + N(4)-[6-phospho-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + N-acetyl-D-glucosamine.
glycerophosphoryl diester phosphodiesterase
Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolyzed.
a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate.
H2O + sn-glycero-3-phospho-(1'-rac-glycerol) = glycerol + H(+) + sn-glycerol 3-phosphate.
H2O + sn-glycero-3-phospho-L-serine = H(+) + L-serine + sn-glycerol 3-phosphate.
dolichylphosphate-glucose phosphodiesterase
a dolichyl beta-D-glucosyl phosphate + H2O = a dolichyl phosphate + D-glucose + H(+).
dolichylphosphate-mannose phosphodiesterase
mannosylphosphodolichol phosphodiesterase
a dolichyl beta-D-mannosyl phosphate + H2O = a dolichyl phosphate + D-mannose + H(+).
glycosylphosphatidylinositol phospholipase D
phosphatidylinositol-glycan-specific phospholipase D
phosphatidylinositol-specific phospholipase D
This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure.
It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas EC 4.6.1.14 does so by elimination.
It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes.
an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+).
glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase
alpha-glucose-1-phosphate phosphodiesterase
This enzyme is specific for the product of EC 2.7.8.19.
6-(alpha-D-glucose-1-phospho)-alpha-D-mannosyl derivative + H2O = alpha-D-glucose 1-phosphate + alpha-D-mannose derivative + H(+).
cyclic-guanylate-specific phosphodiesterase
Linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65 and an allosteric activator of EC 2.4.1.12 rendering it inactive.
It is the balance between these two enzymes that determines the cellular level of cyclic di-3',5'-guanylate.
3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+).
Specific for 3',5'-cAMP and does not hydrolyze other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17 and EC 3.1.4.35).
It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation.
N-acetylphosphatidylethanolamine-hydrolyzing phospholipase D
N-acyl phosphatidylethanolamine phospholipase D
This enzyme is involved in the biosynthesis of anandamide.
It does not hydrolyze phosphatidylcholine and phosphatidylethanolamine.
H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate + an N-acylethanolamine + H(+).
phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
Isolated from the bacterium Escherichia coli, where it participates in the degradation of methylphosphonate.
alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H2O = alpha-D-ribose 1,5-bisphosphate + H(+).
7,8-dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase
Hydrolyzes 7,8-dihydroneopterin 2',3'-cyclic phosphate, a step in tetrahydromethanopterin biosynthesis.
In vitro the enzyme forms 7,8-dihydroneopterin 2'-phosphate and 7,8-dihydroneopterin 3'-phosphate at a ratio of 4:1.
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + H(+).
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-dihydroneopterin 2'-phosphate + H(+).
phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase
The enzyme, characterized from the bacterium Eggerthella lenta, is involed in degradation of methylphosphonate.
alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H2O = D-ribose 2,5-bisphosphate + H(+).
D-ribose 2,5-bisphosphate + H2O = D-ribose 5-phosphate + phosphate.
The enzyme hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
In vitro the enzyme can also ligate tRNA molecules with 2',3'-cyclic phosphate to tRNA with 5'-hydroxyl termini, forming a 2'-5' phosphodiester linkage.
However, the ligase activity is unlikely to be relevant in vivo.
a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+).
The enzyme, described from Gram-positive bacteria, degrades the second messenger cyclic di-3',5'-adenylate.
It is a membrane-bound protein that contains a cytoplasmic facing Per-Arnt-Sim (PAS) domain, a modified GGDEF domain, and a DHH/DHHA1 domain, which confers the phosphodiesterase activity.
Activity requires Mn(2+) and is inhibited by pApA.
3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+).
The enzyme, characterized from the Gram-positive bacterium Staphylococcus aureus, is a cytoplasmic protein that contains a DHH/DHHA1 domain.
It can act on cyclic di-3',5'-adenylate with a much lower activity (cf. EC 3.1.4.59).
Activity requires Mn(2+) and is inhibited by ppGpp.
5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O = 2 AMP + H(+).
The enzyme degrades cyclic 2,3-bisphosphoglycerate, a thermoprotectant that is produced by certain archaeal genera.
Two different enzymes that catalyze this activity, one soluble and one membrane-bound, have been characterized from the archaeon Methanothermobacter thermautotrophicus.
cyclic (2R)-2,3-bisphosphoglycerate + H2O = (2R)-2,3-bisphosphoglycerate + 2 H(+).
Deoxyguanosinetriphosphate triphosphohydrolase
dGTP + H2O = 2'-deoxyguanosine + H(+) + triphosphate.
Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities.
The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate.
This residue is generated by post-translational modification of a conserved cysteine or serine residue by EC 1.8.3.7, EC 1.1.98.7, or EC 1.8.98.7.
an aryl sulfate + H2O = a phenol + H(+) + sulfate.
Also acts on some related steryl sulfates.
dehydroepiandrosterone 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + H(+) + sulfate.
Also acts on other sulfates of mono- and disaccharides and on adenosine 5'-sulfate.
D-glucose 6-sulfate + H2O = D-glucose + H(+) + sulfate.
Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate.
choline sulfate + H2O = choline + H(+) + sulfate.
Hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin.
Hydrolyzes galactose-3-sulfate residues in a number of lipids.
Also hydrolyzes ascorbate 2-sulfate and many phenol sulfates.
H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate.
Also acts on the saturated analog but not on higher oligosaccharides, nor any 6-sulfates.
4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine 4-sulfate + H2O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine + H(+) + sulfate.
Also acts on the saturated analog and N-acetyl-D-galactosamine 4,6-disulfate, but not higher oligosaccharides, nor any 4-sulfate.
4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine 6-sulfate + H2O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine + H(+) + sulfate.
H2O + N(2),6-disulfo-D-glucosamine = H(+) + N-sulfo-D-glucosamine + sulfate.
Also acts on N-acetylglucosamine 4-sulfate.
Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.
Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.
Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
The enzyme from Flavobacterium heparinum also hydrolyzes N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue.
Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin.
Highly specific; does not act on monoethyl sulfate, monoisopropyl sulfate or monododecyl sulfate.
H2O + monomethyl sulfate = H(+) + methanol + sulfate.
(R)-2-O-sulfolactate + H2O = (R)-lactate + H(+) + sulfate.
Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13).
Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate.
(R)-specific secondary-alkylsulfatase (type III)
This enzyme belongs to the type III sulfatase family.
The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates.
The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties.
Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity.
an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate.
S-sulfosulfanyl-L-cysteine sulfohydrolase
It catalyzes two reactions in the pathway.
In both cases the enzyme hydrolyzes a sulfonate moiety that is bound (either directly or via a sulfane) to a cysteine residue of a SoxY protein, releasing sulfate.
The enzyme from Paracoccus pantotrophus contains a pyroglutamate (cycloglutamate) at its N-terminus.
H2O + S-sulfosulfanyl-L-cysteinyl-[SoxY protein] = H(+) + S-sulfanyl-L-cysteinyl-[SoxY protein] + sulfate.
H2O + S-(2-sulfodisulfanyl)-L-cysteinyl-[SoxY protein] = H(+) + S-disulfanyl-L-cysteinyl-[SoxY protein] + sulfate.
The enzyme is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate.
The enzyme from Pseudomonas aeruginosa is secreted out of the cell.
The catalytic mechanism begins with activation of a water molecule by the binuclear Zn(2+) cluster, resulting in a nucleophilic attack on the carbon atom.
a primary linear alkyl sulfate ester + H2O = a primary alcohol + H(+) + sulfate.
type III branched primary-alkylsulfatase
This enzyme belongs to the type III family.
The enzyme, characterized from a Pseudomonas strain, is specific for branched primary-alkyl sulfate esters and does not act on linear substrates such as dodecyl sulfate.
2-butyloctyl sulfate + H2O = 2-butyloctan-1-ol + H(+) + sulfate.
Farnesyl diphosphate is the best substrate so far tested.
dimethylallyl diphosphate + H2O = diphosphate + prenol.
guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase
Penta-phosphate guanosine-3'-diphosphohydrolase
Penta-phosphate guanosine-3'-pyrophosphohydrolase
guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP + H(+).
guanosine 3'-diphosphate 5'-triphosphate + H2O = diphosphate + GTP + H(+).
A group of enzymes with varying specificity for the monoterpenol moiety.
One has highest activity on sterically-hindered compounds such as (+)-bornyl diphosphate; another has highest activity on the diphosphates of primary alylic alcohols such as geraniol.
a monoterpenyl diphosphate + H2O = a monoterpenol + diphosphate.
geranylgeranyl diphosphate diphosphatase
Involved in the biosynthesis of plaunotol.
There are two isoenzymes with different ion requirements.
Neither require Mg(2+) but in addition PII is inhibited by Zn(2+), Mn(2+) and Co(2+).
It is not known which isoenzyme is involved in plaunotol biosynthesis.
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (2E,6E,10E)-geranylgeraniol + diphosphate.
The enzyme is involved in the biosynthesis of acyclic sesquiterpenoids.
(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate.
tuberculosinyl diphosphate + H2O = (13S)-isotuberculosinol + diphosphate.
The enzyme from the lycophyte Selaginella moellendorffii is bifunctional, initially forming (13E)-labda-7,13-dien-15-yl diphosphate, which is hydrolyzed to the alcohol.
geranylgeranyl diphosphate + H2O = (13E)-labda-7,13-dien-15-ol + diphosphate.
Isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree).
Geraniol is labeled when formed in the presence of [(18)O]H2O.
Thus mechanism involves a geranyl cation.
Neryl diphosphate is hydrolyzed more slowly.
(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate.
(+)-kolavenyl diphosphate + H2O = (+)-kolavelool + diphosphate.
The enzyme, characterized from Glycine max (soybeans), is specific for neryl diphosphate.
H2O + neryl diphosphate = diphosphate + nerol.
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids.
Previously regarded as identical with EC 3.1.1.2.
An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.
H2O + paraoxon = 4-nitrophenol + diethylphosphate + 2 H(+).
Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases).
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride + 2 H(+).
Exodeoxyribonucleases producing 5'-phosphomonoesters
The Escherichia coli enzyme hydrolyzes glucosylated DNA.
Similar enzymes; mammalian DNase III, exonuclease IV, T2- and T4-induced exodeoxyribonucleases.
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Has endonucleolytic activity near apurinic sites on DNA.
Similar enzyme: Haemophilus influenzae exonuclease.
Similar enzymes: T4, T5 and T7 exonucleases, mammalian DNase IV.
Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.
exodeoxyribonuclease (phage SP3-induced)
Possesses DNA-dependent ATPase activity.
Acts endonucleolytically on single-stranded circular DNA.
Similar enzyme: Haemophilus influenzae ATP-dependent DNase.
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.
Similar enzyme: Micrococcus luteus exonuclease.
Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Exodeoxyribonucleases producing 3'-phosphomonoesters
5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
5' to 3' single stranded DNA exonuclease
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Exoribonucleases producing 5'-phosphomonoesters
The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5.
Similar enzymes: RNase Q, RNase BN, RNase PIII, RNase Y.
This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13.
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
Exonucleolytic cleavage of oligonucleotides to yield nucleoside 5'-phosphates.
Cleaves poly(A) in either the single- or double-stranded form.
Exonucleolytic cleavage of poly(A) to 5'-AMP.
Alteration of the 3'-terminal base has no effect on the rate of hydrolysis whereas modification of the 3'-terminal sugar has a major effect.
tRNA terminating with a 3'-phosphate is completely inactive.
This enzyme can convert a tRNA precursor into a mature tRNA.
Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Exoribonucleases producing 3'-phosphomonoesters
Exonucleolytic cleavage to nucleoside 3'-phosphates.
Exonucleases active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters
Preference for single-stranded substrate.
Similar enzymes: hog kidney phosphodiesterase, Lactobacillus exonuclease.
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates.
Exonucleases active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters
Similar enzymes: Lactobacillus acidophilus nuclease, Bacillus subtilis nuclease, salmon testis nuclease.
Endodeoxyribonucleases producing 5'-phosphomonoesters
Similar enzymes: streptococcal DNase (streptodornase), T4 endonuclease II, T7 endonuclease II, Escherichia coli endonuclease I, 'nicking' nuclease of calf thymus, colicin E2 and E3.
Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
endodeoxyribonuclease IV (phage T4-induced)
The enzyme is an apurinic/apyrimidinic (AP) site endonuclease that primes DNA repair synthesis at AP sites.
It specifically cleaves the DNA backbone at AP sites and also removes 3' DNA-blocking groups such as 3' phosphates, 3' phosphoglycolates, and 3' alpha,beta-unsaturated aldehydes that arise from oxidative base damage and the activity of combined glycosylase/lyase enzymes.
It is also the only known repair enzyme that is able to cleave the DNA backbone 5' of the oxidative lesion alpha-deoxyadenosine.
The enzyme has a strong preference for single-stranded DNA.
Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Large group of enzymes that have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine.
They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence.
Multifunctional proteins which also catalyze the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.
Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Large group of enzymes which recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition site.
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
type III site-specific deoxyribonuclease
Has an absolute requirement for ATP, but does not hydrolyze it; S-adenosyl-L-methionine stimulates the reaction, but is not absolutely required.
Recognize specific short DNA sequences and cleave a short distance away from the recognition sequence.
Exist as complexes with enzymes of similar specificity listed under EC 2.1.1.72 or EC 2.1.1.73.
5'-CC-3'-preferring endodeoxyribonuclease
Streptomyces glaucescens exocytoplasmic endodeoxyribonuclease
Streptomyces glaucescens exocytoplasmic endonuclease
Prefers CC sites in double-stranded circular and linear DNA.
Greater affinity for double-stranded than single-stranded DNA.
Produces nicks, generating double-stranded fragments with 5'- and/or 3'-protruding single-stranded tails.
endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC.
Escherichia coli endodeoxyribonuclease V
Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.
This phage T4 enzyme is involved in degradation of host DNA.
The enzyme primarily catalyzes nicking of the bottom strand of double stranded DNA between the first and second base pair to the right of a top-strand CCGC motif.
Double-stranded breaks are produced 5- to 10-fold less frequently.
It does not cleave the T4 native DNA, which contains 5-hydroxymethylcytosine instead of cytosine.
Endonucleolytic nicking and cleavage of cytosine-containing double-stranded DNA.
The enzyme does not cleave double-stranded DNA or native T4 DNA, which contains 5-hydroxymethylcytosine instead of cytosine.
Endonucleolytic cleavage of the 5' phosphodiester bond of deoxycytidine in single-stranded DNA.
crossover junction endodeoxyribonuclease
Holliday junction-resolving endoribonuclease
The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions.
Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Endodeoxyribonucleases producing other than 5'-phosphomonoesters
Similar enzymes: crab testis DNase, snail DNase, salmon testis DNase, liver acid DNase, human acid DNases of gastric mucosa and cervix.
Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.
Preference for supercoiled DNA; little activity on linear double-stranded DNA.
Inhibited by single-stranded DNA, ATP and AMP.
Endonucleolytic cleavage of supercoiled plasma DNA to linear DNA duplexes.
Site specific endodeoxyribonucleases: cleavage is sequence specific
Site specific endodeoxyribonucleases: cleavage is not sequence specific
Site-specific endodeoxyribonucleases specific for altered bases
endodeoxyribonuclease (pyrimidine dimer)
Acts on a damaged strand, 5' from the damaged site.
Similar enzymes: T4 endonuclease V, Escherichia coli endonuclease III and V, correndonuclease II.
Endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate.
Endoribonucleases producing 5'-phosphomonoesters
Endonucleolytic cleavage to 5'-phosphomonoester.
An endoribonuclease that cleaves double-stranded RNA molecules.
The cleavage can be either a single-stranded nick or double-stranded break in the RNA, depending in part upon the degree of base-pairing in the region of the cleavage site.
Specificity is conferred by negative determinants, i.e., the presence of certain Watson-Crick base-pairs at specific positions that strongly inhibit cleavage.
RNase III is involved in both rRNA processing and mRNA processing and decay.
Essential for tRNA processing; generates 5'-termini of mature tRNA molecules.
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Forms oligonucleotides with an average chain length of 10.
Endonucleolytic cleavage of poly(A) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Endonucleolytic cleavage of RNA, removing 3'-extranucleotides from tRNA precursor.
Converts the 5S-rRNA precursor from Bacillus subtilis into 5S-rRNA, with 5'-phosphate and 3'-hydroxy groups.
Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor.
Forms oligonucleotides with chain length 6-12.
Endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Acts on poly(U) and poly(C), with a higher affinity for poly(C), but does not act on poly(A) or poly(G).
Endonucleolytic cleavage of poly(U) or poly(C) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication.
The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction.
2'-O-methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5' to that locus.
In Escherichia coli, the enzyme is found in the RNA degradosome.
The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, EC 4.1.1.11 and EC 2.7.7.8.
Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.
Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication.
To perform this task the enzyme combines two distinct activities.
The polymerase domain (EC 2.7.7.49) occupies the N-terminal two-thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third.
The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites.
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
eukaryotic translation initiation factor 2C 2
The enzyme, isolated from animals, is required for RNA-mediated gene silencing (RNAi).
Endoribonucleases producing other than 5'-phosphomonoesters
Cleavage takes place between a cytosine and an adenine.
Endonucleolytic cleavage of RNA precursor into two, leaving 5'-hydroxy and 3'-phosphate groups.
Hydrolysis of poly(A), forming oligoribonucleotides and ultimately 3'-AMP.
Endoribonucleases active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters
Similar enzymes: Neurospora crassa nuclease, mung bean nuclease, Penicillium citrinum nuclease P1.
Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products.
Hydrolyzes double- or single-stranded substrate.
Similar enzymes: silkworm nuclease, potato nuclease, Azotobacter nuclease.
Endoribonucleases active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters
Similar enzymes: Chlamydomonas nuclease, spleen phosphodiesterase, spleen endonuclease.
Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration.
The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion.
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyze 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides.
This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides.
EC 3.2.1.20 from mammalian intestine can catalyze similar reactions.
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Substrates include laminarin, lichenin and cereal D-glucans.
Different from EC 3.2.1.39 and EC 3.2.1.52.
Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.
Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin.
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
This enzyme, like EC 3.2.1.33, can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41, EC 3.2.1.142 and EC 3.2.1.68 is maltose.
It also hydrolyzes isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin.
The enzyme from intestinal mucosa is a single polypeptide chain that also catalyzes the reaction of EC 3.2.1.48.
Differs from EC 3.2.1.33 in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.
The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act.
Activity is greatly stimulated in the presence of EC 1.14.99.53, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase.
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
The enzyme catalyzes the random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
Different forms of the enzyme have different tolerances to methyl esterification of the substrate.
(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
The enzyme does not act on 4-O-acetylated sialic acids.
An endo-alpha-sialidase activity is listed as EC 3.2.1.129.
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Group of enzymes whose specificity is directed mainly toward the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyze oligosaccharides rapidly, relative to polysaccharides, which are hydrolyzed relatively slowly, or not at all.
The intestinal enzyme also hydrolyzes polysaccharides, catalyzing the reactions of EC 3.2.1.3, and, more slowly, hydrolyzes 1,6-alpha-D-glucose links.
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Some examples also hydrolyze one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides and beta-D-fucosides.
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
globoside Gb3Cer (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + D-galactose.
Some enzymes in this group hydrolyze alpha-L-arabinosides; some animal enzymes also hydrolyze beta-D-fucosides and beta-D-glucosides (cf. EC 3.2.1.108).
Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Also hydrolyzes alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Also catalyzes fructotransferase reactions.
Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
The enzyme is an anomer-inverting glucosidase that catalyzes the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha-trehalose, releasing initially equimolar amounts of alpha- and beta-D-glucose.
It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose.
a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate.
This enzyme is found mostly in marine bacteria, which break down the beta(1,3)-xylan found in the cell wall of some green and red algae.
The enzyme produces mainly xylobiose, xylotriose and xylotetraose.
Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
This enzyme hydrolyzes an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain.
The enzyme activity found in mammals and Saccharomyces cerevisiae is in a polypeptide chain containing two active centers.
The other activity is similar to that of EC 2.4.1.25, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyze.
Together, these two activities constitute the glycogen debranching system.
Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.
Also hydrolyzes 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan.
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
Random hydrolysis of (1->3)-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate.
Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Enzymes from some sources also hydrolyze beta-D-galactosides and/or beta-D-glucosides and/or alpha-L-arabinosides.
The activity of EC 3.2.1.37 is an associated activity found in some sources (e.g. liver).
Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides.
Very limited action on mixed-link (1->3,1->4)-beta-D-glucans.
Hydrolyzes laminarin, paramylon and pachyman.
Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing beta-L-rhamnose.
Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal alpha-L-rhamnose.
Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides.
H2O + quercitrin = L-rhamnopyranose + quercetin.
alpha-dextrin endo-1,6-alpha-glucosidase
Different from EC 3.2.1.142 in its action on glycogen, and its rate of hydrolysis of limit dextrins.
Maltose is the smallest sugar that it can release from an alpha-(1->6)-linkage.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
GDP-alpha-D-glucose + H2O = D-glucose + GDP + H(+).
Hydrolysis of terminal, non-reducing beta-L-rhamnose residues in beta-L-rhamnosides.
D-glucosyl-N-acylsphingosine glucohydrolase
Also acts on glucosylsphingosine (cf. EC 3.2.1.62).
a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose.
a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-galactose.
Isolated from intestinal mucosa as a single polypeptide chain also displaying activity toward isomaltose (EC 3.2.1.10).
Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.
an N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H2O = an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + N-acetyl-D-galactosamine.
Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.
an alpha-L-fucoside + H2O = an alcohol + L-fucose.
Acts on N-acetylglucosides and N-acetylgalactosides.
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-beta-D-galactosaminides.
cyclomaltodextrin + H2O = linear maltodextrin.
non-reducing end alpha-L-arabinofuranosidase
Acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans.
Some EC 3.2.1.23 and EC 3.2.1.38 enzymes also hydrolyze alpha-L-arabinosides.
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
glucuronosyl-disulfoglucosamine glucuronidase
3-D-glucuronosyl-N(2),6-disulfo-beta-D-glucosamine + H2O = D-glucuronate + N(2),6-disulfo-D-glucosamine.
The enzyme has practically no action on starch.
Panose (4-alpha-isomaltosylglucose) is hydrolyzed to isomaltose and glucose.
Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose).
Acts on oligosaccharides, but very slowly on laminaribiose.
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.
Products from pseudonigeran (1,3-alpha-D-glucan) are nigerose and alpha-D-glucose.
Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.
Compare EC 3.2.1.2, which removes successive maltose residues, and EC 3.2.1.98 and EC 3.2.1.116.
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
Products are nigerose and 4-alpha-D-nigerosylglucose.
No hydrolysis of alpha-D-glucans containing only 1,3- or 1,4-bonds.
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in alpha-D-glucans containing both (1->3)- and (1->4)-bonds.
glycosyl-N-acylsphingosine glycohydrolase
The enzyme, found in the intestinal mucosa, hydrolyzes beta-D-glucosyl and beta-D-galactosyl residues from a very broad range of substrates using a retaining mechanism.
Characterized substrates include glucosyl- and galactosyl-ceramides, O(3)-, O(4') and O(7)-glucosylated flavonoids, and the 2'-O-glucosylated dihydrochalcone phlorizin.
The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family.
While one domain is responsible for the activity described here, the other catalyzes the reaction of EC 3.2.1.108. cf. EC 3.2.1.45 and EC 3.2.1.46.
glycosyl-N-acylsphingosine + H2O = N-acylsphingosine + a sugar.
a beta-D-galactosyl-N-acylsphingosine + H2O = a ceramide + beta-D-galactose.
a flavonoid-O-beta-D-glucoside + H2O = a flavonoid + beta-D-glucose.
Highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by 1,2-alpha-linkage.
H2O + methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside = L-fucose + methyl beta-D-galactoside.
2,6-beta-D-fructan 6-beta-D-fructofuranosylfructohydrolase
Hydrolysis of (2->6)-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain.
Random hydrolysis of (2->6)-beta-D-fructofuranosidic linkages in (2->6)-beta-D-fructans (levans) containing more than 3 fructose units.
The enzyme hydrolyzes the first glycosidic bond from the non-reducing end of the substrate.
It is specific for saturated oligomers of D-homogalacturonan, and is unable to degrade unsaturated substrates or methyl-esterified substrates.
[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate.
Differs from EC 3.2.1.41 and EC 3.2.1.142 by its inability to hydrolyze pullulan, and by limited action on alpha-limit dextrins.
Maltose is the smallest sugar it can release from an alpha-(1->6)-linkage.
Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.
Hydrolysis is accompanied by inversion at C-1, so that new reducing ends are released in the beta-configuration.
Dextrans and isomaltosaccharides are hydrolyzed, as is isomaltose, but very slowly.
The enzyme from some sources also possesses the activity of EC 3.2.1.59.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha-D-glucans and derived oligosaccharides.
Random hydrolysis of (1->2)-glucosidic linkages in (1->2)-beta-D-glucans.
Hydrolysis of successive xylose residues from the non-reducing termini of (1->3)-beta-D-xylans.
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Acts on 1,4-beta-D-glucans and related oligosaccharides.
Cellobiose is hydrolyzed, but very slowly.
Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.
Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate.
A 1,6-alpha-D-mannan backbone remains after action on Saccharomyces cerevisiae mannan.
Hydrolysis of (1->2)- and (1->3)-linkages in yeast mannan, releasing mannose.
Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Hydrolyzes inulin and levan, and also sucrose.
Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.
Also acts on porphyran, but more slowly.
Cleaves the beta-(1->4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.
The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB.
Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
The enzyme, characterized from bacteria, hydrolyzes the second alpha-1,4-glycosidic bond from the non-reducing end of polygalacturonate, releasing digalacturonate.
[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-2) + alpha-D-galacturonosyl-(1->4)-D-galacturonate.
kappa-carrageenan 4-beta-D-glycanohydrolase
The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate.
Unlike EC 3.2.1.157, but similar to EC 3.2.1.81, this enzyme proceeds with retention of the anomeric configuration.
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.
Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans.
beta-D-phosphogalactoside galactohydrolase
a 6-phospho-beta-D-galactoside + H2O = an alcohol + D-galactose 6-phosphate.
H2O + lactose 6-phosphate = beta-D-glucose + D-galactose 6-phosphate.
Also hydrolyzes several other phospho-beta-D-glucosides, but not their non-phosphorylated forms.
6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.
capsular-polysaccharide endo-1,3-alpha-galactosidase
Hydrolyzes the galactosyl-alpha-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization.
Random hydrolysis of (1->3)-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide.
non-reducing end beta-L-arabinopyranosidase
The enzyme, which was characterized from dormant seeds of the plant Cajanus cajan (pigeon pea), has been shown to remove the terminal non-reducing beta-L-arabinopyranoside residue from the artificial substrate p-nitrophenyl-beta-L-arabinopyranose.
In the presence of methanol the enzyme demonstrates transglycosylase activity, transferring the arabinose moiety to methanol while retaining the anomeric configuration, generating 1-O-methyl-beta-L-arabinopyranose.
Removal of a terminal beta-L-arabinopyranose residue from the non-reducing end of its substrate.
arabinogalactan endo-beta-1,4-galactanase
This enzyme, isolated from the bacterium Bacillus subtilis, hydrolyzes the beta(1->4) bonds found in type I plant arabinogalactans, which are a component of the primary cell walls of dicots.
The predominant product is a tetrasaccharide.
The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.
cellulose 1,4-beta-cellobiosidase (non-reducing end)
4-beta-D-glucan cellobiohydrolase (non-reducing end)
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Hydrolysis of terminal, non-reducing N-acetylmuramic residues.
alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-glucose 6-phosphate.
Optimum activity is on those 1,6-alpha-D-glucans containing 6, 7 and 8 glucose units; those containing 3, 4 and 5 glucose units are hydrolyzed at slower rates.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in dextrans, to remove successive isomaltotriose units from the non-reducing ends of the chains.
mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
di-N-acetylchitobiosyl beta-N-acetylglucosaminidase
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein, the rest of the oligosaccharide is released intact.
D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine mucinaminohydrolase
D-galactosyl-N-acetyl-alpha-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
glycopeptide alpha-N-acetylgalactosaminidase
The enzyme catalyzes the liberation of Gal-(1->3)-beta-GalNAc alpha-linked to serine or threonine residues of mucin-type glycoproteins.
EngBF from Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1->3)-beta-GalNAc.
The enzymes from Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. release of the core 2 trisaccharide Gal-(1->3)-beta-(GlcNAc-(1->6)-beta)-GalNAc or the core 3 disaccharide GlcNAc-(1->3)-beta-GalNAc).
The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] = beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + L-seryl-[protein].
H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] = beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + L-threonyl-[protein].
Cf. EC 3.2.1.3, which removes successive glucose residues.
Cf. EC 3.2.1.2, which removes successive maltose residues.
Cf. EC 3.2.1.116, which removes successive maltotriose residues.
Cf. EC 3.2.1.60, which removes successive maltotetraose residues.
The products have the alpha-configuration.
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.
Acts best on linear 1,5-alpha-L-arabinan.
Also acts on branched arabinan, but more slowly.
Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Hydrolysis of (1->4)-beta-D-mannosidic linkages in (1->4)-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends.
Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
blood-group-substance endo-1,4-beta-galactosidase
Hydrolyzes the 1,4-beta-D-galactosyl linkages adjacent to a 1,3-alpha-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-alpha-D-fucosyl residue.
Endohydrolysis of (1->4)-beta-D-galactosidic linkages in blood group A and B substances.
keratan-sulfate endo-1,4-beta-galactosidase
Hydrolyzes the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha-D-glucosaminyl residues.
Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102).
Endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate.
Acts on glucosides of cholesterol and sitosterol, but not on some related sterols such as coprostanol.
cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D-glucose.
H2O + sitosteryl 3-beta-D-glucoside = D-glucose + sitosterol.
3alpha(S)-strictosidine beta-glucosidase
Does not act on a number of closely related glycosides.
Strictosidine is a precursor of indole alkaloids.
3alpha(S)-strictosidine + H2O = D-glucose + strictosidine aglycone.
Glc3Man9NAc2 oligosaccharide glucosidase
This enzyme catalyzes the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal alpha-1,2-linked glucose residue.
This and subsequent processing steps are required before complex N-glycans can be synthesized.
H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein].
protein-glucosylgalactosylhydroxylysine glucosidase
The enzyme specifically hydrolyzes glucose from alpha-D-glucosyl-(1->2)-beta-D-galactosyl disaccharide units that are linked to hydroxylysine residues of collagen and collagen-like proteins.
Acetylation of the epsilon-amino group of the glycosylated hydroxylysine abolishes activity.
(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysyl-[collagen] + H2O = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + D-glucose.
The enzyme from intestinal mucosa contains two glycosyl hydrolase domains, both of which belong to glycosyl hydrolase family 1 (GH1).
While the first domain catalyzes the activity described here, the second domain catalyzes the reaction of EC 3.2.1.62. cf. EC 3.2.1.33.
H2O + lactose = beta-D-galactose + D-glucose.
Endohydrolysis of (1->4)-alpha-D-galactosaminidic linkages in poly(D-galactosamine).
Hydrolysis of (1->3)-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins.
a 2-deoxy-alpha-D-glucoside + H2O = 2-deoxy-D-glucose + an alcohol.
mannosyl-oligosaccharide 1,2-alpha-mannosidase
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures.
The enzymes catalyze the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins.
Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209.
The enzymes are type II membrane proteins, require Ca(2+), and use an inverting mechanism.
While all three human enzymes can catalyze the reactions listed here, some of the enzymes can additionally catalyze hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same.
The names of the isomers listed here are based on a nomenclature system proposed by Prien et al.
4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2).
3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2).
mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site.
2 H2O + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = 2 alpha-D-mannopyranose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein].
branched-dextran exo-1,2-alpha-glucosidase
Does not hydrolyze disaccharides or oligosaccharides containing linear 1,2-alpha-glucosidic linkages.
Hydrolysis of (1->2)-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose.
The products of all these enzymes have the alpha-configuration.
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends.
Highly specific; does not act on prunasin, linamarin, gentiobiose or cellobiose (cf. EC 3.2.1.21).
(R)-amygdalin + H2O = (R)-prunasin + D-glucose.
Highly specific; does not act on amygdalin, linamarin or gentiobiose (cf. EC 3.2.1.21).
(R)-prunasin + H2O = D-glucose + mandelonitrile.
Also hydrolyzes, more slowly, (R)-amygdalin and (R)-prunasin, but not gentiobiose, linamarin or cellobiose.
(R)-vicianin + H2O = mandelonitrile + vicianose.
isoprimeverose-producing oligoxyloglucan hydrolase
Hydrolysis of (1->4)-beta-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose [i.e. alpha-xylo-(1->6)-beta-D-glucosyl-] residues from the non-reducing chain ends.
Does not act on alginic acid, which is a copolymer of polymannuronate.
Endohydrolysis of the D-mannuronide linkages of polymannuronate.
Hydrolyzes a variety of 6-phospho-alpha-D-glucosides, including alpha-maltose 6-phosphate, alpha,alpha-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (as a chromogenic substrate).
The enzyme is activated by Fe(2+), Mn(2+), Co(2+) and Ni(2+).
alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.
oligoglycosylglucosylceramide glycohydrolase
An enzyme from Rhodococcus sp. which degrades various acidic and neutral glycosphingolipids to oligosaccharides and ceramides, by cleaving a glucosyl bond.
Does not act on monoglycosylceramides (cf. EC 3.2.1.62).
an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose.
The enzyme from a bacteriophage catalyzes the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli.
Endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides.
Highly specific; some other ajmalan glucoside alkaloids are hydrolyzed, more slowly.
H2O + raucaffricine = D-glucose + vomilenine.
Also hydrolyzes syringin, 4-cinnamyl alcohol beta-glucoside and, more slowly, some other aryl beta-glycosides.
A plant cell-wall enzyme involved in the biosynthesis of lignin.
4-O-(beta-D-glucosyl)-trans-coniferol + H2O = (E)-coniferol + D-glucose.
The enzyme from Aspergillus niger does not act on 1,2-, 1,3-, or 1,4-L-fucosyl linkages.
Hydrolysis of (1->6)-linkages between alpha-L-fucose and N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin.
The enzyme from Aspergillus niger is specific for the hydrolysis of the triterpenoid glycoside glycyrrhizinate from roots of Glycyrrhiza sp.
glycyrrhizin + H2O = 2-(beta-D-glucuronosyl)-D-glucuronate + glycyrrhetinate.
poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase
Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetyl-substituted substrates.
An exo-alpha-sialidase activity is listed as EC 3.2.1.18.
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.
The enzyme catalyzes the hydrolysis of the terminal alpha-D-glucosyl-(1->3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus.
H2O + N-{alpha-Glc-(1->3)-alpha-Man-(1->2)-alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->6)]-alpha-Man-(1->6)]-beta-Man-(1->4)-beta-GlcNAc-(1->4)-beta-GlcNAc}-L-asparaginyl-[protein] = alpha-D-glucosyl-(1->3)-D-mannopyranose + N(4)-{alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlaNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,2).
Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.
A whole spectrum of chitosanases are now known that can hydrolyze various types of links in chitosan.
The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases.
One known chitosanase is limited to this link recognition, while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both.
They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.
Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan.
Acts on starch and related polysaccharides and oligosaccharides.
The product is alpha-maltose; cf. EC 3.2.1.2.
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.
Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
glucuronoarabinoxylan endo-1,4-beta-xylanase
High activity toward feruloylated arabinoxylans from cereal plant cell walls.
Endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Mannose residues linked alpha-D-1,3- are also released very slowly.
Hydrolysis of (1->2)-alpha-D- and (1->6)-alpha-D- linkages in yeast mannan, releasing D-mannose.
Considerable differences in the specificities of the enzymes from different fungi for alpha-D-glucosiduronates have been reported.
an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate.
The enzyme from Streptomyces specifically hydrolyzes the terminal lacto-N-biosyl residue (beta-D-Gal-(1->3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->R).
Lacto-N-hexaose (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolyzed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose.
Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates.
Asialo GM1 tetraose (beta-D-Gal-(1->3)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is hydrolyzed very slowly, but lacto-N-neotetraose (beta-D-Gal-(1->4)-beta-D-GalNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) is not a substrate.
beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + H2O = beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + lactose.
4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase
maltooligosyl trehalose trehalohydrolase
malto-oligosyltrehalose trehalohydrolase
hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
Plant enzymes with little or no action on glycogen.
Action on amylopectin is incomplete, but action on alpha-limit dextrins is complete.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and beta-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan.
Specific to (1''-2') linkage of ribose-ribose bond of poly(ADP-D-ribose).
[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D-ribose](n-1) + ADP-D-ribose.
Releases Kdo (alpha- and beta-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S.minnesota, and de-O-acyl-re-LPS.
4-Methylumbelliferyl-alpha-Kdo (alpha-Kdo-OMec) is also a substrate.
3-deoxyoctulosonyl-[lipopolysaccharide] + H2O = 3-deoxyoctulosonate + [lipopolysaccharide].
This enzyme removes not only free galactose, but also 6-glycosylated residues, e.g., (1->6)-beta-D-galactobiose, and galactose bearing oligosaccharide chains on O-6.
Hence, it releases branches from [arabino-galacto-(1->6)]-(1->3)-beta-D-galactans.
Hydrolysis of terminal, non-reducing beta-D-galactose residues in (1->3)-beta-D-galactopyranans.
The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.
Hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose.
Has a wide specificity for thioglycosides.
a thioglucoside + H2O = a sugar + a thiol.
The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea.
In addition to beta-primeverosides [i.e. 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranosides], it also hydrolyzes 6-O-(beta-D-apiofuranosyl)-beta-D-glucopyranosides and, less rapidly, beta-vicianosides and 6-O-(alpha-L-arabinofuranosyl)-beta-D-glucopyranosides, but not beta-glucosides.
Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolyzed.
a 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranoside + H2O = a 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose + an alcohol.
oligoxyloglucan reducing-end-specific cellobiohydrolase
The enzyme is found in the fungus Geotrichum sp. M128.
The substrate is a hemicellulose found in plant cell walls.
Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
xyloglucan-specific endo-beta-1,4-glucanase
The enzyme from Aspergillus aculeatus is specific for xyloglucan and does not hydrolyze other cell-wall components.
The reaction involves endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues.
xyloglucan + H2O = xyloglucan oligosaccharides.
mannosylglycoprotein endo-beta-mannosidase
The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein.
The mannose residue at the non-reducing end of the sequence may carry further alpha-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the beta-D-mannosyl group prevents the action of the enzyme.
The enzyme was obtained from the lily, Lilium longiflorum.
Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequences.
beta-(2-1)-linkage-specific fructan-beta-fructosidase
Possesses one of the activities of EC 3.2.1.80.
While the best substrates are the inulin-type fructans, such as 1-kestose (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside) and 1,1-nystose (beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside), some (but not all) levan-type fructans can also be hydrolyzed, but more slowly (see EC 3.2.1.154).
Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.
Hydrolysis of terminal, non-reducing (2->1)-linked beta-D-fructofuranose residues in fructans.
While the best substrates are the levan-type fructans such as 6-kestotriose (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl alpha-D-glucopyranoside) and 6,6-kestotetraose (beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl-(2->6)-beta-D-fructofuranosyl alpha-D-glucopyranoside), some (but not all) inulin-type fructans can also be hydrolyzed, but more slowly (cf. EC 3.2.1.153).
Hydrolysis of terminal, non-reducing (2->6)-linked beta-D-fructofuranose residues in fructans.
xyloglucan-specific endo-processive beta-1,4-glucanase
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucohydrolase
xyloglucan-specific exo-beta-1,4-glucanase
The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide.
Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group.
The enzyme does not display activity, or shows very low activity, toward other beta-D-glucans.
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the newly-formed chain end after endo-initiation on a polymer molecule.
reducing end xylose-releasing exo-oligoxylanase
The enzyme, originally isolated from the bacterium Bacillus halodurans C-125, releases the xylose unit at the reducing end of oligosaccharides ending with the structure beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the new reducing end in the alpha configuration.
It is specific for the beta anomers of xylooligosaccharides whose degree of polymerization is equal to or greater than 3.
The penultimate residue must be beta-D-xylopyranose, but replacing either of the flanking residues with glucose merely slows the rate greatly.
Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides.
The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate.
Iota-neocarraoctaose is the shortest substrate oligomer that can be cleaved.
Unlike EC 3.2.1.81 and EC 3.2.1.83, this enzyme proceeds with inversion of the anomeric configuration.
Iota-carrageenan differs from kappa-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the kappa-compound on O-4 of the D-galactose residues.
Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans.
The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate.
The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer.
While the enzyme can also hydrolyze the highly sulfated agarose porphyran very efficiently, it cannot hydrolyze kappa-carrageenan and iota-carrageenan.
Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product.
alpha-neoagaro-oligosaccharide hydrolase
When neoagarohexaose is used as a substrate, the oligosaccharide is cleaved at the non-reducing end to produce 3,6-anhydro-L-galactose and agaropentaose, which is further hydrolyzed to agarobiose and agarotriose.
With neoagarotetraose as substrate, the products are predominantly agarotriose and 3,6-anhydro-L-galactose.
In Vibrio sp. the actions of EC 3.2.1.81 and EC 3.2.1.159 can be used to degrade agarose to 3,6-anhydro-L-galactose and D-galactose.
Hydrolysis of the 1,3-alpha-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose.
isoflavonoid-7-O-beta[D-apiosyl-(1->6)-beta-D-glucoside] disaccharidase
isoflavonoid 7-O-beta-apiosyl-glucoside beta-glucosidase
Removes disaccharides from the natural substrates dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and 7-hydroxy-2',4',5',6-tetramethoxy-7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside (dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides.
Daidzin and genistin are also substrates.
7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.
dalnigrein beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside + H2O = beta-D-apiofuranosyl-(1->6)-D-glucopyranose + dalnigrein + H(+).
dalpatein beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside + H2O = beta-D-apiofuranosyl-(1->6)-D-glucopyranose + dalpatein + H(+).
endo-beta-1,4-carrageenose 2,6,2'-trisulfate-hydrolase
The enzyme from Pseudoalteromonas sp. is specific for lambda-carrageenan.
iota-carrageenan (see EC 3.2.1.157), kappa-carrageenan (see EC 3.2.1.83), agarose and porphyran are not substrates.
Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Galp2,6S2-(1->3)-beta-D-Galp2S-(1->4)-alpha-D-Galp2,6S2-(1->3)-D-Galp2S.
Specific for (1->6)-linked mannobiose and has no activity toward any other linkages, or toward p-nitrophenyl-alpha-D-mannopyranoside or mannan from Saccharomyces cerevisiae (baker's yeast).
It is strongly inhibited by Mn(2+) but does not require Ca(2+) or any other metal cofactor for activity.
Hydrolysis of the 1,6-linked alpha-D-mannose residues in alpha-D-Manp-(1->6)-D-Manp.
Specifically hydrolyzes 1,6-beta-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals.
1,3-beta-D- and 1,4-beta-D-galactosyl residues cannot act as substrates.
Can also hydrolyze alpha-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots.
AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death.
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and beta-(1->6)-galactaobiose as the final products.
Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues.
Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols.
Can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc.
Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.
Heparanase cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group.
Heparanase-1 cuts macromolecular heparin into fragments of 5000-20000 Da.
The enzyme cleaves the heparan sulfate glycosaminoglycans from proteoglycan core proteins and degrades them to small oligosaccharides.
Inside cells, the enzyme is important for the normal catabolism of heparan sulfate proteoglycans, generating glycosaminoglycan fragments that are then transported to lysosomes and completely degraded.
When secreted, heparanase degrades basement membrane heparan sulfate glycosaminoglycans at sites of injury or inflammation, allowing extravasion of immune cells into nonvascular spaces and releasing factors that regulate cell proliferation and angiogenesis.
endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan.
The enzyme also hydrolyzes wogonin 7-O-beta-D-glucuronide and oroxylin 7-O-beta-D-glucuronide with lower efficiency.
Neglegible activity with p-nitrophenyl-beta-D-glucuronide.
baicalin + H2O = baicalein + D-glucuronate + H(+).
H2O + wogonin 7-O-beta-D-glucuronate = D-glucuronate + H(+) + wogonin.
H2O + oroxylin A 7-O-beta-D-glucuronate = D-glucuronate + H(+) + oroxylin A.
hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase
The enzyme exhibits high specificity toward 7-O-linked flavonoid beta-rutinosides.
(2S)-hesperidin + H2O = (2S)-hesperetin + rutinose.
EC 2.4.1.155 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.
3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine.
3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O = L-threonyl-[protein] + N-acetyl-D-glucosamine.
The enzyme participates in the mannosylglycerate degradation pathway of some bacteria.
Mannosylglycerate is phosphorylated during transport into the cell, and the phosphorylated form is hydrolyzed by this enzyme.
(2R)-2-O-(alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + D-mannose.
The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus.
Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end.
unsaturated rhamnogalacturonyl hydrolase
The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168.
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose.
Exohydrolysis of the alpha-D-GalA-(1->2)-alpha-L-Rha bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing D-galacturonic acid from the non-reducing end of rhamnogalacturonan oligosaccharides.
Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides.
beta-D-glucopyranosyl abscisate beta-glucosidase
beta-D-glucopyranosyl abscisate hydrolase
The enzyme hydrolzes the biologically inactive beta-D-glucopyranosyl ester of abscisic acid to produce active abscisate.
Abscisate is a phytohormone critical for plant growth, development and adaption to various stress conditions.
The enzyme does not hydrolyze beta-D-glucopyranosyl zeatin.
(+)-abscisic acid D-glucopyranosyl ester + H2O = 2-cis-(+)-abscisate + beta-D-glucose + H(+).
cellulose 1,4-beta-cellobiosidase (reducing end)
Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48), act at the reducing ends of cellulose and similar substrates.
The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism.
It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism.
Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end.
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
The enzyme catalyzes hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide.
Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
The backbone of porphyran consists largely (approximately 70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate [the other 30% are mostly agarobiose repeating units of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked 3,6-anhydro-alpha-L-galactopyranose].
This enzyme cleaves the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose, although some longer oligosaccharides of even number of residues are also observed.
Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products.
Methylation of the D-galactose prevents the enzyme from Zobellia galactanivorans, but not that from Wenyingzhuangia fucanilytica, from binding at position -1.
Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran.
gellan tetrasaccharide unsaturated glucuronosyl hydrolase
gellan tetrasaccharide unsaturated glucuronyl hydrolase
The enzyme releases 4-deoxy-4(5)-unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases, e.g. the tetrasaccharide beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp produced by EC 4.2.2.25.
The enzyme can also hydrolyze unsaturated chondroitin and hyaluronate disaccharides (beta-D-4-deoxy-Delta(4)-GlcAp-(1->3)-beta-D-GalNAc, beta-D-4-deoxy-Delta(4)-GlcAp-(1->3)-beta-D-GalNAc6S, beta-D-4-deoxy-Delta(4)-GlcAp2S-(1->3)-beta-D-GalNAc, beta-D-4-deoxy-Delta(4)-GlcAp-(1->3)-beta-D-GlcNAc), preferring the unsulfated disaccharides to the sulfated disaccharides.
beta-D-Delta(4)-GlcA-(1->4)-beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc + H2O = 5-dehydro-4-deoxy-D-glucuronate + beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc.
beta-D-4-deoxy-Delta(4)-GlcpA-(1->3)-beta-D-GalpNAc + H2O = 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine.
4-deoxy-Delta(4)-beta-D-GlcpA2S-(1->3)-beta-D-GalpNAc + H2O = 5-dehydro-4-deoxy-2-O-sulfo-D-glucuronate + N-acetyl-beta-D-galactosamine.
beta-D-4-deoxy-Delta(4)-GlcpA-(1->3)-beta-D-GlcpNAc + H2O = 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine.
unsaturated chondroitin disaccharide hydrolase
The enzyme releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides, hyaluronan disaccharides and heparin disaccharides and cleaves both glycosidic (1->3) and (1->4) bonds.
It prefers the sulfated disaccharides to the unsulfated disaccharides.
beta-D-4-deoxy-Delta(4)-GlcpA-(1->3)-beta-D-GalpNAc6S + H2O = 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine 6-sulfate.
The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyzes the beta(1->3) bonds found in type II plant arabinogalactans, which occur in cell walls of dicots and cereals.
The enzyme is an endohydrolase, and requires at least 3 contiguous beta-1,3-residues.
The enzyme specifically hydrolyzes beta-1,3-galactan and beta-1,3-galactooligosaccharides.
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase
The enzyme from Triticum aestivum (wheat) has a higher affinity for DIMBOA glucoside than DIBOA glucoside.
With Secale cereale (rye) the preference is reversed.
DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA.
DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA.
UDP-N-acetylglucosamine 2-epimerase (hydrolyzing)
The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus.
It catalyzes the first step of sialic acid (N-acetylneuraminic acid) biosynthesis.
The initial product formed is the alpha anomer, which rapidly mutarotates to a mixture of anomers.
The mammalian enzyme is bifunctional and also catalyzes EC 2.7.1.60.
H2O + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-D-mannosamine + UDP.
UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolyzing)
Involved in biosynthesis of legionaminic acid, a nonulosonate derivative that is incorporated by some bacteria into assorted virulence-associated cell surface glycoconjugates.
The initial product formed by the enzyme from Legionella pneumophila, which incorporates legionaminic acid into the O-antigen moiety of its lipopolysaccharide, is 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose, which rapidly mutarotates to a mixture of anomers.
The enzyme from Campylobacter jejuni, which incorporates legionaminic acid into flagellin, prefers GDP-N,N'-diacetylbacillosamine.
H2O + UDP-N,N'-diacetylbacillosamine = 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + H(+) + UDP.
GDP-N,N'-diacetylbacillosamine + H2O = 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + GDP + H(+).
non-reducing end beta-L-arabinofuranosidase
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the beta-L-arabinofuranose residue from the non-reducing end of multiple substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose.
In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue.
beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O = 2 beta-L-arabinofuranose.
furostanol 26-O-beta-D-glucoside glucohydrolase
furostanol glycoside 26-O-beta-D-glucosidase
The enzyme has been characterized from the plants Cheilocostus speciosus and Solanum torvum.
It also hydrolyzes the 26-beta-D-glucose group from related steroid glucosides such as protogracillin, torvoside A and torvoside H.
H2O + protodioscin = 26-deglucoprotodioscin + D-glucose.
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, is specific for (Ara-f)3-Hyp, a sugar chain found in hydroxyproline-rich glyoproteins such as extensin and lectin.
The enzyme was not able to accept (Ara-f)2-Hyp or (Ara-f)4-Hyp as substrates.
4-O-(beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H2O = 4-O-(beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose.
Isolated from oat (Avena sativa) seedlings.
The product acts as a defense system against fungal infection.
avenacoside B + H2O = 26-desgluco-avenacoside B + D-glucose.
The enzyme is involved in degradation of the steroid saponin dioscin by some fungi of the Absidia genus.
The enzyme can also hydrolyze 3-O-[alpha-L-Ara-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin into diosgenin and free sugars as the final products.
dioscin + 3 H2O = D-glucose + diosgenin + 2 L-rhamnopyranose.
dioscin glycosidase (3-O-beta-D-Glc-diosgenin-forming)
The enzyme is involved in the hydrolysis of the steroid saponin dioscin by the digestive system of Sus scrofa (pig).
dioscin + 2 H2O = diosgenin 3-O-beta-D-glucoside + 2 L-rhamnopyranose.
Ginsenosidase type III catalyzes the sequential hydrolysis of the 3-O-beta-D-(1->2)-glucopyranosyl bond followed by hydrolysis of the 3-O-beta-D-glucopyranosyl bond of protopanaxadiol ginsenosides.
When acting for example on ginsenoside Rb1 the enzyme first generates ginsenoside XVII, and subsequently ginsenoside LXXV.
a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + 2 H2O = a protopanaxadiol-type ginsenoside with no glycosidic modification at position 3 + 2 D-glucopyranose.
(20S)-ginsenoside Rd + 2 H2O = (20S)-ginsenoside C-K + 2 D-glucose.
(20S)-ginsenoside Rb2 + 2 H2O = (20S)-ginsenoside C-Y + 2 D-glucose.
(20S)-ginsenoside Rb1 + 2 H2O = 2 D-glucose + gypenoside LXXV.
(20S)-ginsenoside Rg3 + 2 H2O = (20S)-protopanaxadiol + 2 D-glucose.
Ginsenosidases catalyze the hydrolysis of glycosyl moieties attached to the C-3, C-6 or C-20 position of ginsenosides.
They are specific with respect to the nature of the glycosidic linkage, the position and the order in which the linkages are cleaved.
Ginsenoside Rb1 beta-glucosidase specifically and sequentially hydrolyzes the 20-[beta-D-glucopyranosyl-(1->6)-beta-D glucopyranosyloxy] residues attached to position 20 by first hydrolyzing the (1->6)-glucosidic bond to generate ginsenoside Rd as an intermediate, followed by hydrolysis of the remaining 20-O-beta-D-glucosidic bond.
(20S)-ginsenoside Rb1 + 2 H2O = (20S)-ginsenoside Rg3 + 2 D-glucose.
The enzyme hydrolyzes the 3-O-beta-D-(1->2)-glucosidic bond, the 3-O-beta-D-glucopyranosyl bond and the 20-O-beta-D-(1->6)-glycosidic bond of protopanaxadiol-type ginsenosides.
It usually leaves a single glucosyl residue attached at position 20 and one or no glucosyl residues at position 3.
Starting with a ginsenoside that is glycosylated at both positions (e.g. ginsenoside Rb1, Rb2, Rb3, Rc or Rd), the most common products are ginsenoside F2 and ginsenoside C-K, with low amounts of ginsenoside Rh2.
a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O = a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose.
a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + H2O = a protopanaxadiol-type ginsenoside with no glycosidic modifications at position 3 + D-glucopyranose.
a protopanaxadiol-type ginsenoside with two glycosyl residues at position 20 + H2O = a protopanaxadiol-type ginsenoside with a single glucosyl residue at position 20 + a monosaccharide.
Ginsenosidase type IV catalyzes the sequential hydrolysis of the 6-O-beta-D-(1->2)-glycosidic bond or the 6-O-alpha-D-(1->2)-glycosidic bond in protopanaxatriol-type ginsenosides with a disacchride attached to the C6 position, followed by the hydrolysis of the remaining 6-O-beta-D-glycosidic bond (e.g. ginsenoside Re -> ginsenoside Rg1 -> ginsenoside F1).
a protopanaxatriol-type ginsenoside with two glycosyl residues at position 6 + 2 H2O = a protopanaxatriol-type ginsenoside with no glycosidic modification at position 6 + D-glucopyranose + a monosaccharide.
(20S)-ginsenoside Re + H2O = (20S)-ginsenoside Rg1 + L-rhamnopyranose.
(20S)-ginsenoside R1 + H2O = (20S)-ginsenoside Rg1 + D-xylose.
(20S)-ginsenoside Rg1 + H2O = (20S)-ginsenoside F1 + D-glucose.
The 20-O-multi-glycoside ginsenosidase catalyzes the hydrolysis of the 20-O-alpha-(1->6)-glycosidic bond and the 20-O-beta-(1->6)-glycosidic bond of protopanaxadiol-type ginsenosides.
The enzyme usually leaves a single glucosyl residue attached at position 20, although it can cleave the remaining glucosyl residue with a lower efficiency.
Starting with a ginsenoside that is glycosylated at positions 3 and 20, such as ginsenosides Rb1, Rb2, Rb3 and Rc, the most common product is ginsenoside Rd, with a low amount of ginsenoside Rg3 also formed.
(20S)-ginsenoside Rb1 + H2O = (20S)-ginsenoside Rd + D-glucose.
limit dextrin alpha-1,6-maltotetraose-hydrolase
This bacterial enzyme catalyzes a reaction similar to EC 3.2.1.33.
However, while EC 3.2.1.33 removes single glucose residues linked by 1,6-alpha-linkage, and thus requires the additional activity of EC 2.4.1.25 to act on limit dextrins formed by EC 2.4.1.1, this enzyme removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin without a need for another enzyme.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.
The enzyme, characterized from multiple bacterial species, catalyzes the hydrolysis of terminal, non-reducing D-mannose residues from beta-1,2-mannotriose and beta-1,2-mannobiose.
The mechanism involves anomeric inversion, resulting in the release of alpha-D-mannopyranose.
Activity with beta-1,2-mannotriose or higher oligosaccharides is higher than that with beta-1,2-mannobiose.
beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp + H2O = alpha-D-mannopyranose + beta-D-mannopyranosyl-(1->2)-D-mannopyranose.
The enzyme, characterized from the gut bacteria Bacteroides thetaiotaomicron and Bacteroides xylanisolvens, can also catalyze the reaction of EC 3.2.1.130.
Hydrolysis of the terminal alpha-D-mannosyl-(1->3)-alpha-D-mannose disaccharide from alpha-D-mannosyl-(1->3)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl side chains in fungal cell wall alpha-mannans.
The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, hydrolyzes terminal non-reducing alpha-sulfoquinovoside residues in alpha-sulfoquinovosyl diacylglycerides and alpha-sulfoquinovosyl glycerol.
a 6-sulfo-alpha-D-quinovosyldiacylglycerol + H2O = 6-sulfo-alpha-D-quinovose + a 1,2-diacyl-sn-glycerol.
The enzyme hydrolyzes the second glycosidic (1->4) linkage from non-reducing ends of chitin and chitodextrin molecules, liberating N,N'-diacetylchitobiose disaccharides.
Hydrolysis of N,N'-diacetylchitobiose from the non-reducing end of chitin and chitodextrins.
The enzyme hydrolyzes the second glycosidic (1->4) linkage from reducing ends of chitin and chitodextrin molecules, liberating N,N'-diacetylchitobiose disaccharides.
Hydrolysis of N,N'-diacetylchitobiose from the reducing end of chitin and chitodextrins.
The enzyme, characterized from the bacterium Vibrio furnissii, is an endo-cleaving chitodextrinase that participates in the the chitin catabolic pathway found in members of the Vibrionaceae.
Unlike EC 3.2.1.14, it has no activity on chitin.
The smallest substrate is a tetrasaccharide, and the final products are N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose.
Hydrolysis of chitodextrins, releasing N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose.
The enzyme from the acidophilic bacterium Alicyclobacillus acidocaldarius is an endo-cleaving hydrolase that cleaves beta(1->4)-linked residues.
However, it is specific for (carboxymethyl)cellulose and does not act on cellulosic substrates such as avicel.
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in (carboxymethyl)cellulose.
The enzyme, characterized from the bacteria Bacillus sp.
NRRL B-21195 and Kribbella flavida, participates in the degradation of starch.
The cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl is formed from starch extracellularly and imported into the cell, where it is degraded to glucose.
cyclobis-(1->3)-alpha-D-isomaltosyl + 2 H2O = 2 isomaltose.
The enzyme catalyzes the hydrolysis of alpha-1,6-glucosidic linkages from the non-reducing end of its substrate.
Unlike EC 3.2.1.10 the enzyme inverts the anomeric configuration of the released residue.
The enzyme can also act on panose and maltotriose at a lower rate.
H2O + isomaltose = beta-D-glucose + D-glucose.
Oleuropein is a glycosylated secoiridoid exclusively biosynthesized by members of the Oleaceae plant family where it is part of a defense system againt herbivores.
The enzyme also hydrolyzes ligstroside and demethyloleuropein.
H2O + oleuropein = D-glucose + oleuropein aglycone.
mannosyl-oligosaccharide alpha-1,3-glucosidase
This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein].
H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3).
The enzyme has been isolated from non-tuberculous mycobacteria (e.g. Mycobacterium hassiacum), which accumulate 2-O-(alpha-D-glucopyranosyl)-D-glycerate during growth under nitrogen deprivation.
(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate + D-glucose.
endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al (pmid:19181540)).
The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast.
In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation.
When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = beta-D-mannose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3).
endoplasmic reticulum Man8GlcNAc2 1,2-alpha-mannosidase
In yeast this activity is catalyzed by a dedicated enzyme that processes unfolded protein-bound Man8GlcNAc2 N-glycans within the endoplasmic reticulum to Man7GlcNAc2.
The exposed alpha-1,6-linked mannose residue in the product enables the recognition by the YOS9 lectin, targeting the proteins for degradation.
In mammalian cells this activity is part of the regular processing of N-glycosylated proteins, and is not associated with protein degradation.
H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = beta-D-mannose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 7A1,2,3B3).
poly(1,3-alpha-L-fucoside-2/4-sulfate) glycanohydrolase
The enzyme specifically hydrolyzes (1->3)-alpha-L-fucoside linkages in fucan.
Fucans are found mainly in different species of seaweed and are sulfated polysaccharides with a backbone of (1->3)-linked or alternating (1->3)- and (1->4)-linked alpha-L-fucopyranosyl residues.
In the literature, the sulfated polysaccharides are often called fucoidans.
Fucoidans include polysaccharides with a relatively low proportion of fucose and some polysaccharides that have a backbone composed of other saccharides with fucose in the branching side chains.
The sulfation of the alpha-L-fucopyranosyl residues may occur at positions 2 and 4.
The enzyme degrades fucan to sulfated alpha-L-fucooligosaccharides but neither L-fucose nor small fucooligosaccharides are produced.
endohydrolysis of (1->3)-alpha-L-fucoside linkages in fucan.
poly(1,4-alpha-L-fucoside-2/3-sulfate) glycanohydrolase
The enzyme specifically hydrolyzes (1->4)-alpha-L-fucoside linkages in fucan.
The sulfation of the alpha-L-fucopyranosyl residues may occur at positions 2 and 3.
endohydrolysis of (1->4)-alpha-L-fucoside linkages in fucan.
galactan exo-1,6-beta-galactobiohydrolase (non-reducing end)
The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyzes (1->6)-beta-galactobiose from the non-reducing terminal of (1->6)-beta-D-galactooligosaccharides with a degree of polymerization (DP) of 3 or higher, using an exo mode of action.
The enzyme cannot hydrolyze alpha-L-arabinofuranosylated (1->6)-beta-galactans (as found in arabinogalactans) and does not act on (1->3)-beta-D- or (1->4)-beta-D-galactans.
Hydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield (1->6)-beta-galactobiose as the final product.
exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)
The enzyme, characterized from the bacterium Parabacteroides distasonis, specifically hydrolyzes (1->2)-beta-D-glucooligosaccharides to sophorose.
The best substrates are the tetra- and pentasaccharides.
The enzyme is not able to cleave the trisaccharide, and activity with longer linear (1->2)-beta-D-glucans is quite low.
This enzyme acts in exo mode and is not able to hydrolyze cyclic (1->2)-beta-D-glucans.
[(1->2)-beta-D-glucosyl](n) + H2O = [(1->2)-beta-D-glucosyl](n-2) + sophorose.
blood group B branched chain alpha-1,3-galactosidase
The enzyme has exclusive specificity for the branched blood group B structures.
Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-galactosidic residues, producing free D-galactose.
blood group B linear chain alpha-1,3-galactosidase
Hydrolysis of terminal, non-reducing linear (1->3)-alpha-D-galactosidic residues, producing free D-galactose.
Differs from EC 3.2.1.17, lysozyme, as it does not hydrolyze linkages between N-acetyl-D-glucosamine residues.
Hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan.
inosine-adenosine-guanosine preferring nucleoside hydrolase
purine-specific nucleoside N-ribohydrolase
The enzyme from the bacterium Ochrobactrum anthropi specifically catalyzes the irreversible N-riboside hydrolysis of purine nucleosides.
Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD(+), NADP(+) and nicotinaminde mononucleotide are not substrates.
a purine D-ribonucleoside + H2O = a purine nucleobase + D-ribose.
H2O + inosine = D-ribose + hypoxanthine.
AMP + H2O = adenine + D-ribose 5-phosphate.
nicotinamide adenine dinucleotide glycohydrolase
nicotinamide adenine dinucleotide nucleosidase
This enzyme catalyzes the hydrolysis of NAD(+), without associated ADP-ribosyl cyclase activity (unlike the metazoan enzyme EC 3.2.2.6, bifunctional ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase).
The enzyme from Group A streptococci has been implicated in the pathogenesis of diseases such as streptococcal toxic shock-like syndrome (STSS) and necrotizing fasciitis.
The enzyme from the venom of the snake Agkistrodon acutus also catalyzes EC 3.6.1.5.
H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide.
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
This multiunctional enzyme catalyzes both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes.
In addition, the enzyme also catalyzes EC 2.4.99.20.
It is also able to act on beta-nicotinamide D-ribonucleotide.
Also hydrolyzes purine D-ribonucleosides, more slowly.
2'-, 3'- and 5'-deoxynucleosides are not substrates.
a pyrimidine ribonucleoside + H2O = a pyrimidine nucleobase + D-ribose.
S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine.
5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine.
H2O + S-methyl-5'-thioadenosine = 5-(methylsulfanyl)-D-ribose + adenine.
a pyrimidine ribonucleoside 5'-phosphate + H2O = a pyrimidine nucleobase + D-ribose 5-phosphate.
CMP + H2O = cytosine + D-ribose 5-phosphate.
H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = L-asparagine + N-acetyl-D-glucosamine.
H2O + IMP = D-ribose 5-phosphate + hypoxanthine.
1-methyladenosine + H2O = 1-methyladenine + D-ribose.
The enzyme is thought to participate in an NAD(+)-salvage pathway.
In eukaryotic organisms this activity has been attributed to EC 3.2.2.6.
beta-nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + H(+) + nicotinamide.
Hydrolyzes DNA and polynucleotides, releasing free hypoxanthine.
methylthioadenosine methylthioribohydrolase
Unlike EC 3.2.2.9, this plant enzyme has little or no activity with S-adenosyl-L-homocysteine.
Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
N(omega)-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
The enzyme will remove ADP-D-ribose from arginine residues in ADP-ribosylated proteins.
H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-ribose + L-arginyl-[protein].
H2O + N(omega)-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + L-arginine.
Hydrolysis of alkylated DNA, releasing 3-methyladenine.
Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.
Ricin A-chain and related toxins show this activity.
Naked rRNA is attacked more slowly than rRNA in intact ribosomes.
Naked rRNA from Escherichia coli is cleaved at a corresponding position.
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents.
Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
ADP-ribosyl-[dinitrogen reductase] hydrolase
dinitrogenase reductase activating glycohydrolase
The enzyme restores the activity of EC 1.18.6.1 by catalyzing the removal of ADP-ribose from an arginine residue of the dinitrogenase reductase component of nitrogenase.
This activity occurs only when the nitrogenase product, ammonium, is not available.
The combined activity of this enzyme and EC 2.4.2.37 controls the level of activity of nitrogenase.
H2O + N(omega)-alpha-(ADP-D-ribosyl)-L-arginyl-[dinitrogen reductase] = ADP-D-ribose + L-arginyl-[dinitrogen reductase].
Preferentially hydrolyzes 3- and 7-methylpurine nucleosides, such as 3-methylxanthosine, 3-methyladenosine and 7-methylguanosine.
Hydrolysis of 7-methylxanthosine to form 7-methylxanthine is the second step in the caffeine biosynthesis pathway.
7-methylxanthosine + H2O = 7-methylxanthine + D-ribose + H(+).
This enzyme, which is specific for futalosine, catalyzes the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
futalosine + H2O = dehypoxanthine futalosine + hypoxanthine.
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms.
Uracil-DNA glycosylase (EC 3.2.2.27) and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolyzing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalyzing the removal of mis-incorporated uracil from DNA.
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N(4)-ethenocytosine residue, significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing Escherichia coli.
Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil.
mismatch-specific thymine-DNA glycosylase
mismatch-specific thymine-DNA N-glycosylase
Thymine-DNA glycosylase is part of the DNA-repair machinery.
Thymine removal is fastest when it is from a G/T mismatch with a 5'-flanking C/G pair.
The glycosylase removes uracil from G/U, C/U, and T/U base pairs faster than it removes thymine from G/T.
Hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free thymine.
The enzyme, found in several bacterial species, catalyzes a step in a modified futalosine pathway for menaquinone biosynthesis.
While the enzyme from some organisms also has the activity of EC 3.2.2.9 the enzyme from Chlamydia trachomatis is specific for 6-amino-6-deoxyfutalosine.
6-amino-6-deoxyfutalosine + H2O = adenine + dehypoxanthine futalosine.
The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA.
The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity.
After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break.
In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
cytokinin riboside 5'-monophosphate phosphoribohydrolase
The enzyme, isolated from plants, is involved in the activation of cytokinins (such as N(6)-(dimethylallyl)adenine and trans-zeatin) plant hormones that are important for meristem activity.
H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-phosphate + N(6)-dimethylallyladenine.
9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin.
Thioether and trialkylsulfonium hydrolases
The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4.
H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine.
S-adenosyl-L-methionine hydrolase (L-homoserine-forming)
methylmethionine-sulfonium-salt hydrolase
Also hydrolyzes S-methyl-L-methionine to dimethyl sulfide and homoserine.
H2O + S-adenosyl-L-methionine = H(+) + L-homoserine + S-methyl-5'-thioadenosine.
2,3-dihydro-2,3-dihydroxybenzoate synthase
H2O + isochorismate = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate.
alkenylglycerophosphoethanolamine hydrolase
Lysoplasmalogenase is specific for the sn-2-deacylated (lyso) form of plasmalogen and catalyzes hydrolytic cleavage of the vinyl ether bond, releasing a fatty aldehyde and sn-glycero-3-phosphocholine or sn-glycero-3-phosphoethanolamine.
1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-saturated aldehyde + sn-glycerol 3-phosphocholine.
1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = a 2,3-saturated aldehyde + sn-glycero-3-phosphoethanolamine.
Acts on both optical isomers of the substrate.
H2O + trans-2,3-epoxysuccinate = (2R,3S)-tartrate.
A bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities.
It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates.
It also converts leukotriene A4 into leukotriene B4, unlike EC 3.2.2.10 which converts leukotriene A4 into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid.
Converts hepoxilin A3 into trioxilin A3.
Highly specific for the substrate, having only slight activity with other epoxides such as leukotriene A4 and styrene oxide.
Probably plays a modulatory role in inflammation, vascular physiology, systemic glucose metabolism and neurological function.
Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis.
The enzyme hydrolyzes several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide.
It differs from the previously described epoxide hydrolases (EC 3.3.2.4, EC 3.3.2.6, EC 3.3.2.7, EC 3.3.2.9 and EC 3.3.2.10) as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl pyrocarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline.
H2O + limonene 1,2-epoxide = limonene-1,2-diol.
This is a key hepatic enzyme that catalyzes the hydrolytic ring opening of oxiranes (epoxides) and oxetanes to give the corresponding diols.
The enzyme is involved in the metabolism of numerous substrates including the stereoselective hydrolytic ring opening of 7-oxabicyclo[4.1.0]hepta-2,4-dienes (arene oxides) to the corresponding trans-dihydrodiols.
The reaction proceeds via a triad mechanism and involves the formation of an hydroxyalkyl-enzyme intermediate.
Five epoxide-hydrolase enzymes have been identified in vertebrates to date: EC 3.3.2.6, EC 3.3.2.7, EC 3.3.2.9, EC 3.3.2.10 and EC 3.3.2.11.
cis-stilbene oxide + H2O = (1R,2R)-hydrobenzoin.
1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-yl)methyl]methanamine + H2O = 2-{[(4-methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol.
AZD1979 + H2O = AZD1979 oxetane hydrolysis product + H(+).
Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism.
It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides.
The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76.
Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate.
The enzyme can also use leukotriene A4, the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B4 as the product.
The enzyme appears to work equally well with both diastereoisomers of cholesterol 5,6-epoxide.
The product is a competitive inhibitor of the reaction.
5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5,6beta-triol.
5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5,6beta-triol.
The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyzes EC 1.17.1.7.
The enzyme from Escherichia coli also exhibits enoyl-CoA hydratase activity utilizing crotonyl-CoA as a substrate.
2-oxepin-2(3H)-ylideneacetyl-CoA + H2O = 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde.
chorismate/3,4-dihydroxycyclohexa-1,5-dienoate synthase
The enzyme found in several bacterial species is involved in the biosynthesis of macrocyclic polyketides.
chorismate + H2O = (3R,4R)-3,4-dihydroxy-3,4-dihydrobenzoate + pyruvate.
The enzyme, characterized from the bacterium Nocardioides sp. JS1661, is involved in the degradation of 2,4-dinitroanisole.
Unlike other known O-demethylases, such as EC 1.14.99.15 or EC 1.14.11.32, it does not require oxygen or electron donors, and produces methanol rather than formaldehyde.
2,4-dinitroanisole + H2O = 2,4-dinitrophenol + H(+) + methanol.
trans-2,3-dihydro-3-hydroxyanthranilic acid synthase
Isolated from the bacterium Pseudomonas aeruginosa.
(2S)-2-amino-4-deoxychorismate + H2O = (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate + pyruvate.
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.
Widely distributed in mammalian tissues.
Release of the N-terminal residue from a tripeptide.
Present in the cytosol of mammalian and microbial cells.
In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide.
The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1.
Release of N-terminal proline from a peptide.
Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds.
One of the activities of the bifunctional enzyme EC 3.3.2.6.
Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
Calcium-activated and generally membrane-bound.
Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.
Generally membrane bound enzyme present in both mammalian and bacterial cells.
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus.
Belongs to peptidase families M17 and M28.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
A secreted enzyme from Clostridium histolyticum.
Release of any N-terminal amino acid, including proline and hydroxyproline, but no cleavage of Xaa-|-Pro.
A puromycin-sensitive, cobalt-activated zinc-sialoglycoprotein that is generally cytosolic.
Multiple forms are widely distributed in mammalian tissues and body fluids.
Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.
Hydrolyzes L-lysyl-4-nitroanilide and, more slowly, L-arginyl-4-nitroanilide.
Preferentially, release of N-terminal lysine.
Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on Glu-|-Trp, Leu-|-Trp and a number of other dipeptides.
H2O + N-terminal L-tryptophanyl-L-alpha-aminoacyl-[peptide] = L-tryptophan + N-terminal L-alpha-aminoacyl-[peptide].
This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides.
The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val).
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
A thiol-dependent peptidase known from the bacterium Ochrobactrum anthropi.
Not metal dependent; probably has serine at the active center.
Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.
From the plasma fraction of chicken egg yolk.
Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyze peptides of four or five residues that contain Pro in the P1' position.
Aminoacyl-arylamides are poor substrates.
Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.
A 270-kDa protein composed of six 46.3-kDa subunits.
The pH optimum is in the alkaline range and activity is stimulated by KCl.
Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln.
In the presence of Ca(2+), the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe.
Peptides with proline in the P1' position are not substrates.
Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues.
Sphingosinicella xenopeptidilytica strain 3-2W4 is able to utilize the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu as sole carbon and energy sources.
Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids.
Icp55 removes the destabilizing N-terminal amino acid residues that are left after cleavage by the mitochondrial processing peptidase, leading to the stabilization of the substrate.
The enzyme can remove single amino acids or a short peptide, as in the case of cysteine desulfurase (EC 2.8.1.7), where three amino acids are removed.
The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.
Peptidylamino-acid hydrolases or acylamino-acid hydrolases
N(2)-(4-amino-butyryl)-L-lysine hydrolase
beta-alanyl-L-lysine + H2O = beta-alanine + L-lysine.
beta-alanyl-L-ornithine + H2O = beta-alanine + L-ornithine.
beta-alanyl-L-arginine + H2O = beta-alanine + L-arginine.
H2O + N(2)-(4-aminobutanoyl)-L-lysine = 4-aminobutanoate + L-lysine.
H2O + N(2)-(4-aminobutanoyl)-L-ornithine = 4-aminobutanoate + L-ornithine.
H2O + N(2)-(4-aminobutanoyl)-L-arginine = 4-aminobutanoate + L-arginine.
Identical with acetylhistidine deacetylase.
Hydrolysis of anserine (beta-alanyl-|-N(pi)-methyl-L-histidine), carnosine, homocarnosine, glycyl-|-leucine and other dipeptides with broad specificity.
anserine + H2O = beta-alanine + N(pros)-methyl-L-histidine.
carnosine + H2O = beta-alanine + L-histidine.
H2O + L-homocarnosine = 4-aminobutanoate + L-histidine.
It is unclear whether the specificity of this enzyme extends to other alpha-glutamyl dipeptides.
Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Escherichia coli enzyme with thiol dependence.
Hydrolysis of dipeptides containing either D- or L-amino acids or both.
Broad specificity, varying somewhat with source species.
Activated and stabilized by dithiothreitol and manganese.
Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid.
Present in the serum of humans and higher primates, but not in the serum of other mammals.
Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine.
PepE gene product (Salmonella typhimurium)
A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolyzed somewhat more slowly than dipeptides with free C-termini.
No peptide larger than a C-blocked dipeptide is known to be a substrate.
Asp-NH-Np is hydrolyzed and is a convenient substrate for routine assay.
The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride.
Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Protects Enterococcus faecium from the antibiotic vancomycin, which can bind to the -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan pentapeptide.
Reduces the availability of the free dipeptide D-Ala-D-Ala, which is the precursor for this pentapeptide sequence, allowing D-Ala-(R)-lactate (for which vancomycin has much less affinity) to be added to the cell wall instead.
The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates.
cysteinylglycine-S-conjugate dipeptidase
The enzyme participates in a widespread glutathione-mediated detoxification pathway.
In animals the activity is usually catalyzed by enzymes that have numerous additional activities, such as EC 3.4.11.1, EC 3.4.11.2 and EC 3.4.13.19.
However, in the bacterium Corynebacterium sp.Ax20, which degrades axillary secretions, the enzyme appears to be specific for this task.
an S-substituted L-cysteinylglycine + H2O = an S-substituted L-cysteine + glycine.
Dipeptidyl-peptidases and tripeptidyl-peptidases
Also polymerizes dipeptide amides, arylamides and esters at neutral pH.
Cl(-)-dependent lysosomal cysteine-type peptidase.
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
A lysosomal serine-type peptidase maximally active at acidic pH.
Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.
A cytosolic peptidase that is active at neutral pH.
It has broad activity on peptides, although it is highly selective for Arg-Arg-2-naphthylamide, at pH 9.2.
Active in the hydrolysis of enkephalins.
Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
post-proline dipeptidyl aminopeptidase IV
A membrane-bound serine-type peptidase in mammals.
EC 3.4.14.11 catalyzes a similar reaction.
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala without prior activation of the carboxy group.
Preferential release of dipeptides from a tetrapeptide, e.g. Ala-Gly-|-Ala-Gly. Acts more slowly on Ala-Ala-|-Ala-Ala and Gly-Gly-|-Gly-Gly.
A lysosomal enzyme that is active at acidic pH.
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
A cytosolic enzyme active at neutral pH.
Inhibited by diisopropyl fluorophosphate.
Release of an N-terminal tripeptide from a polypeptide.
EC 3.4.14.5 catalyzes a similar reaction.
Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease.
The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6.
The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position.
The size of the peptide does not affect the rate of reaction.
Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.
gamma-D-glutamyl-L-lysine dipeptidyl-peptidase
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the recycling of the murein peptide.
The enzyme releases L-Ala-gamma-D-Glu dipeptides from cell wall peptides via cleavage of an L-Ala-gamma-D-Glu-|-L-Lys bond.
[mycofactocin precursor peptide] peptidase
It catalyzes cleavage of the mycofactocin precursor peptide following its modification by MftC to liberate its final two residues, which consist of a cross-linked valine-tyramine dipeptide.
[mycofactocin precursor peptide]-C-terminal glycyl-N-{5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-oxopyrrolidin-3-yl}acetamide + H2O = 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one + [mycofactocin precursor peptide]-C-terminal glycine.
A glycoprotein that is generally membrane-bound.
Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline.
Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.
angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine.
A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes.
Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides.
In contrast to EC 3.4.15.1 it displays no chlorine dependence and shows no action on angiotensin I.
Conversely, peptidyl-dipeptidase a is unable to release Phe-Arg from the C-terminus of atriopeptin II.
Release of a C-terminal dipeptide or exceptionally a tripeptide.
Inhibited by captopril, as is peptidyl-dipeptidase A.
Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyze bonds in which P1' is Pro, or both P1 and P1' are Gly.
Highly specific for the branched polypeptide cyanophycin and does not hydrolyze poly-L-aspartate or poly-L-arginine.
[L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspartate.
A lysosomal peptidase active at acidic pH that inactivates angiotensin II.
Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.
serine-type D-Ala-D-Ala carboxypeptidase
A group of bacterial enzymes, membrane-bound.
Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme.
Belongs to peptidase families S11, S12 and S13.
Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Carboxypeptidases of broad specificity with optimum pH 4.5-6.0, inhibited by the action of diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents.
This enzyme is probably also identical to lysosomal tyrosine carboxypeptidase.
Release of a C-terminal amino acid with broad specificity.
Preferential release of a C-terminal arginine or lysine residue.
Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells and skeletal muscle.
Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
Isolated from cattle, pig and dogfish pancreas, and other sources, including skin fibroblasts and adrenal medulla.
Preferential release of a C-terminal lysine or arginine amino acid.
Inactivates bradykinin and anaphylatoxins in blood plasma.
Release of a C-terminal basic amino acid, preferentially lysine.
Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.
Peptide can be replaced by a pteroyl group or variety of acyl groups.
The enzyme from Corynebacterium equi also hydrolyzes N-benzoylglycine and N-benzoyl-L-aminobutyric acid.
Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups.
UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase
Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-gamma-D-glutamyl-6-carboxy-L-lysyl-D-alanine.
Competitively inhibited by penicillins and cephalosporins.
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-6-carboxy-L-lysyl-D-alanyl-|-D-alanine.
Inhibited by 1,10-phenanthroline and other chelating agents.
Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides.
Distinct from EC 3.4.17.2 and EC 3.4.17.3.
Release of C-terminal arginine or lysine residues from polypeptides.
Produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp.
Its ability to hydrolyze pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumor agent.
Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups.
A membrane-bound enzyme optimally active at neutral pH.
Distinct from EC 3.4.17.3 and EC 3.4.17.10.
Cleavage of C-terminal arginine or lysine residues from polypeptides.
Variants are known from various microorganisms.
Involved in peptidoglycan synthesis, catalyzing both decarboxylation and transpeptidation.
Stimulated by divalent cations such as magnesium and calcium, but not zinc.
Inhibited by thiol-blocking reagents, but unaffected by penicillin.
H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl.
Catalyzes carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism.
Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-|-D-alanine.
Isolated from rat pancreas but not present in cattle pancreas.
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.
One of the renal brush border exopeptidases.
Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond.
C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-tyrosine.
Releases a C-terminal residue, which may be hydrophobic or positively charged.
Release of a C-terminal amino acid with broad specificity, except for -Pro.
thrombin-activatable fibrinolysis inhibitor
Pro-carboxypeptidase U in plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.
Activity similar to that of the more stable lysine carboxypeptidase, except no preference is shown for Lys over Arg.
Release of C-terminal Arg and Lys from a polypeptide.
N-acetylated-gamma-linked-acidic dipeptidase
pteroylpoly-gamma-glutamate carboxypeptidase
Hydrolyzes alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu and folylpoly-gamma-glutamates.
With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate.
Inhibited by quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl-pentanedioate.
The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalyzed by EC 3.4.17.11 and EC 3.4.19.9.
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.
H2O + N-acetyl-L-aspartyl-L-glutamate = L-glutamate + N-acetyl-L-aspartate.
Inhibited by [(2-guanidinoethyl)sulfanyl]butanedioate.
Releases C-terminal Arg and Lys from polypeptides.
A transmembrane glycoprotein with an extracellular catalytic domain.
Angiotensin-converting enzyme 2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates.
Catalytic efficiency is 400-fold higher with angiotensin II (1-8) as a substrate than with angiotensin I (1-10).
Angiotensin-converting enzyme 2 also efficiently hydrolyzes des-Arg(9)-bradykinin, but it does not hydrolyze bradykinin.
angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine.
This is a subfamily of enzymes that cleave C-terminal and/or side chain amino acids from tubulins.
The dual-specificity enzymes can cleave both alpha- and gamma-linked L-glutamate from tubulins, removing the post-translationally added polyglutamyl side chains from the C-terminal regions.
In addition, the enzyme removes two glutamate residues from the C-terminus of beta-tubulin and detyrosinated alpha-tubulin (from which the C-terminal L-tyrosine has been removed by EC 3.4.17.17).
The latter is cleaved to Delta2-tubulin and further to Delta3-tubulin.
C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate.
C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate.
Deamidates Z-Arg-NH2, but shows no action on the arylamide derivatives.
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.
Best if P1 = Ser, Ala, Met; poor if P1 = Gly, Tyr, Asp, Asn or Pro.
Group of similar enzymes liberating N-acetyl or N-formyl amino acid from proteins and peptides.
Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides.
Display dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of misrecognition of the glycyl residue as an uncharged N-acyl group.
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
Inactivates vasopressin and oxytocin by splitting off glycinamide.
Also cleaves ester substrates of trypsin and chymotrypsin.
Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide.
The toad skin enzyme is inhibited by diisopropyl fluorophosphate.
Cleavage of C-terminal glycinamide from polypeptides.
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Other isopeptide bonds, e.g. gamma-glutamyl and beta-alanyl, are not hydrolyzed.
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
thyrotropin-releasing hormone degrading ectoenzyme
Highly specific for thyrotropin releasing hormone (pyroglutamyl-histidyl-prolylamide).
Will not cleave the pyroglutamyl-histidyl bond of luteinizing hormone releasing hormone.
Release of the N-terminal pyroglutamyl group from pGlu-|-His-Xaa tripeptides and pGlu-|-His-Xaa-Gly tetrapeptides.
Highly specific for N-formylmethionyl-peptides.
Will not cleave methionyl peptides or N-formyl derivatives of amino acids other than methionine.
Inhibited by heavy metals and activated by chloride.
Release of an N-terminal, formyl-methionyl residue from a polypeptide.
lysosomal gamma-glutamyl carboxypeptidase
tetrahydropteroyl-poly-gamma-glutamyl gamma-glutamyl hydrolase
The enzyme, which occurs only in animals and plants, can be either endo- and/or exopeptidase.
It acts on tetrahydropteroyl polyglutamates and their modified forms, as well as the polyglutamates of the folate breakdown product N-(4-aminobenzoyl)-L-glutamate (pABA-Glu).
The initial cleavage may release either monoglutamate or poly-gamma-glutamate of two or more residues, depending on the specific enzyme.
For example, GGH1 from the plant Arabidopsis thaliana cleaves pentaglutamates, mainly to di- and triglutamates, whereas GGH2 from the same organism yields mainly monoglutamates.
The enzyme is lysosomal (and secreted) in animals and vacuolar in plants.
(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate.
gamma-D-glutamyl-meso-diaminopimelate peptidase
gamma-D-glutamyl-L-diamino acid endopeptidase I
gamma-D-glutamyl-meso-diaminopimelate peptidase I
Metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall.
Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted.
Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides.
Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals.
Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde).
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
This is a bifunctional protein that also has the activity of EC 2.3.2.2.
The enzyme binds its substrate by forming an initial gamma-glutamyl-enzyme intermediate, releasing the L-cysteinylglycine part of the molecule.
The enzyme then reacts with either a water molecule or a different acceptor substrate (usually an L-amino acid or a dipeptide) to form L-glutamate or a product containing a new gamma-glutamyl isopeptide bond, respectively.
The enzyme acts on glutathione, glutathione-S-conjugates, and, at a lower level, on other substrates with an N-terminal L-gamma-glutamyl residue.
It plays a crucial part in the glutathione-mediated xenobiotic detoxification pathway.
glutathione + H2O = L-cysteinylglycine + L-glutamate.
an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate.
The mouse enzyme is specific for leukotriene C4, while the human enzyme also has considerable activity toward glutathione and oxidized glutathione (cf. EC 3.4.19.13).
H2O + leukotriene C4 = L-glutamate + leukotriene D4.
SAMP-protein conjugate cleaving protease
The enzyme, characterized from the archaeon Haloferax volcanii, specifically cleaves the ubiquitin-like small modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein.
an N(6)-[small archaeal modifier protein]-[protein]-L-lysine + H2O = a [protein]-L-lysine + a [small archaeal modifier protein].
This enzyme, characterized from the plant Arabidopsis thaliana, participates in the biosynthesis of the plant defense compounds glucosinolates and camalexin.
It is the only known plant enzyme capable of hydrolyzing the gamma-glutamyl residue of glutathione in the cytosol.
an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-glutathione + H2O = an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-cysteinylglycine + L-glutamate.
(E)-1-(glutathione-S-yl)-2-(1H-indol-3-yl)acetohydroximate + H2O = (E)-1-(glycyl-L-cystein-S-yl)-2-(1H-indol-3-yl)acetohydroximate + L-glutamate.
2-(glutathion-S-yl)-2-(1H-indol-3-yl)acetonitrile + H2O = 2-(glycyl-L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + L-glutamate.
(Z)-1-(glutathione-S-yl)-2-phenylacetohydroximate + H2O = (Z)-1-(glycyl-L-cystein-S-yl)-2-phenylacetohydroximate + L-glutamate.
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Reacts more readily with Tos-Leu-CH2Cl than Tos-Phe-CH2Cl, in contrast to chymotrypsin.
Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa.
Digestive enzyme from the sea anemone Metridium senile.
Preferential cleavage: Tyr-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. Little action on Trp-|-Xaa.
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
More selective than trypsin and plasmin.
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
A blood coagulation factor formed from the proenzyme factor X by limited proteolysis.
Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds.
The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca(2+) and phospholipids.
Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va.
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Formed from plasminogen by proteolysis which results in multiple forms of the active plasmin.
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
Not inhibited by protein inhibitors of trypsin.
Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.
Inhibited by naturally occurring trypsin inhibitors.
Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.
In appropriate buffer the specificity is restricted to Glu-|-Xaa.
Bonds involving bulky side-chains of hydrophobic amino acids are cleaved at a lower rate.
Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
From azurophil granules of polymorphonuclear leukocytes.
The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human.
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
The proenzyme factor IX is activated by EC 3.4.21.27.
From the sarcocarp of the musk melon (Cucumis melo).
Other endopeptidases from plants, which are less well characterized but presumably of serine-type, include euphorbain from Euphorbia cerifera, solanain from horse-nettle Solanum elaeagnifolium, hurain from Hura crepitans and tabernamontanain from Tabernamontana grandiflora.
Hydrolysis of proteins with broad specificity.
Found in vertebrates, plants and Flavobacterium.
Generally cytosolic, commonly activated by thiol compounds.
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
The proenzyme XI is activated by EC 3.4.21.38.
Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.
From hepatopancreas of the fiddler crab (Uca pugilator).
Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidase from U.pugilator, digestive enzymes from other decapod crustacea, and an enzyme from the fungus Entomophthora coronata.
Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.
Formed from plasma prokallikrein (Fletcher factor) by factor XIIa.
Activates coagulation factors XII, VII and plasminogen.
Selective for Arg > Lys in P1, in small molecule substrates.
Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.
Formed from tissue prokallikrein by activation with trypsin.
A large number of tissue kallikrein-related sequences have been reported for rats and mice, though fewer seem to exist in other mammals.
The few that have been isolated and tested on substrates include mouse EC 3.4.21.54, submandibular proteinase a, epidermal growth-factor-binding protein, nerve growth factor gamma-subunit, rat tonin, submaxillary proteinases A and B, T-kininogenase, kallikreins K7 and K8.
The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|-Xaa bonds.
Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.
Formed by activation of proelastase from mammalian pancreas by trypsin.
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.
Differs from pancreatic elastase in specificity on synthetic substrates and in inhibitor sensitivity.
Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.
Also activates plasma prekallikrein and plasminogen.
Formed from the proenzyme, factor XII, by plasma kallikrein or factor XIIa.
Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.
Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.
Activates C1s by proteolytic cleavage so that it can, in turn, activate C2 and C4.
Activated from proenzyme C1r in plasma by autocatalytic mechanism during activation of the complement system by the 'classical' route.
Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).
Activated from proenzyme C1s in plasma by the activated complement subcomponent C1r.
Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.
classical-complement-pathway C3/C5 convertase
A complex of complement fragments C4b, C2a and C2b.
Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.
Cleavage of complement subcomponent C3b requires its binding to cofactor H or complement receptor CR1; cleavage of iC3b requires complement receptor CR1; cleavage of C4b requires C4b-binding protein.
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.
A component of the alternative pathway of complement activation.
This reaction is analogous to the activation of complement component C2 by activated complement subcomponent C1s.
Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.
alternative-complement-pathway C3/C5 convertase
complement component C3/C5 convertase (alternative)
A bimolecular complex of complement fragment Bb with either C3b or cobra venom factor; Bb contains the active site.
Bb is formed by cleavage of proenzyme factor B by factor D.
Cleavage of complement component C5 requires additional C3b which binds C5 and renders it susceptible to cleavage by C3b,Bb complex.
C3b,Bb is stabilized in plasma by factor P.
Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b.
Contains a Cys residue near the active site His, and is inhibited by mercurials.
Proteinase ycaB is a similar enzyme from the yeast Candida albicans.
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
Little action on small molecule substrates of trypsin, chymotrypsin, elastase or microbial collagenases.
Hydrolysis of proteins including native collagen at Xaa-|-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment.
Enzymes with similar specificity are produced by Lysobacter enzymogenes (endoproteinase Lys-C) and Pseudomonas aeruginosa (Ps-1).
Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.
ATP hydrolysis is linked with peptide bond hydrolysis.
A similar enzyme occurs in animal mitochondria.
Hydrolysis of proteins in presence of ATP.
Unlike EC 3.4.23.15, does not act on natural angiotensinogen.
A member of the tissue kallikrein family, from submandibular glands of male mice.
Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide renin substrate, to produce angiotensin I, but not active on natural angiotensinogen. Also hydrolyzes Bz-Arg-p-nitroanilide.
From the venom of the Gaboon viper Bitis gabonica.
Not inhibited by antithrombin III/heparin or hirudin, unlike EC 3.4.21.5.
Preferential cleavage: Arg-|-Xaa bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
The enzyme from spinach leaves shows high specificity for leucine in peptides and 4-nitroanilides.
Hydrolysis of proteins. Preferential cleavage: Leu-|-Xaa in small molecule substrates.
Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules.
Not inhibited by alpha-1-proteinase inhibitor of alpha-2-macroglobulin.
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.
From the venom of the Taipan snake (Oxyuranus scutellatus).
Specificity is similar to that of Factor Xa (EC 3.4.21.6).
However, unlike Factor Xa this enzyme can cleave its target in the absence of coagulation Factor Va.
Activity is potentiated by phospholipid and Ca(2+) which binds via gamma-carboxyglutamic acid residues.
Similar enzymes are known from the venom of other Australian elapid snakes, including Pseudonaja textilis textilis, Oxyuranus microlepidotus and Demansia nuchalis affinis.
Selective cleavage of Arg-|-Thr and Arg-|-Ile in prothrombin to form thrombin and two inactive fragments.
Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors.
Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin.
It contains no cysteine residues (although these are found in homologous enzymes).
Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo).
Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species.
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.
Identical or closely related enzymes are produced by A.flavus and A.sojae.
From the mold Tritirachium album Limber.
Contains two disulfide bridges and one free Cys near the active site His.
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.
From the thermophilic fungus Malbranchea pulchella var. sulfurea.
Contains Cys, but not inhibited by p-mercuribenzoate.
Rather non-specific hydrolysis of proteins. Preferential cleavage: -Ala-|-Xaa-, -Tyr-|-Xaa-, -Phe-|-Xaa- in small molecular substrates.
thermophilic Streptomyces serine protease
From Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate.
The N-terminal extension of the polypeptide chain relative to subtilisin contributes to calcium-binding and the high thermostability.
The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus are closely similar.
Hydrolysis of proteins, including collagen.
Inhibited by Tos-Phe-CH2Cl, but not by Tos-Lys-CH2Cl.
Hydrolysis of proteins, but not Bz-Tyr-OEt, Ac-Phe-beta-naphthylester, or Bz-Arg-OEt.
From a wide variety of mammalian tissues, especially endothelial cells.
Secreted as a single chain precursor which is cleaved to a two-chain form by plasmin.
Activity is considerably enhanced by fibrin.
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
One of the gamma-carboxyglutamic acid-containing coagulation factors.
Formed from protein C, the proenzyme that circulates in plasma, by the action of a complex of thrombin with thrombomodulin, or by serine endopeptidases present in several snake venoms.
Degradation of blood coagulation factors Va and VIIIa.
Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.
Formed by activation of proelastase II from mammalian pancreas by trypsin.
Usually, only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species; human pancreatic elastase is of type II.
Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.
Species variants differing slightly in specificity are secreted by Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus influenzae.
Some other bacterial endopeptidases with similar specificity are of metallotype (see EC 3.4.24.13).
Cleavage of immunoglobulin A molecules at certain Pro-|-Xaa bonds in the hinge region. No small molecule substrates are known.
Formed from the inactive precursor by action of plasmin or plasma kallikrein.
Differs in structure from EC 3.4.21.68, and does not bind to fibrin.
A somewhat thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group.
Species variants of the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit viper), batroxobin from Bothrops atrox (South American pit viper) and crotalase from Crotalus adamanteus (Eastern diamondback rattlesnake).
Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.
paired basic amino acid residue cleaving enzyme
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
Not inhibited by secretory leukocyte proteinase inhibitor.
Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.
Slowly inhibited by alpha-1-antichymotrypsin.
The human enzyme does not cleave Phe-|-Xaa.
Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.
Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.
Not inhibited by Tos-Phe-CH2Cl or ovomucoid.
Hydrolysis of proteins with specificity similar to chymotrypsin.
Hydrolysis of proteins with trypsin-like specificity.
Inhibited by (18-Leu->Glu) modified turkey ovomucoid third domain.
Preferential cleavage: -Glu-|-Xaa- >> -Asp-|-Xaa-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-|-Asp- and -Glu-|-Pro- bonds is slow.
Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline.
From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus.
Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin.
Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates.
Selective cleavage of 98-Arg-|-Ile-99 bond in Limulus proclotting enzyme to form active clotting enzyme.
Limulus clotting enzyme is activated by factor B.
Selective cleavage of 18-Arg-|- and 47-Arg-|- bonds in coagulogen to form coagulin and fragments.
In the presence of single-stranded DNA, the RecA protein interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
The activity was previously attributed to the RecA protein (formerly EC 3.4.99.37).
Hydrolysis of Ala-|-Gly bond in repressor LexA.
Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity.
Cleaves a single bond -Ala-|-Ala- in M13 phage procoat protein, producing free signal peptide and coat protein.
Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane.
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Once released, the core protein does not retain catalytic activity.
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
A calcium dependent enzyme, maximally active at about pH 5.5.
Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin.
Unlike prohormone convertase 2, does not cleave proluteinizing-hormone-releasing hormone.
Usually processing of prodynorphin occurs at a bond in which P2 is Thr.
Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 2.
Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
Specificity is broader than that of prohormone convertase 1.
Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proinsulin and proluteinizing-hormone-releasing hormone.
Unlike prohormone convertase 1, does not cleave prorenin or prosomatostatin.
Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 1.
Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2.
lactococcal cell envelope-associated proteinase
Responsible for the hydrolysis of casein in milk and the provision of peptides essential for cell growth.
Specificity differences between lactocepins from different starter strains may be partly responsible for imparating different flavor qualities to cheese.
Endopeptidase activity with very broad specificity, although some subsite preference have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyze hemoglobin and oxidized insulin B-chain.
Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion.
Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins.
The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein.
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
The enzyme from the ascidian (Prochordate) Halocynthia roretzi is localized in the sperm head, and released during sperm activation.
A proline-rich region is involved in binding to the vitelline coat of the egg.
Hydrolyzes arginyl bonds, preferably with Pro in the P2 position.
Pseudomonas sp. pepstatin-insensitive carboxyl proteinase
An enzyme secreted by Pseudomonas sp. No. 101.
It is distinguished from EC 3.4.21.101 by its insensitivity to EPNP and from EC 3.4.23.31 by this property and by its unrelated amino-acid sequence.
Inhibited by tyrostatin, a peptide aldehyde.
Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO2)-Arg-Leu.
Secreted by the bacterium Xanthomonas sp.
photosystem II D1 protein processing peptidase
In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II; this proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.
The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.
Dictyostelium discoideum aspartic proteinase
Dictyostelium discoideum aspartic proteinase E
From the slime mold Physarum polycephalum.
Is not inhibited by pepstatin, but is blocked by methyl 2-diazoacetamidohexanoate.
Closely similar enzymes are found in Dictyostelium discoideum and P.flavicomum.
Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)2.
mannan-binding lectin-associated serine protease-2
mannan-binding lectin-associated serine peptidase 2
mannose-binding lectin-associated serine protease-2
Mannan-binding lectin (MBL) recognizes patterns of neutral carbohydrates, such as mannose and N-acetylglucosamine, on a wide range of microbial surfaces and is able to initiate activation of the lectin pathway of complement.
Displays C1s-like esterolytic activity (cf. EC 3.4.21.42).
It also cleaves C4 and C2 with efficiencies that are relatively higher than those of EC 3.4.21.42.
Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).
These endopeptidases are multi-spanning membrane proteins.
Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains.
Important for embryo development in Drosophila melanogaster.
Rhomboid is a key regulator of EGF receptor signaling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway.
Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
This type-II membrane-associated serine peptidase has been implicated in cell growth and development.
The enzyme has been shown to activate blood coagulation factor VII by cleavage of the 152-Arg-|-Ile-153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation.
There is no cleavage after aromatic or aliphatic residues.
The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue.
The nature of the residue at S3 also affects hydrolysis, with Gln being much more favorable than Ala.
Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.
This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli.
Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli.
The enzyme has weak peptidase activity with casein and other non-native substrates.
The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures.
Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding.
They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding.
If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme.
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.
Up-regulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment.
Can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP).
Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.
tumor-associated differentially-expressed gene 15 protein
This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis.
Can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active alpha- and beta-HGF, but it does not activate plasminogen, which shares high homology with HGF.
The enzyme can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade.
Hemojuvelin has been shown to be a physiologic substrate for matriptase-2.
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position.
Surface-associated subtilisin-like serine peptidase with very specific substrate specificity.
Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a.
Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties.
The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59.
This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase.
It has three subsites, S1, S2, and S3, in the substrate binding site.
The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile.
These specificities are similar to those of EC 3.4.21.62 and EC 3.4.21.64.
The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyzes elastin substrates such as succinyl-(Ala)n-p-nitroanilide (n = 1,2,3) and some peptide esters.
Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.
membrane-bound transcription factor site-1 protease
sterol regulatory element-binding protein proteinase
sterol regulatory element-binding protein site 1 protease
Cleaves sterol regulatory element-binding proteins (SREBPs) and thereby initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholesterol and unsaturated fatty acids into the bloodstream.
The enzyme also processes pro-brain-derived neurotrophic factor and undergoes autocatalytic activation in the endoplasmic reticulum through sequential cleavages.
The enzyme can also process the unfolded protein response stress factor ATF6 at an Arg-His-Lys-Lys-|- site, and the envelope glycoprotein of the highly infectious Lassa virus and Crimean Congo hemorrhagic fever virus at Arg-Arg-Lys-Lys-|-.
Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3.
bovine viral diarrhea virus NS3 endopeptidase
classical swine fever virus NS3 endopeptidase
The polyprotein of noncytopathogenic pestiviruses is cleaved co- and post-translationally into at least 11 proteins (N(pro), C, E(rns), E1, E2, p7, NS2-3, NS4A, NS4B, NS5A, and NS5B).
The genomes of cytopathogenic pestivirus strains express at least one additional protein, called NS3 (p80).
This enzyme, which resides in the N-terminal region of NS3 (non-structural protein 3), is essential for generation of its own C-terminus and for processing of the downstream cleavage sites, leading to the release of the pestivirus non-structural proteins NS4A, NS4B, NS5A and NS5B.
Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.
chymotrypsin-like serine proteinase nsp4
non-structural protein 4 serine protease
In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins.
This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield non-structural proteins (nsp5-nsp12).
It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position.
Cleavage of ORF1ab by this enzyme is essential for viral replication.
Cleavage of (Glu/Gln)-|-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab.
infectious pancreatic necrosis birnavirus Vp4 peptidase
infectious pancreatic necrosis virus protease
Infectious pancreatic necrosis virus (IPNV) is a birnavirus that causes an acute, contagious disease in young salmonid fish.
As with most viruses that infect eukaryotic cells, the proteolytic processing of viral precursor proteins is a crucial step in the life cycle of this virus.
pVP2 is converted into VP2 by cleavage near the carboxy end of pVP2; this cleavage is most likely due to host-cell proteases rather than VP4.
Differs from most serine peptidases in not having the catalytic triad Ser-His-Asp.
Cleaves the (Ser/Thr)-Xaa-Ala-|-(Ser/Ala)-Gly motif in the polyprotein NH2-pVP2-VP4-VP3-COOH of infectious pancreatic necrosis virus at the pVP2-VP4 and VP4-VP3 junctions.
This enzyme plays a central role in a regulatory checkpoint (the sigma(K) checkpoint), which coordinates gene expression during the later stages of spore formation in Bacillus subtilis.
The enzyme activates proteolytic processing of a sporulation-specific sigma factor, pro-sigma(K), to its mature and active form, sigma(K), by self-cleavage.
The enzyme is also subject to secondary proteolysis, which presumably inactivates SpoIVB.
The enzyme is also essential for the formation of heat-resistant spores.
Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-Thr-75 at the N-terminus of SpoIVB.
This enzyme has wide substrate specificity, being able to degrade heat-denatured bovine casein and the alpha-chain of native human fibrinogen.
It cleaves the B chain of bovine insulin at 6-Leu-|-Cya-7 (cysteic acid), 16-Tyr-|-Leu-17, 25-Phe-|-Tyr-26 and 26-Tyr-|-Thr-27.
It is thought to play a role in the desquamation (skin-shedding) of the outer layer of skin, the stratum corneum, by degrading intercellular cohesive structures.
Cleavage of proteins with aromatic side chains in the P1 position.
tumor-associated differentially expressed gene 14
Activated by removal of an N-terminal prepropeptide.
The highest amidolytic activity is observed using Boc-Val-Pro-Arg-|-7-amido-4-methylcoumarin, which is a substrate of alpha-thrombin.
Substrates lacking basic amino acids in the P1 position are not cleaved.
Degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease.
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.
epidermal growth factor-binding protein type B
Specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates.
Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used.
Also able to process pro-interleukin-1beta (pro-IL-1beta) in mouse submandibular gland to form IL-1beta.
Hydrolyzes mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin.
The egg envelope of Xenopus laevis is modified during transit of the egg through the pars rectus oviduct, changing the egg envelope from an unfertilizable form to a fertilizable form.
This process involves the conversion of glycoprotein gp43 to gp41 (ZPC) by the pars recta protease oviductin.
It is thought that the enzymatically active protease molecule comprises the N-terminal protease domain coupled to two C-terminal CUB domains, which are related to the mammalian spermadhesin molecules implicated in mediating sperm-envelope interactions.
Preferential cleavage at 371-Gly-Ser-Arg-|-Trp-374 of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41.
The enzyme is a serine peptidase, which has been shown to cleave prothrombin and prekallikrein.
It hydrolyzes the complement component C5 releasing complement component C5a.
Cleavage of -Lys-Lys-|-Xaa and -Lys-Arg-|-Xaa bonds.
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
From latex of the papaya (Carica papaya).
Inhibited by compound E-64 and proteins of the cystatin family.
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.
The major proteolytic component of the latex of fig, Ficus glabrata.
Cysteine endopeptidases with similar properties are present in other members of the large genus Ficus.
The major endopeptidase of papaya (Carica papaya) latex.
From the latex of milkweed, Asclepias syriaca.
From the bacterium Clostridium histolyticum.
Activated by calcium; inhibited by EDTA.
Preferential cleavage: Arg-|-Xaa, including Arg-|-Pro bond, but not Lys-|-Xaa.
From the bacterium, group A Streptococcus.
Formed from the proenzyme by limited proteolysis.
Preferential cleavage with hydrophobic residues at P2, P1 and P1'.
From the kiwi fruit or Chinese gooseberry (Actinidia chinensis).
A lysosomal enzyme that is readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64.
Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
N-benzoylarginine-beta-naphthylamide hydrolase
Present in lysosomes of mammalian cells.
Because of the combination of endopeptidase and aminopeptidase activity it can be considered as 'endoaminopeptidase'.
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.
Degrades azocasein and denatured hemoglobin; the only native protein on which it has been shown to act is EC 2.6.1.5.
Interconversion of the three forms of EC 2.6.1.5.
Not inhibited by chicken cystatin, unlike most other homologs of papain.
Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.
Apparently produced only by malignant and fetal cells.
Specific cleavage of Arg-|-Ile bond in Factor X to form Factor Xa.
A lysosomal cysteine endopeptidase that is unusual among such enzymes for its stability to neutral pH.
Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.
From entero-, rhino-, aphto- and cardioviruses.
Larger than the homologous virus picornain 2A.
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Smaller than the homologous virus picornain 3C.
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain.
From stem of pineapple plant, Ananas comosus.
Differs from stem and fruit bromelains in being inhibited by chicken cystatin.
Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-|-NHMec, but broader specificity than fruit bromelain.
The most abundant of cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus.
Distinct from the bromelain found in the pineapple fruit (EC 3.4.22.33).
Scarcely inhibited by chicken cystatin and also very slowly inactivated by E-64.
Broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-|-NHMec among small molecule substrates.
From the pineapple plant, Ananas comosus.
Another cysteine endopeptidase, with similar action on small molecule substrates, pinguinain (formerly EC 3.4.99.18), is obtained from the related plant, Bromelia pinguin, but pinguinain differs from fruit bromelain in being inhibited by chicken cystatin.
Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg-|-NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-|-NHMec (cf. stem bromelain).
Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes.
Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
From the protozoan, Entamoeba histolytica.
Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|-Xaa in small molecule substrates including Z-Arg-Arg-|-NHMec.
interleukin 1beta-converting endopeptidase
Part of the family of inflammatory-caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice.
Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation.
Cleaves pro-interleukin-1beta (pro-IL-1beta) to form mature IL-1beta, a potent mediator of inflammation.
Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor.
Caspase-11 plays a critical role in the activation of caspase-1 in mice whereas caspase-4 enhances its activation in humans.
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
Strongly activated by glycine and stabilized by calcium.
Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1.
Prominently expressed in mammalian osteoclasts, and believed to play a role in bone resorption.
Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.
A cysteine endopeptidase from adenoviruses.
Activity is greatly stimulated by the binding to the enzyme of an 11-residue peptide from the adenovirus capsid protein pre-VI at a site separate from the active site.
Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).
The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain.
Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity.
Known from bacteria as well as eukaryotic organisms.
Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyzes Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates.
Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred.
The enzyme is unstable at neutral pH values and is inhibited by compound E-64.
The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (kcat/Km) comparable to that of cathepsin L.
The recombinant human enzyme is catalytically active at pH 6.0 and is inhibited by compound E-64.
The recombinant human enzyme hydrolyzes synthetic endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec.
Maximally active at pH 5.7 and unstable at neutral pH.
Compound E-64, leupeptin and chicken cystatin are inhibitors.
The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).
The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei, protein a of these being the endopeptidase.
The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage.
It is also reported that transgenic plants expressing the enzyme are resistant to viral infection.
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities.
The N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity.
Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses.
Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue.
The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
Known from the bacterium Porphyromonas gingivalis and contributes to the pathogenicity of the organism.
Endopeptidase with strict specificity for lysyl bonds.
Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate.
In both Saccharomyces cerevisiae and human cells, cleavage of the cohesin subunit Scc1 by separase is required for sister chromatid separation in mitosis.
S.cerevisiae separase is also known to cleave the Rec8 subunit of a meiotic cohesin complex and the kinetochore protein Slk19.
All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.
Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus.
Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
Is located in the digestive vacuoles of the parasitic trypanosome and contributes to the nutrition of the organism by digestion of host proteins.
Broad endopeptidase specificity similar to that of cathepsin L.
The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.53.
The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52.
muscle-specific calcium-activated neutral protease 3
Activated by autoproteolytic cleavage of insertion sequence 1 (IS1), which allows substrates and inhibitors gain access to the active site.
Substrates include the protein itself and connectin/titin.
neural precursor cell expressed developmentally down-regulated protein 2
Caspase-2 is an initiator caspase, as are caspases-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63).
Two forms of caspase-2 exist that have antagonistic effects: caspase-2L induces programed cell death and caspase-2S suppresses cell death.
Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease.
Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments.
Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide.
Apart from itself, the enzyme can cleave golgin-16, which is present in the Golgi complex and has a cleavage site that is unique for caspase-2.
alphaII-spectrin, a component of the membrane cytoskeleton, is a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S).
Strict requirement for an Asp residue at P1, with 316-Asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.
Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60).
These caspases are responsible for the proteolysis of the majority of cellular polypeptides, [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype.
Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B.
Caspase-3 can activate procaspase-2 (EC 3.4.22.55).
Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain.
While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate.
Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a better substrate than Asp-Val-Ala-Asp-|-.
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
Part of the family of inflammatory-caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice.
Able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1beta (IL-1beta) from pro-IL-1beta.
Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17).
The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly.
Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.
This enzyme is part of the family of inflammatory-caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice.
The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1beta (IL-1beta) from pro-IL-1beta.
Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17).
Unlike caspase-4, this enzyme can be induced by lipopolysaccharide.
Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60).
These caspases are responsible for the proteolysis of the majority of cellular polypeptides, [e.g. poly(ADP-ribose) polymerase (PARP)], which lead to the apoptotic phenotype.
Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to cytochrome c release from the mitochondria; the release of cytochrome c, which is an essential component of the intrinsic apoptosis pathway.
Can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragementation in the final phases of apoptosis.
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.
Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59).
Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect.
Caspase-7 is activated by the initiator caspases [caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)].
Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits.
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63).
Apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation.
Contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation.
Linked to cell surface death receptors such as Fas.
When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated.
Has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala at the P1' position.
Has very broad P4 specificity, tolerating substrates with Asp, Val or Leu in this position.
Endogenous substrates for caspase-8 include procaspase-3, the pro-apoptotic Bcl-2 family member Bid, RIP, PAK2 and the caspase-8 activity modulator FLIPL.
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala).
Caspase-9 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63).
An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2.
Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo.
The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage.
Procaspase-3 is the enzyme's physiological substrate.
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.
FAS-associated death domain protein interleukin-1beta-converting enzyme 2
Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62).
Like caspase-8, it contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation.
Has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-kappaB survival signaling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation).
Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at Lys-Gln-Thr-Asp-|- to yield the pro-apoptotic p15 fragment.
The p15 fragment is N-myristoylated and enhances cytochrome c release from mitochondria (which initiatiates the intrinsic apoptosis pathway).
Bid can be further cleaved by caspase-10 and granzyme B but not by caspase-3 and caspase-8 at Ile-Glu-Thr-Asp-|- to yield a p13 fragment that is not N-myristoylated.
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly.
Part of the family of inflammatory-caspases, which also includes caspase-1 (EC 3.4.22.36), caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-12, caspase-13 and caspase-14 in mice.
Like caspase-5, but unlike caspase-4, this enzyme can be induced by lipopolysaccharide.
Not only activates caspase-1, which is required for the maturation of proinflammatory cytokines such as interleukin-1beta (IL-1beta) and IL-18, but it also activates caspase-3 (EC 3.4.22.56), which leads to cellular apoptosis under pathological conditions.
Strict requirement for Asp at the P1 position and has a preferred cleavage sequence of (Ile/Leu/Val/Phe)-Gly-His-Asp-|-.
This enzyme, derived from the house dust mite, is a major component of the allergic immune response.
The substrate specificity of this enzyme is not altogether clear; it cleaves the low-affinity IgE receptor CD23 at 298-Glu-|-Ser-299 and 155-Ser-|-Ser-156.
It also cleaves the pulmonary structural proteins occludin and claudin at Leu-|-Leu, Asp-|-Leu and at Gly-|-Thr bonds, and it can also cleave the alpha subunit of the interleukin-2 (IL-2) receptor (CD25).
Using a positional scanning combinatorial library, it was found that the major substrate-specificity determinant is for Ala in the P2 position.
The enzyme shows only a slight preference for basic amino acids in the P1 and P3 positions and a preference for aliphatic amino acids such as Ile, Pro, Val, Leu and norleucine in the P4 position.
calicivirus trypsin-like cysteine protease
rabbit hemorrhagic disease virus 3C endopeptidase
Viruses that are members of the Norovirus genus (Caliciviridae family) are a major cause of epidemic acute viral gastroenteritis.
The non-structural proteins of these viruses are produced by proteolytic cleavage of a large precursor polyprotein, performed by a protease that is incorporated into the polyprotein.
Cleavage sites are apparently defined by features based on both sequence and structure since several sites in the polyprotein fulfilling the identified sequence requirements are not cleaved.
The presence of acidic (Asp), basic (Arg), aromatic (Tyr) or aliphatic (Leu) amino acids at the P1' position results in only minor differences in cleavage efficiency, suggesting that steric or conformational constraints may play a role in determining specificity.
Changes to the amino acid at the P2 position do not alter cleavage efficiency.
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.
Found in ginger (Zingiber officinale) rhizome and is a member of the papain family.
The enzyme is inhibited by some divalent metal ions, such as Hg(2+), Cu(2+), Cd(2+) and Zn(2+).
Preferential cleavage of peptides with a proline residue at the P2 position.
The enzyme from Saccharomyces cerevisiae can also recognize small ubiquitin-like modifier 1 (SUMO-1) from human as a substrate in both SUMO-processing (alpha-linked peptide bonds) and SUMO-deconjugation (epsilon-linked peptide bonds) reactions.
Ulp1 has several functions, including an essential role in chromosomal segregation and progression of the cell cycle through the G2/M phase of the cell cycle.
Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
severe acute respiratory syndrome coronavirus main protease
SARS coronavirus main protease is the key enzyme in SARS coronavirus replicase polyprotein processing.
TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.
The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a NPXTN motif is cleaved between the Thr and Asn residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.
The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis.
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
Degradation of gelatin, little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A. Does not cleave 1-Phe-|-Val-2, 4-Gln-|-His-5 or 23-Gly-|-Phe-24.
Formed from progastricsin, apparently in the gastric juice of most vertebrates.
In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum.
Seminal plasma contains a zymogen that is immunologically identical with progastricsin.
More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.
Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin.
Found among mammals with postnatal uptake of immunoglobins.
Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of casein.
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
From the insectivorous plants Nepenthes sp. (secretions) and Drosera peltata (ground-up leaves).
Aspartic endopeptidases are probably present in many other plants, including lotus and sorghum.
Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg.
Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
human immunodeficiency virus type 1 protease
Present in human immunodeficiency virus type 1.
Contributes to the maturation of the viral particle, and is a target of antiviral drugs.
Active enzyme is a dimer of identical 11-kDa subunits.
Similar enzymes occur in other retroviruses.
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
A 70 kDa membrane-bound enzyme isolated from cattle pituitary secretory vesicle.
Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side.
Found in a variety of Aspergillus species (imperfect fungi): A.awamori, A.foetidus, A.fumigatus, A.kawachii, A.niger, A.oryzae, A.saitoi, and A.sojae.
Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.
Aspergillus niger var. macrosporus aspartic proteinase
Isolated from Aspergillus niger var. macrosporus, distinct from aspergillopepsin I in specificity and insensitivity to pepstatin.
Preferential cleavage in B chain of insulin: 3-Asn-|-Gln-4, 13-Gly-|-Ala-14, and 26-Tyr-|-Thr-27.
Penicillium janthinellum aspartic protease
From the imperfect fungus Penicillium janthinellum.
Closely related enzymes have been isolated from P.roqueforti and P.duponti.
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
From the zygomycete fungi Rhizopus chinensis and R.niveus.
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.
From the ascomycete Endothia parasitica.
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
Isolated from the zygomycete fungi Mucor pusillus and M.miehei.
Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen.
This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamido-hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane.
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
From the imperfect yeast Rhodotorula glutinis.
Somewhat similar enzymes have been isolated from the imperfect yeast-like organism Cladosporium sp. and the imperfect fungus Paecilomyces varioti.
Specificity similar to that of pepsin A. Cleaves Z-Lys-|-Ala-Ala-Ala and activates trypsinogen.
From the imperfect fungus Acrocylindrium sp.
Has a very low pH optimum on casein of 2.0.
Preference for hydrophobic residue at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves 6-Leu-|-Cys(SO3H)-7, 21-Glu-|-Arg-22 and 3-Asn-|-Gln-4, although not 4-Gln-|-His-5.
From the basidiomycete Irpex lacteus (also known as Polyporus tulipiferae).
Milk clotting activity, broad specificity, but fails to cleave 15-Leu-|-Tyr-16 or 16-Tyr-|-Leu-17 of insulin B chain.
From the basidiomycete Pycnoporus sanguineus, formerly known as P.coccineus and Trametes sanguinea.
Specificity similar to pepsin A, but narrower, cleaving only three bonds in the B chain of insulin: 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17, and 24-Phe-|-Phe-25.
Isolated from the imperfect fungus Scytalidium lignicolum.
Not inhibited by pepstatin-Ac, methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenyl)propane.
A related enzyme from the same organism, proteinase C, is also insensitive to these inhibitors and has molecular weight 406 kDa.
Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves 7-Cys(SO3H)-|-Gly-8 and 17-Leu-|-Val-18 in the B chain of insulin.
A second endopeptidase from S.lignicolum (see scytalidopepsin A) that is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate.
1,2-epoxy-3-(p-nitrophenoxy)propane reacts with Glu-53, which replaces one of the aspartic residues at the active center.
One of the smallest aspartic endopeptidases active as the monomer, with molecular weight 22 kDa.
Similarly inhibitor-resistant endopeptidases are found in the basidiomycetes Lentinus edodes and Ganoderma lucidum, and in Polyporus tulipiferae (a second endopeptidase distinct from polyporopepsin), but these are of typical aspartic endopeptidase size.
Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin.
erythrocyte membrane aspartic proteinase
Found in stomach, spleen, erythrocyte membrane; not lysosomal.
Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomers.
Similar to cathepsin D, but slightly broader specificity.
Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone alpha-mating factor.
Inhibited by pepstatin and the antibiotic globomycin.
Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Hydrolysis of the 33-Phe-|-Leu-34 bond in the alpha-chain of hemoglobin, leading to denaturation of molecule.
Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr.
Known particularly fron barley grain, but present in other plants also.
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
Can partially substitute for kexin in a deficient strain of Saccharomyces cerevisiae.
The homologous product of the MKC7 gene (S.cerevisiae) has similar catalytic activity and has been termed yapsin 2.
Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions.
Isolated from cells and culture medium of the thermophilic archae Sulfolobus acidocaldarius, optimum digestion at pH 2 and 90 degrees Celsius, inhibited by pepstatin.
Another thermostable bacterial endopeptidase has been isolated from Bacillus sp., but this is not inhibited by pepstatin.
Specificity similar to pepsin A, prefers bulky hydrophobic side-chains on either side of the scissible bond.
Many species of bacteria carry pili on their cell surfaces.
These are virulence determinants in pathogenic strains, and are assembled biosynthetically from type IV prepilin subunits.
Before assembly, the prepilin molecules require proteolytic processing, which is done by the prepilin peptidase.
Prepilin peptidase and its homologs play a central role not only in type IV pilus biogenesis but also in transport of macromolecules across cell membranes.
Although both peptide-bond hydrolysis and N-methylation are catalyzed by the same molecule, the methylation can be inhibited without affecting peptidase activity, and it is believed that the enzyme has two separate catalytic sites.
Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
A single aspartic residue is critical for activity, and inhibition by EDTA indicates that a metal ion is also important.
The enzyme is known from several nodaviruses that are pathogens of insects.
Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.
beta-site Alzheimer's amyloid precursor protein cleaving enzyme 2
Can cleave beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease, but is not significantly expressed in human brain.
Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.
beta-site Alzheimer's amyloid precursor protein cleaving enzyme 1
Suggested to be the major 'beta-secretase' responsible for the cleavage of the beta-amyloid precursor protein to form the amyloidogenic beta-peptide that is implicated in the pathology of Alzheimer's disease.
Responsible for the post-translational processing of the human immunodeficiency virus polyprotein.
Endopeptidase for which the P1 residue is preferably hydrophobic.
From the bacterium Yersinia pestis that causes plague.
Converts human Glu-plasminogen to plasmin by cleaving the 560-Arg-|-Val-561 peptide bond that is also hydrolyzed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins.
Shows a preference for cleavage between consecutive basic amino acids, but is capable of cleavage when P1' is a non-basic residue.
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val.
human endogenous retrovirus K endopeptidase
human endogenous retrovirus K10 endopeptidase
human endogenous retrovirus K113 protease
Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ- cleavage site.
The reaction requires nickel to be bound to the precursor of the large subunit of hydrogenase 3.
The endopeptidase uses the metal in the large subunit of [NiFe]-hydrogenases as a recognition motif.
This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of E.coli hydrogenase 3 by cleavage at the C-terminal side of Arg-537.
An aspartic peptidase from Archaea but not bacteria.
In peptidase family A24 (type IV prepilin peptidase family).
Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-|- or Lys-Gly-|-, to release flagellin.
A hemorrhagic endopeptidase of 68 kDa, one of six hemorrhagic toxins in the venom of the western diamondback rattlesnake.
The 60 kDa hemorrhagic toxin 1 of Crotalus ruber ruber shows identical specificity.
Cleavage of 3-Asn-|-Gln-4, 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain. Removes C-terminal Leu from small peptides.
Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.
Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa).
The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary.
The enzymes also act as peptidyl-tripeptidases.
Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus).
Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
From the venom of the western cottonmouth moccasin snake (Agkistrodon piscivorus leucostoma).
Cleavage of 1-Phe-|-Val-2, 5-His-|-Leu-6, 14-Ala-|-Leu-15, 20-Gly-|-Glu-21, 23-Gly-|-Phe-24 and 24-Phe-|-Phe-25 bonds in insulin B chain as well as N-blocked dipeptides.
The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain.
alpha-macroglobulins are cleaved much more rapidly.
The enzyme is widely distributed in vertebrate animals.
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
A membrane-bound glycoprotein widely distributed in animal tissues.
Inhibited by phosphoramidon and thiorphan.
Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
Dissolves fertilization envelope in embryos of sea urchin.
Hydrolysis of proteins of the fertilization envelope and dimethylcasein.
Found in several pathogenic species of Streptococcus such as S.sanguis and S.pneumoniae.
There is also an IgA-specific prolyl endopeptidase of serine-type (see EC 3.4.21.72).
Cleavage of Pro-|-Thr bond in the hinge region of the heavy chain of human IgA.
Removes N-terminal propeptides of type I and II collagens prior to fibril assembly.
Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-|-Gln and of alpha1(II) and alpha2(I) at Ala-|-Gln.
Thiol compounds activate at low concentrations.
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.
No absolute requirement for a prolyl bond; the enzyme acts on some peptides, such as dynorphin 1-8, that do not contain proline, and does not act on some others that do.
Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.
Extracellular endopeptidase of vertebrate tissues.
Degradation of proteoglycans, fibronectin, collagen type III, IV, V and IX and activates procollagenase.
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts.
Differences from EC 3.4.24.11 include insensitivity to phosphoramidon and thiorphan.
PABA-peptide hydrolase is a very similar enzyme found in human intestinal microvilli.
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.
The activity is increased by calcium and by an enhancer glycoprotein.
Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.
From the honey fungus Armillaria mellea.
A similar specificity is shown by Myxobacter sp. AL-1 proteinase II (endoproteinase Lys-C).
Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa may be Pro).
A digestive endopeptidase from the cardia of the crayfish Astacus fluviatilis.
Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
Digests gelatin types I, III, IV, V, fibronectin and proteoglycan.
Similar to stromelysin 1, but action on collagen types III, IV and V is weak.
putative (or punctuated) metalloproteinase-1
Similar in specificity to stromelysin, but more active on azocoll.
Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I).
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Aeromonas proteolytica neutral proteinase
Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica).
Specificity related to, but distinct from, those of the thermolysin and Bacillus subtilis endopeptidase.
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
Pseudomonas aeruginosa neutral metalloproteinase
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.
Bacillus thermoproteolyticus neutral proteinase
A thermostable extracellular metalloendopeptidase containing four calcium ions.
Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae.
Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin.
Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
Variants of this enzyme have been found in species of Bacillus including B.subtilis, B.amyloliquefaciens, B.megaterium, B.mesentericus, B.cereus and B.stearothermophilus.
Similar, but not identical, to that of thermolysin.
Staphylococcus aureus neutral proteinase
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residues. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus.
Streptococcus thermophilus intracellular proteinase
A 30 kDa endopeptidase found intracellularly in Streptococcus thermophilus and S.diacetilactis and in the medium of Enterococcus faecalis.
Preferential cleavage: Xaa-|-Leu, Xaa-|-Phe, Xaa-|-Tyr, Xaa-|-Ala.
The enzyme has been characterized from the bacteria Streptomyces griseus, S.naraensis, and S.cacaoi.
Specificity is similar to that of thermolysin, but much more sensitive to inhibition by sulfanylacetyl-Phe-Leu.
Preferential cleavage of bonds with hydrophobic residues in P1'.
From Achromobacter lyticus and Lysobacter enzymogenes.
Myxobacter sp. AL-1 proteinase I also has characteristics of this enzyme.
Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain at 23-Gly-|-Phe-24 > 18-Val-|-Cys(SO3H).
A metalloenzyme isolated from Pseudomonas fragi.
Useful in protein sequencing applications because of its limited specificity.
Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds.
Similar to interstitial collagenase in specificity.
Stored in the specific granules of neutrophil leukocytes.
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
Cleavage of gelatin types I and V and collagen types IV and V.
A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans.
Contains consensus sequence for a zinc binding site; Z-Tyr-Leu-NHOH is a strong inhibitor.
The enzyme can activate its proenzyme by cleavage of the 100-Val-|-Val-101 bond.
An acidic pH optimum is found with certain protein substrates.
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
Cleavage of Pro-|-Phe and Ala-|-Ala bonds.
Chlamydomonas cell wall degrading protease
Inhibited by phosphoramidon, but also thiol-dependent.
Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall. Also cleaves azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala.
Proteolytic activity found in Penicillium roqueforti, P.caseicolum, Aspergillus sojae and A.oryzae.
Optimum pH of 5 for digesting various proteins.
Strong action on protamine and histones.
A distinct A.sojae endopeptidase is larger and has neutral pH optimum.
Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.
Pseudomonas aeruginosa alkaline protease
Serratia marcescens extracellular proteinase
An extracellular endopeptidase from Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi.
There is broad specificity in cleavage of the insulin B chain, with some species variations.
The pH optimum for digesting various proteins is about 9-10.
From the venom of the western diamondback rattlesnake (Crotalus atrox).
Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. Identical to the cleavage of insulin B chain by atrolysin C. Also cleaves Xaa-|-Ser bonds in glucagon.
Hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox).
Phosphoramidon inhibits in the 0.1 mM range.
Hemorrhagic toxin-2 of C.ruber ruber has the same molecular weight and specificity.
Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1.
A nonhemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox).
Cleavage of 5-His-|-Leu-6, 9-Ser-|-His-10, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain.
Digests basement membrane components, including the triple helix of type IV collagen.
Such action is believed to contribute to the hemorrhagic property by weakening capillary walls.
Cleavage of 3-Asn-|-Gln-4, 9-Ser-|-His-10 and 14-Ala-|-Leu-15 bonds in insulin B chain and 14-Tyr-|-Gln-15 and 8-Thr-|-Ser-9 in A chain. Cleaves type IV collagen at 73-Ala-|-Gln-74 in alpha1-(IV) and at 7-Gly-|-Leu-8 in alpha2-(IV).
Cleavage of 2-Val-|-Asn-3, 4-Gln-|-His-5, 6-Leu-|-Cys-7, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 bonds in insulin B chain.
Crotalus adamanteus metalloendopeptidase
From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus).
Two isoenzymes of approximately 24 kDa that inactivate alpha1-proteinase inhibitor by a single cleavage.
Cleavage of 1-Phe-|-Val-2, 5-His-|-Leu-6, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, and 16-Tyr-|-Leu-17 of insulin B chain.
Cleaves basement membrane, hide powder and fibrinogen.
Hemorrhagic endopeptidase from the venom of the timber rattlesnake (Crotalus horridus horridus).
Cleavage of only the single bond 14-Ala-|-Leu-15 in the insulin B chain, 12-Ser-|-Leu-13 in the A chain, and Ile-|-Gly, Pro-|-Ala, and Ser-|-Trp in mellitin.
Hemorrhagic endopeptidase from the venom of the red rattlesnake (Crotalus ruber ruber).
Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 bonds of the B chain of insulin, His-|-Pro, Pro-|-Phe, and Trp-|-Ser of angiotensin I, and Gly-|-Phe of Met enkephalin.
Caseinolytic endopeptidase of jararaca snake (Bothrops jararaca) venom.
Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.
Endopeptidase from the venom of the jararaca snake (Bothrops jararaca).
Insensitive to phosphoramidon at 0.5 mM.
Cleavage of 4-Gln-|-His-5, 9-Ser-|-His-10 and 14-Ala-|-Leu-15 of insulin B chain and Pro-|-Phe of angiotensin I.
Endopeptidase from the venom of the king cobra (Ophiophagus hannah).
Cleavage of 3-Asn-|-Gln-4, 4-Gln-|-His-5, 10-His-|-Leu-11, 14-Ala-|-Leu-15, and 16-Tyr-|-Leu-17 in insulin B chain.
Hemorrhagic endopeptidase of pI 4.4 from the venom of the habu snake (Trimeresurus flavoviridis).
Cleavage of only two bonds: 10-His-|-Leu-11 and 14-Ala-|-Leu-15, in the insulin B chain.
Nonhemorrhagic endopeptidase from the venom of the habu snake (Trimeresurus flavoviridis).
Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase.
Hemorrhagic and fibrinogenolytic endopeptidase from the Chinese habu snake (Trimeresurus mucrosquamatus) venom.
Cleavage of 9-Ser-|-His-10, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16 and 16-Tyr-|-Leu-17 bonds in the insulin B chain.
From the periplasmic space of Escherichia coli.
Inhibited by EDTA and 1,10-phenanthroline; not thiol dependent.
Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.
Cytosolic enzyme, known from mammals and Drosophila melanogaster.
Inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon.
Degradation of insulin, glucagon and other polypeptides. No action on proteins.
Inhibited by EDTA (100 mM) and 1,10-phenanthroline.
Hydrolysis of O-sialoglycoproteins. Cleaves 31-Arg-|-Asp-32 bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated.
blood-coagulation factor X-activating enzyme
Russell's viper venom factor X activator
Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain.
Natural substrates are precursor proteins that have already been processed by mitochondrial processing peptidase.
Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.
peptide hormone inactivating endopeptidase
An endopeptidase of 100 kDa secreted from the skin of Xenopus laevis.
Resembles neprilysin in insensitivity to 1 uM captopril, but differs in being insensitive to thiorphan and unable to digest (5-Met)-enkephalin, (5-Leu)-enkephalin, oxytocin and substance P-(7-11)-peptide.
Hydrolysis of peptides of at least six residues, with bulky hydrophobic residues in the P1' position. Shows a preference for hydrophobic doublets such as -Phe-|-Phe- and -Phe-|-Leu- in somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide, respectively.
Unusually for a metallopeptidase, inhibited by bestatin, amastin and ethylmaleimide.
Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.
neurosecretory granule protease cleaving pro-ocytocin/neurophysin
Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyze pro-oxytocin at -Lys-Arg-|-Ala-Val-. The specificity further depends on the organization of a beta-turn-alpha-helix of nine or more residues containing the paired basic amino acids near the center.
Inhibited by EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan.
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 and 19-Cys-|-Gly-20 bonds in insulin B chain.
Known from the mitochondrial matrix of fungi and mammals.
Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.
Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide.
Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
Differs from thimet oligopeptidase in lack of thiol activation.
Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.
Hydrolysis of 14-Ala-|-Leu-15 in insulin B chain and 413-Lys-|-Leu-414 in alpha-chain of fibrinogen.
Hemorrhagic endopeptidase from the venom of the jararaca snake.
Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 bonds in insulin B chain.
Hydrolyzes extracellular matrix proteins, and disrupts tight junctions of intstinal cells.
Also degrades intracellular, cytoskeletal proteins actin, myosin and others.
Broad proteolytic specificity, bonds hydrolyzed includes -Gly-|-Leu-, -Met-|-Leu-, -Phe-|-Leu-, -Cys-|-Leu-, -Leu-|-Gly-.
Lyses cells of Staphylococcus aureus in particular, by its action on the cross-bridge of the cell wall.
Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.
The specificity is similar to that of EC 3.4.24.33, but the two are reported to be structurally dissimilar.
Hydrolyzes polypeptides on the amino-side of Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu.
Hydrolyzes proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides.
Initiates the degradation of small, acid-soluble proteins during spore germination in Bacillus megaterium.
Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala.
insulin-like growth factor binding protein-4 protease
Circulates in human pregnancy mainly as a complex with the proform of eosinophil major basic protein, which acts as an inhibitor of the peptidase.
The rate of hydrolysis of IGFBP-4 is increased about 20-fold by the presence of insulin-like growth factor (IGF), whereas that of IGFBP-5 is decreased about two-fold.
Cleavage of the 135-Met-|-Lys-136 bond in insulin-like growth factor binding protein (IGFBP)-4, and the 143-Ser-|-Lys-144 bond in IGFBP-5.
membrane-type matrix metalloproteinase-1
Believed to play an important role in the activation of progelatinase A at cell surfaces.
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
myelin-associated disintegrin metalloproteinase
Partially responsible for the 'alpha-secretase' activity in brain that degrades the potentially harmful beta-amyloid peptide.
Work with ADAM10-deficient mice supports a role in Notch signaling.
Thought to be biologically significant for the degradation of the aggrecan component of cartilage matrix.
Glutamyl endopeptidase. Bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.
From the bacterium Bacilus anthracis that causes anthrax.
One of three proteins that are collectively termed anthrax toxin.
Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases.
Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.
One of two enzymes that can catalyze this processing step for mating a-factor in Saccharomyces cerevisiae.
Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane-anchor.
The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
membrane-bound transcription factor site 2 protease
sterol-regulatory element-binding proteins intramembrane protease
The transcription factors SREBP-1 and -2 are synthesized as precursor proteins that are attached to the membranes of the endoplasmic reticulum and two cleavages are needed to release the active factor so that it can move to the nucleus.
This enzyme cleaves the second of these, and is thus the 'site 2 protease', S2P.
Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.
tumor necrosis factor alpha-converting enzyme
In vivo, the cleavage of tumor necrosis factor alpha precursor releases the soluble, 17-kDa TNF-alpha, which induces inflammation.
Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNFalpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.
The enzyme cleaves the von Willebrand factor at bond 842-Tyr-|-Met-843 within the A2 domain.
This metalloprotease is secreted by the bacterium Peptoclostridium difficile.
The enzyme catalyzes the hydrolytic cleavage of peptide bonds between two proline residues.
A 20-S protein composed of 28 subunits arranged in four rings of seven.
The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
The molecule is barrel-shaped, and the active sites are on the inner surfaces.
Terminal apertures restrict access of substrates to the active sites.
Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
Cleavage of peptide bonds with very broad specificity.
The HslU subunit of the HslU--HslV complex functions as an ATP dependent 'unfoldase'.
The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV.
HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
ATP-dependent cleavage of peptide bonds with broad specificity.
Endopeptidases of unknown catalytic mechanism
Acting on carbon-nitrogen bonds, other than peptide bonds
H2O + L-asparagine = L-aspartate + NH4(+).
H2O + L-glutamine = L-glutamate + NH4(+).
Acts on glutaramate, succinamate and their 2-oxo derivatives.
a monoamide of a dicarboxylate + H2O = a dicarboxylate + NH4(+).
2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+).
2-oxosuccinamate + H2O = NH4(+) + oxaloacetate.
a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+).
H2O + indole-3-acetamide = (indol-3-yl)acetate + NH4(+).
The animal enzyme also acts on beta-ureidoisobutyrate.
3-(carbamoylamino)propanoate + 2 H(+) + H2O = beta-alanine + CO2 + NH4(+).
3-(carbamoylamino)-2-methylpropanoate + 2 H(+) + H2O = (R)-3-amino-2-methylpropanoate + CO2 + NH4(+).
2 H(+) + H2O + N-carbamoyl-L-aspartate = CO2 + L-aspartate + NH4(+).
H2O + N-formyl-L-aspartate = formate + L-aspartate.
Also acts on other aromatic formylamines.
H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine.
(6S)-10-formyltetrahydrofolate + H2O = (6S)-5,6,7,8-tetrahydrofolate + formate + H(+).
H2O + penicillin = 6-aminopenicillanate + a carboxylate.
an anilide + H2O = a carboxylate + aniline + H(+).
N-acyl-aliphatic-L-amino acid amidohydrolase
The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids.
Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114.
an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid.
an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-substituted L-cysteine.
H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate.
H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine.
an N(6)-acyl-L-lysine + H2O = a carboxylate + L-lysine.
H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate.
H2O + nicotinamide = NH4(+) + nicotinate.
2 H(+) + H2O + L-citrulline = CO2 + L-ornithine + NH4(+).
H2O + N-acetyl-beta-alanine = acetate + beta-alanine.
(R)-pantothenate + H2O = (R)-pantoate + beta-alanine.
an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine.
Also acts on the 3alpha,12alpha-dihydroxy-derivative, and on choloyl-taurine.
N-acetylglucosamine-6-phosphate deacetylase
H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate.
beta-aspartylglucosylamine amidohydrolase
Acts only on asparagine-oligosaccharides containing one amino acid, i.e. the asparagine has free alpha-amino and alpha-carboxyl groups (cf. EC 3.5.1.52).
H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+) + L-aspartate + N-acetyl-beta-D-glucosaminylamine.
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
2-(acetamidomethylene)succinate hydrolase
Involved in the degradation of pyridoxine in Pseudomonas.
2-(acetamidomethylene)succinate + H(+) + 2 H2O = acetate + CO2 + NH4(+) + succinate semialdehyde.
The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.
5-aminopentanamide + H2O = 5-aminopentanoate + NH4(+).
H2O + N-formyl-L-methionine = formate + L-methionine.
H2O + N-benzoylglycine = benzoate + glycine.
H2O + N-acetyl-D-glucosamine = acetate + D-glucosamine.
D-glutamine + H2O = D-glutamate + NH4(+).
5-hydroxy-N-methylpyroglutamate synthase
In the reverse reaction, the product cyclizes non-enzymically to 2-hydroxy-N-methyl-5-oxoproline.
H2O + N-methyl-2-oxoglutaramate = 2-oxoglutarate + methylamine.
L-asparagine is hydrolyzed at 0.8 of the rate of L-glutamine.
The D-isomers are also hydrolyzed, more slowly.
The enzyme hydrolyzes N-monosubstituted and N,N-disubstituted amides, and there is some activity toward primary amides.
It has little or no activity toward short-chain substrates.
H2O + N-methylhexanamide = hexanoate + methylamine.
Also acts on acetylagmatine, propanoylagmatine and bleomycin B2.
H2O + N(4)-benzoylagmatine = agmatine + benzoate.
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan.
Also acts more slowly on beta-nicotinamide D-ribonucleoside.
beta-nicotinamide D-ribonucleotide + H2O = NH4(+) + nicotinate beta-D-ribonucleotide.
Specific for the hydrolysis of the gamma-amide of glutamine substituted at the alpha-amino group, e.g., glycyl-L-glutamine, N-acetyl-L-glutamine and L-leucylglycyl-L-glutamine.
[protein]-C-terminal-L-glutamine + H2O = [protein]-C-terminal-L-glutamate + NH4(+).
Specific for the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L-glutaminylglycine.
H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+).
The enzyme is involved in degradation of nylon-6 oligomers.
It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2-20 by exo-type cleavage, removing residues sequentially from the N-terminus.
Activity decreases with the increase of the polymerization number of the oligomer; cf. EC 3.5.1.117 and EC 3.5.2.12.
[N-(6-aminohexanoyl)](n) + H2O = 6-aminohexanoate + [N-(6-aminohexanoyl)](n-1).
H2O + N-(6-aminohexanoyl)-6-aminohexanoate = 2 6-aminohexanoate.
H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + acetate.
It was initially thought that N(1)-acetylspermidine was the substrate for this deacetylase reaction but this has since been disproved.
H2O + N(8)-acetylspermidine = acetate + spermidine.
Also acts, more slowly, on acetamide, propanamide and butanamide.
Also acts, more slowly, on other short-chain aliphatic amides.
H2O + pentanamide = NH4(+) + pentanoate.
The enzyme also hydrolyzes 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.
4-acetamidobutanoyl-CoA + H2O = 4-aminobutanoyl-CoA + acetate.
peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino-acid residues in the substrate (cf. EC 3.5.1.26).
Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
2 H(+) + H2O + N-carbamoylputrescine = CO2 + NH4(+) + putrescine.
Along with EC 3.5.2.15 and EC 3.5.1.84, forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria.
The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 6.3.4.6, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate.
The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate.
3 H(+) + H2O + urea-1-carboxylate = 2 CO2 + 2 NH4(+).
long-chain-fatty-acyl-glutamate deacylase
Does not act on acyl derivatives of other amino acids.
Optimum chain length of acyl residue is 12 to 16.
H2O + N-(long-chain-fatty-acyl)-L-glutamate = a long-chain fatty acid + L-glutamate.
Also acts on N-ethylformamide and N-methylformamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.
H2O + N,N-dimethylformamide = dimethylamine + formate.
Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.
H2O + L-tryptophanamide = L-tryptophan + NH4(+).
Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides (cf. EC 3.5.1.64).
H(+) + H2O + N-benzyloxycarbonylglycine = benzyl alcohol + CO2 + glycine.
2 H(+) + H2O + N-carbamoylsarcosine = CO2 + NH4(+) + sarcosine.
N-(long-chain-acyl)ethanolamine deacylase
This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines.
Unlike EC 3.5.1.99 it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide.
The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex.
H2O + N-(long-chain fatty acyl)ethanolamine = a long-chain fatty acid + ethanolamine.
An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.
H2O + L-mimosine = 3-hydroxy-4H-pyrid-4-one + L-serine.
The enzyme from Micrococcus luteus also acts on N(8)-acetylspermidine and acetylcadaverine, but more slowly.
H2O + N-acetylputrescine = acetate + putrescine.
Also acts on N-acetyl-beta-alanine and 5-acetamidopentanoate.
4-acetamidobutanoate + H2O = 4-aminobutanoate + acetate.
5-acetamidopentanoate + H2O = 5-aminopentanoate + acetate.
N(alpha)-benzyloxycarbonylleucine hydrolase
Also acts on N(alpha)-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine (cf. EC 3.5.1.58).
H(+) + H2O + N-benzyloxycarbonyl-L-leucine = benzyl alcohol + CO2 + L-leucine.
Also acts on other N-alkyl-L-glutamines.
H2O + N(5)-ethyl-L-glutamine = ethylamine + L-glutamate.
2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
Involved in the degradation of pyridoxine by Pseudomonas and Arthrobacter.
2-(acetamidomethylene)-3-(hydroxymethyl)succinate + H(+) + 2 H2O = 2-(hydroxymethyl)-4-oxobutanoate + acetate + CO2 + NH4(+).
4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH4(+).
The animal enzyme also acts on beta-citryl-L-glutamate and beta-citryl-L-glutamine.
H2O + N-formyl-L-glutamate = formate + L-glutamate.
Does not act on sphingolipids such as ceramide.
Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives.
Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain.
Hydrolyzes a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series.
H2O + N-feruloylglycine = (E)-ferulate + glycine.
D-benzoylarginine-4-nitroanilide amidase
H2O + N(2)-benzoyl-D-arginine-4-nitroanilide = 4-nitroaniline + H(+) + N(2)-benzoyl-D-arginine.
(R)-carnitinamide + H2O = (R)-carnitine + NH4(+).
Some other taurine conjugates are hydrolyzed, but not glycine conjugates of bile acids.
H2O + taurochenodeoxycholate = chenodeoxycholate + taurine.
H(+) + H2O + urethane = CO2 + ethanol + NH4(+).
Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin.
It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13.
an N-acetylarylalkylamine + H2O = acetate + an aralkylamine.
H2O + N-(2-phenylethyl)acetamide = 2-phenylethylamine + acetate.
This enzyme, along with EC 3.5.1.87, EC 5.1.99.5 and EC 3.5.2.2, forms part of the reaction cascade known as the 'hydantoinase process', which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids.
Has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
an N-carbamoyl-D-amino acid + 2 H(+) + H2O = a D-alpha-amino acid + CO2 + NH4(+).
glutathionylspermidine amidohydrolase (spermidine-forming)
Transforms glutathionylspermidine into glutathione and spermidine.
The enzyme from Escherichia coli is bifunctional and also catalyzes the reaction of EC 6.3.1.8, resulting in a net hydrolysis of ATP.
glutathionylspermidine + H2O = glutathione + spermidine.
Phthalyl is used to mean 2-carboxybenzoyl.
The enzyme from Xanthobacter agilis hydrolyzes phthalylated amino acids, peptides, beta-lactams, aromatic and aliphatic amines.
The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative.
Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine.
a phtalamide + H2O = a primary amine + phthalate.
Has a wide specificity; hydrolyzes N-acyl derivative of neutral D-amino acids.
Used in separating D- and L-amino acids.
an N-acyl-D-amino acid + H2O = a carboxylate + a D-alpha-amino acid.
an N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate.
an N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate.
The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanurate, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine].
The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of 1-carboxybiuret hydrolase.
biuret + H2O = NH4(+) + urea-1-carboxylate.
(S)-N-acetyl-1-phenylethylamine hydrolase
(S)-N-acetyl-1-phenylethylamine amidohydrolase
Inhibited by phenylmethanesulfonyl fluoride.
Some related acetylated compounds are hydrolyzed with variable enantiomeric selectivities.
(S)-N-acetyl-1-phenylethylamine + H2O = (S)-1-phenylethylamine + acetate.
(R)-mandelamide + H2O = (R)-mandelate + NH4(+).
This enzyme, along with EC 3.5.1.77, EC 5.1.99.5 and EC 3.5.2.2, forms part of the reaction cascade known as the 'hydantoinase process', which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids.
The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan.
The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyze N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents.
The enzyme is inactive on derivatives of D-amino acids.
In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyze formyl and acetyl derivatives to varying degrees.
an N-carbamoyl-L-alpha-amino acid + 2 H(+) + H2O = an L-alpha-amino acid + CO2 + NH4(+).
Also requires at least a dipeptide for an efficient rate of reaction.
N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Differs in substrate specificity from EC 3.5.1.31.
H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide].
N-acetylglucosaminylphosphatidylinositol deacetylase
acetylglucosaminylphosphatidylinositol deacetylase
N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase
N-acetylglucosaminylphosphatidylinositol de-N-acetylase
Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes.
The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in Saccharomyces cerevisiae).
In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.
a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol.
Involved in the salvage pathway of cobinamide in archaea.
Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps.
First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10 (CbiB).
adenosylcob(III)inamide + H2O = (R)-1-aminopropan-2-ol + adenosylcob(III)yrate.
While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly.
Amides of other acids do not act as substrates.
H2O + N-benzylformamide = benzylamine + formate.
Hydrolyzes only one of the amide bonds of pantetheine.
The substrate analogs phosphopantetheine and CoA are not substrates.
Recycles pantothenate (vitamin B5) and produces cysteamine, a potent anti-oxidant.
(R)-pantetheine + H2O = (R)-pantothenate + cysteamine.
glutaryl-7-aminocephalosporanic-acid acylase
7beta-(4-carboxybutanamido)cephalosporanic acid acylase
glutaryl-7-aminocephalosporanic acid acylase
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics.
It reacts only weakly with cephalosporin C.
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
gamma-glutamyl-gamma-aminobutyrate hydrolase
Forms part of a novel putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form gamma-glutamylputrescine, which is oxidized to 4-(gamma-glutamylamino)butanal and then to 4-(gamma-glutamylamino)butanoate.
Also can catalyze the reactions of EC 3.5.1.35 and EC 3.5.1.65.
4-(gamma-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate.
Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 and EC 3.5.2.1.
3-oxo-3-ureidopropanoate + H2O = H(+) + malonate + urea.
N(2)-acetylglutamate is not a substrate.
The final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine.
H2O + N-succinyl-L-glutamate = L-glutamate + succinate.
This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules.
It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons.
Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity.
an N-acyl-L-homoserine lactone + H2O = a carboxylate + L-homoserine lactone.
A class of enzymes that remove acetyl groups from N(6)-acetyl-lysine residues on a histone.
The reaction of this enzyme is opposite to that of EC 2.3.1.48.
Histone deacetylases (HDACs) can be organized into three classes depending on sequence similarity and domain organization.
Histone acetylation plays an important role in regulation of gene expression.
In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation.
H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone].
Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.
H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine.
(9Z)-octadecenamide + H2O = (9Z)-octadecenoate + NH4(+).
In addition (R)-piperidine-3-carboxamide is hydrolyzed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolyzed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity.
The enzyme does not act on the other amide substrates which are hydrolyzed by EC 3.5.1.4 (amidase).
(R)-piperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylate + NH4(+).
beta-alaninamide + H2O = beta-alanine + NH4(+).
(3R)-piperidine-3-carboxamide + H2O = (3R)-piperidine-3-carboxylate + NH4(+).
(R)-N-tert-butylpiperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylate + tert-butylamine.
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase
(S)-piperazine-2-carboxamide + H2O = (S)-piperazine-2-carboxylate + NH4(+).
H2O + L-prolinamide = L-proline + NH4(+).
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
The enzyme catalyzes the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis.
The first step is catalyzed by EC 3.5.4.29.
The bacterial enzyme, EC 3.5.4.25 catalyzes both reactions.
2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + formate + H(+).
N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase
This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway.
In addition to acetylase activity, the enzyme possesses weak mycothiol conjugate amidase activity, and shares sequence similarity with mycothiol S-conjugate amidase.
1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate.
peptidoglycan-N-acetylglucosamine deacetylase
peptidoglycan N-acetylglucosamine deacetylase
Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.
The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively.
peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.
Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains.
Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-beta-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus.
In contrast to EC 3.5.1.41 this enzyme is specific for the chitin disaccharide.
It also deacetylates the chitin trisaccharide with lower efficiency.
No activity with higher polymers of GlcNAc.
H2O + N,N'-diacetylchitobiose = acetate + N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine.
H2O + N-formylmaleamate = formate + H(+) + maleamate.
UDP-3-O-acyl-N-acetylglucosamine deacetylase
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase
The enzyme catalyzes a committed step in the biosynthesis of lipid A.
a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate.
glucosylceramide sphingomyelin deacylase
sphingomyelin glucosylceramide deacylase
The enzyme is involved in the sphingolipid metabolism in the epidermis.
a sphingomyelin + H2O = a carboxylate + sphing-4-enine-phosphocholine.
a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = a fatty acid + beta-D-glucosyl-(1<->1)-sphing-4-enine.
(Z)-3-ureidoacrylate + H(+) + H2O = (Z)-3-aminoacrylate + CO2 + NH4(+).
(Z)-2-methylureidoacrylate + H(+) + H2O = (Z)-2-methylaminoacrylate + CO2 + NH4(+).
The enzyme, which is highly specific for its substrate, participates in the nicotine degradation pathway of several Gram-positive bacteria.
The enzyme from the bacterium Streptomyces fradiae can also accept 2'''-acetyl-6'''-hydroxyneomycin C as substrate, cf. EC 3.5.1.113.
2'-N-acetylparomamine + H2O = acetate + paromamine.
2'''-acetyl-6'''-hydroxyneomycin C deacetylase
The enzyme from the bacterium Streptomyces fradiae also catalyzes EC 3.5.1.112.
2'''-acetyl-6'''-hydroxyneomycin C + H2O = 6'''-deamino-6'''-hydroxyneomycin C + acetate.
N-acyl-aromatic-L-amino acid amidohydrolase
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
It preferentially deacetylates N(alpha)-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14.
Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114.
an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + an aromatic L-alpha-amino acid.
The enzyme that is found in actinomycetes is involved in the detoxification of oxidizing agents and electrophilic antibiotics.
The enzyme has low activity with 1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol as substrate (cf. EC 3.5.1.103).
H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-conjugate.
This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation.
Not to be confused with EC 4.3.2.3, which releases urea rather than ammonia.
(S)-ureidoglycolate + 2 H(+) + H2O = CO2 + glyoxylate + 2 NH4(+).
endo-type 6-aminohexanoate oligomer hydrolase
It degrades linear or cyclic oligomers of poly(6-aminohexanoate) with a degree of polymerization greater than three (n > 3) by endo-type cleavage, to oligomers of a length of two or more (2 <= x < n).
It shows negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate (cf. EC 3.5.1.46) or with 1,8-diazacyclotetradecane-2,9-dione (cf. EC 3.5.2.12).
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x.
gamma-glutamyl hercynylcysteine S-oxide hydrolase
The enzyme is part of the biosynthesis pathway of ergothioneine in mycobacteria.
gamma-L-glutamyl-hercynylcysteine S-oxide + H2O = L-glutamate + S-(hercyn-2-yl)-L-cysteine S-oxide.
The enzyme has been characterized from the bacterium Mycobacterium tuberculosis.
It catalyzes the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalyzed by EC 6.3.1.19.
Deamination requires ATP as cofactor but not its hydrolysis.
The enzyme also catalyzes the hydrolytic cleavage of the bond formed by the ligase, between an epsilon-amino group of a lysine residue of the target protein and the gamma-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein.
[prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate + NH4(+).
protein N-terminal asparagine amidohydrolase
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn.
Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate.
The latter serves as a substrate for EC 2.3.2.8 making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.
H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal L-aspartyl-[protein] + NH4(+).
protein N-terminal glutamine amidohydrolase
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Gln.
Following the acetylation and removal of the initiator methionine, the exposed N-terminal glutamine is deaminated, resulting in its conversion to L-glutamate.
H2O + N-terminal L-glutaminyl-[protein] = N-terminal L-glutamyl-[protein] + NH4(+).
The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyzes the opposite reaction from that catalyzed by EC 6.3.1.18, which is part of an aniline degradation pathway.
Its purpose is likely to maintain a low concentration of N(5)-phenyl-L-glutamine, which is potentially toxic.
H2O + N(5)-phenyl-L-glutamine = aniline + H(+) + L-glutamate.
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal.
The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines.
The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively.
H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate.
H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate.
H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate.
H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein].
H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein].
H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein].
N(2)-acetyl-L-2,4-diaminobutanoate deacetylase
The enzyme, found in bacteria, has no activity with (2S)-4-acetamido-2-aminobutanoate (cf. EC 3.5.4.44).
(2S)-2-acetamido-4-aminobutanoate + H2O = acetate + L-2,4-diaminobutanoate.
The enzyme has been characterized from the bacterium Klebsiella pneumoniae.
This entry includes a family of enzymes that recyle jasmonoyl-amino acid conjugates back to jasmonates.
The enzymes from Arabidopsis thaliana have been shown to also act on 12-hydroxyjasmonoyl-L-isoleucine, generating tuberonic acid.
a jasmonyl-L-amino acid + H2O = a jasmonate + an L-alpha-amino acid.
H2O + L-isoleucine-(+)-7-isojasmonate = (+)-7-isojasmonate + L-isoleucine.
H2O + L-isoleucine-(+)-12-hydroxy-7-isojasmonate = L-isoleucine + tuberonate.
The enzyme, present in animals, fungi and bacteria, is involved in clearing cells of the toxic compound deaminated glutathione, which can be produced as an unwanted side product by several transaminases.
H2O + N-(4-oxoglutaryl)-L-cysteinylglycine = 2-oxoglutarate + L-cysteinylglycine.
N(5)-(cytidine 5'-diphosphoramidyl)-L-glutamine hydrolase
N(5)-(cytidine 5'-diphosphoramidyl)-L-glutamine deacylase
H2O + N(5)-(cytidine 5'-diphosphoramidyl)-L-glutamine = cytidine 5'-diphosphoramidate + H(+) + L-glutamate.
[amino group carrier protein]-lysine hydrolase
The enzyme participates in an L-lysine biosynthetic pathway in certain species of archaea and bacteria.
In some organisms the enzyme also catalyzes the activity of EC 3.5.1.132.
[amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [amino-group carrier protein]-C-terminal-L-glutamate + L-lysine.
The enzyme, characterized from the bacterium Pseudomonas sp ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine].
The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex.
1-carboxybiuret + H2O = NH4(+) + urea-1,3-dicarboxylate.
[amino group carrier protein]-ornithine hydrolase
The enzyme participates in an L-arginine biosynthetic pathways in certain species of archaea and bacteria.
In all cases known so far the enzyme also catalyzes the activity of EC 3.5.1.130.
[amino-group carrier protein]-C-terminal-gamma-(L-ornithyl)-L-glutamate + H2O = [amino-group carrier protein]-C-terminal-L-glutamate + L-ornithine.
The enzyme, characterized from the bacterium Corynebacterium sp.Ax20, hydrolyzes odorless N(alpha)-acyl-L-glutamine conjugates of short- and medium-chain fatty acids, releasing axillary malodor compounds.
While the enzyme is highly specific for the L-glutamine moiety, it is quite promiscuous regarding the acyl moiety.
The two most common products of the enzyme's activity in axillary secretions are (2E)-3-methylhex-2-enoate and 3-hydroxy-3-methylhexanoate.
an N(2)-acyl-L-glutamine + H2O = a carboxylate + L-glutamine.
H2O + N(2)-[(2E)-3-methylhex-2-enoyl]-L-glutaminate = (2E)-3-methylhex-2-enoate + L-glutamine.
H2O + N(2)-(3-hydroxy-3-methylhexanoyl)-L-glutaminate = 3-hydroxy-3-methylhexanoate + L-glutamine.
(indol-3-yl)acetyl-L-aspartate hydrolase
The enzyme, isolated from the bacterium Pantoea agglomerans, is specific for its substrate and does not act efficiently on other indole-3-acetate conjugates.
(indol-3-yl)acetyl-L-aspartate + H2O = (indol-3-yl)acetate + L-aspartate.
The enzyme from the bacterium Escherichia coli is one of the smallest known monomeric amidohydrolases (103-amino acids).
The enzyme is active toward a wide range of N(4)-acylcytosines/cytidines, but is by far most active against N(4)-acetylcytidine.
H2O + N(4)-acetylcytidine = acetate + cytidine + H(+).
H2O + N(4)-acetyl-2'-deoxycytidine = 2'-deoxycytidine + acetate + H(+).
H2O + N(4)-acetylcytosine = acetate + cytosine + H(+).
N,N'-diacetylchitobiose non-reducing end deacetylase
The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N'-diacetylchitobiose, the end product of the archaeal chitinase, to produce beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine.
This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N'-diacetylchitobiose at the reducing residue to produce N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine.
H2O + N,N'-diacetylchitobiose = acetate + beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine.
4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase
undecaprenyl-phosphate-alpha-L-Ara4FN deformylase
4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate.
Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 and EC 3.5.1.95.
It was previously thought that the end-products of the reaction were malonate and urea.
May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9.
barbiturate + H2O = 3-oxo-3-ureidopropanoate.
Also acts on dihydrothymine and hydantoin.
5,6-dihydrouracil + H2O = 3-(carbamoylamino)propanoate + H(+).
5,6-dihydrothymine + H2O = 3-(carbamoylamino)-2-methylpropanoate + H(+).
(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate.
H2O + L-5-carboxymethylhydantoin = H(+) + N-carbamoyl-L-aspartate.
(S)-allantoin + H2O = allantoate + H(+).
Zinc is only requires in class-B enzymes.
A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins.
a beta-lactam + H2O = a substituted beta-amino acid.
4(5)-imidazolone-5(4)-propionic acid hydrolase
4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate.
5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate.
H2O + L-2-aminohexano-6-lactam = L-lysine.
The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.
1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate.
Highly specific; does not hydrolyze other dioxopiperazines, glycylglycine, proteins or barbiturates.
2,5-dioxopiperazine + H2O = glycylglycine.
ATP + 2 H2O + N-methylhydantoin = ADP + 2 H(+) + N-carbamoylsarcosine + phosphate.
The enzyme catalyzes the ring cleavage of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine].
The enzyme is highly specific for cyanuric acid.
The product was initially thought to be bioret, but was later shown to be 1-carboxybioret.
cyanurate + H2O = 1-carboxybiuret + H(+).
Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4.
The reverse, cyclization, reaction is also catalyzed, but much more slowly.
It has lower activity toward cyclic ureides, which are the substrates of EC 3.5.2.2.
The reaction is the first stage in the conversion of 5-hydroxyisourate into (S)-allantoin.
This reaction will also occur spontaneously, but more slowly.
5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+).
1,4,5,6-tetrahydro-6-oxonicotinate + 2 H2O = 2-formylglutarate + NH4(+).
The enzyme also catalyzes the hydrolysis of streptothricin-D to streptothricin-D acid.
The enzyme is responsible for streptothricin resistance in Streptomyces albulus and Streptomyces noursei.
H2O + streptothricin F = streptothricin F acid.
H2O + streptothricin D = streptothricin D acid.
This enzyme, found in several bacterial species, is involved in the degradation of indole-3-acetic acid.
Also hydrolyzes alpha-N-substituted L-arginines and canavanine.
guanidinoacetate + H2O = glycine + urea.
Also hydrolyzes (R)-ureidoglycolate to glyoxylate and urea.
allantoate + H2O = (S)-ureidoglycolate + urea.
H2O + N-formimidoyl-L-aspartate = N-formyl-L-aspartate + NH4(+).
H2O + L-arginine = L-citrulline + NH4(+).
Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidino-hexanoate.
4-guanidinobutanoate + H2O = 4-aminobutanoate + urea.
H2O + N-formimidoyl-L-glutamate = formamide + L-glutamate.
This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds.
This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria.
In plants it is localized in the endoplasmic reticulum.
allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+).
The plant enzyme also catalyzes the reactions of EC 2.1.3.3, EC 2.1.3.6 and EC 2.7.2.2, thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.
agmatine + H2O = N-carbamoylputrescine + NH4(+).
H2O + N-formimidoyl-L-glutamate = N-formyl-L-glutamate + NH4(+).
Also acts slowly on N-amidino-L-glutamate.
H2O + N-amidino-L-aspartate = L-aspartate + urea.
Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.
H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+).
Acts on other alkylguanidines, very slowly.
H2O + methylguanidine = methylamine + urea.
Also acts, more slowly, on taurocyamine and 4-guanidinobutanoate.
3-guanidinopropanoate + H2O = beta-alanine + urea.
N(G),N(G)-dimethylarginine dimethylaminohydrolase
Also acts on N(omega)-methyl-L-arginine.
H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline.
H2O + N(omega)-methyl-L-arginine = L-citrulline + methylamine.
Other diguanidinoalkanes with 3 to 10 methylene groups can act, more slowly.
1,4-diguanidinobutane + H2O = agmatine + urea.
The methylenediurea is hydrolyzed and decarboxylated to give an aminated methylurea, which then spontaneously hydrolyzes to hydroxymethylurea.
The enzyme from Ochrobactrum anthropi also hydrolyzes dimethylenetriurea and trimethylenetetraurea as well as ureidoglycolate, which is hydrolyzed to urea and glyoxylate, and allantoate, which is hydrolyzed to ureidoglycolate, ammonia and carbon dioxide.
2 H(+) + 2 H2O + methylenediurea = CO2 + N-(hydroxymethyl)urea + 2 NH4(+).
Forms part of the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus.
It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, and the second and third reactions of that enzyme.
amidinoproclavaminate + H2O = proclavaminate + urea.
Arginine, N(2)-acetylarginine and N(2)-glutamylarginine do not act as substrates.
The second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine.
2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-succinyl-L-ornithine + 2 NH4(+).
The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
H2O + N(1)-aminopropylagmatine = spermidine + urea.
N(omega)-hydroxy-L-arginine amidinohydrolase
H2O + N(omega)-hydroxy-L-arginine = hydroxyurea + L-ornithine.
This enzyme, found in plants and bacteria, is part of the ureide pathway, which enables the recycling of the nitrogen in purine compounds.
(S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH4(+).
cytosine + H(+) + H2O = NH4(+) + uracil.
adenine + H(+) + H2O = hypoxanthine + NH4(+).
guanine + H(+) + H2O = NH4(+) + xanthine.
adenosine + H(+) + H2O = inosine + NH4(+).
2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+).
Catalyzes the deamination of cytidine and 2'-deoxycytidine with similar efficiencies.
The enzyme, which is widely distributed among organisms, is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
cytidine + H(+) + H2O = NH4(+) + uridine.
2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+).
Forms part of the xanthine-degradation pathway in some bacteria.
The product of the reaction, imidazol-4-one, can be converted non-enzymically into formiminoglycine.
4-aminoimidazole + H(+) + H2O = imidazol-4-one + NH4(+).
5,10-methenyltetrahydrofolate + H2O = (6S)-10-formyltetrahydrofolate + H(+).
H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
The animal enzyme is specific for pterin, isoxanthopterin and tetrahydropterin.
a 2-amino-4-hydroxypteridine + H(+) + H2O = a 2,4-dihydroxypteridine + NH4(+).
2-amino-4-hydroxypteridine + H(+) + H2O = 2,4-dihydroxypteridine + NH4(+).
guanosine + H(+) + H2O = NH4(+) + xanthosine.
The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic.
Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12.
GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+).
Acts on AMP, ADP, ATP, NAD(+) and adenosine, in decreasing order of activity.
The bacterial enzyme can also accept the deoxy derivatives (cf. EC 3.5.4.6).
The Neurospora crassa enzyme also catalyzes the reactions of EC 1.1.1.23 and EC 3.6.1.31.
1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide.
1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium + H(+) + H2O = 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium + NH4(+).
creatinine + H(+) + H2O = N-methylhydantoin + NH4(+).
1-pyrroline-4-hydroxy-2-carboxylate deaminase
4-hydroxy-1-pyrroline-2-carboxylate + H(+) + H2O = 2,5-dioxopentanoate + NH4(+).
Catalyzes the deamination of the cytosine group of the antibiotics blasticidin S, cytomycin and acetylblasticidin S.
blasticidin S + H(+) + H2O = deaminohydroxyblasticidin S + NH4(+).
Also acts on isosepiapterin, more slowly.
H(+) + H2O + sepiapterin = NH4(+) + xanthopterin-B2.
GTP 7,8-8,9-dihydrolase (diphosphate-forming)
guanosine triphosphate cyclohydrolase II
The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the alpha-beta phosphodiester bond of the triphosphate to form diphosphate.
The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions.
The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively.
It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, EC 3.5.4.29, and EC 3.5.4.39.
GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate.
diaminohydroxyphosphoribosylaminopyrimidine deaminase
The substrate is the product of EC 3.5.4.25.
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+).
methenyltetrahydromethanopterin cyclohydrolase
Involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin.
H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine.
This enzyme catalyzes the hydrolysis of the imidazole ring of guanosine 5'-triphosphate, N(7)-methylguanosine 5'-triphosphate or inosine 5'-triphosphate.
Xanthosine 5'-triphosphate and ATP are not substrates.
It also catalyzes the hydrolysis of diphosphate to form two equivalents of phosphate.
Unlike EC 3.5.4.25, this enzyme does not release formate, but does hydrolyze the diphosphate from GTP to phosphate.
GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + 2 H(+) + 2 phosphate.
Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated.
While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13 and EC 3.6.1.23), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions.
This enzyme can also act as a dUTP diphosphatase, but more slowly.
dCTP + 2 H2O = diphosphate + dUMP + NH4(+).
The enzyme from Thermotoga maritima also functions as S-adenosylhomocysteine deaminase (EC 3.5.4.28) and has some activity against adenosine.
Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) are not substrates.
H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-thioinosine.
8-oxoguanine is formed via the oxidation of guanine within DNA by reactive oxygen species.
If uncorrected, this modification leads to the incorporation of 8-oxoG:A mismatches and eventually to G:C to T:A transversions.
8-oxoguanine + H(+) + H2O = NH4(+) + urate.
The enzyme is involved in editing of tRNA.
adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+).
The enzyme deaminates adenosine(37) to inosine in eukaryotic tRNA(Ala).
adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+).
The enzyme from Methanopyrus kandleri specifically catalyzes the deamimation of cytosine at poition 8 of tRNA in 30 different tRNAs.
This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.
cytidine(8) in tRNA + H(+) + H2O = NH4(+) + uridine(8) in tRNA.
The apolipoprotein B mRNA editing enzyme complex catalyzes the editing of apolipoprotein B mRNA at cytidine(6666) to uridine, thereby transforming the codon for glutamine-2153 to a termination codon.
Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport.
The catalytic component (APOBEC-1) contains zinc at the active site.
cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) + uridine(6666) in apoB mRNA.
double-stranded RNA-specific adenosine deaminase
This eukaryotic enzyme is involved in RNA editing.
It destabilizes double-stranded RNA through conversion of adenosine to inosine.
Inositol hexakisphosphate is required for activity.
adenosine in double-stranded RNA + H(+) + H2O = inosine in double-stranded RNA + NH4(+).
The enzyme exclusively catalyzes deamination of cytosine in single-stranded DNA.
It preferentially deaminates five-nucleotide bubbles.
The optimal target consists of a single-stranded NWRCN motif (W = A or T, R = A or G).
The enzyme initiates antibody diversification processes by deaminating immunoglobulin sequences.
a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+).
The enzyme is involved in methanopterin biosynthesis in methanogenic archaea.
GTP + H2O = 7,8-dihydroneopterin 2',3'-cyclic phosphate + diphosphate + formate + H(+).
6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+).
The enzyme from the archaeon Methanocaldococcus jannaschii is involved in the recycling of 5'-deoxyadenosine.
5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+).
N-isopropylammelide isopropylaminohydrolase
This bacterial enzyme is involved in degradation of the herbicide atrazine.
It can hydrolyze other N-substituted amino dihydroxy-s-triazine molecules, and prefers substrates with linear N-alkyl groups to those with branched alkyl groups.
H(+) + H2O + N-isopropylammelide = cyanurate + isopropylamine.
hydroxydechloroatrazine ethylaminohydrolase
2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase
The enzyme has a broad substrate range, and requires a monohydroxylated S-triazine ring with a minimum of one primary or secondary amine substituent and either a chloride or amine leaving group.
It catalyzes both deamination and dechlorination reactions.
H(+) + H2O + hydroxyatrazine = ethylamine + N-isopropylammelide.
The enzyme, found in some halophilic bacteria, is involved in the degradation of the compatible solute ectoine.
The enzyme, which belongs to peptidase family M24, only acts in the direction of ectoine hydrolysis.
It also produces smaller amounts of (2S)-4-acetamido-2-aminobutanoate, which is recycled back to ectoine by EC 4.2.1.108.
H2O + L-ectoine = (2S)-2-acetamido-4-aminobutanoate.
The enzyme, isolated from the bacterium Acidovorax citrulli, performs the deamination of melamine 15-fold faster than the deamination of ammeline.
It also has activity with 2-chloro-4,6-diamino-S-triazine, but has no activity toward halo-substituted triazine ring compounds such as atrazine (cf. EC 3.8.1.8).
ammeline + H(+) + H2O = ammelide + NH4(+).
The enzyme, isolated from the bacterium Leptospira interrogans, is specific for cAMP.
Acts on a wide range of aromatic nitriles including (indol-3-yl)acetonitrile, and also on some aliphatic nitriles, and on the corresponding acid amides (cf. EC 4.2.1.84).
a nitrile + 2 H2O = a carboxylate + NH4(+).
(indol-3-yl)acetonitrile + 2 H2O = (indol-3-yl)acetate + NH4(+).
2 H2O + phenylpropanonitrile = 3-phenylpropanoate + NH4(+).
2 H2O + ricinine = 4-methoxy-1-methyl-2-oxo-1,2-dihydropyridine-3-carboxylate + NH4(+).
L-Asparagine is formed as an intermediate.
3-cyano-L-alanine + 2 H2O = L-aspartate + NH4(+).
Also hydrolyzes other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.
4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH4(+).
Involved in the bacterial degradation of the herbicide bromoxynil.
3,5-dibromo-4-hydroxybenzonitrile + 2 H2O = 3,5-dibromo-4-hydroxybenzoate + NH4(+).
Preferentially hydrolyzes aliphatic nitriles, some of which are apparently not substrates for other known EC 3.5.5.1.
Substrates include crotononitrile, acrylonitrile and glutaronitrile.
an aliphatic nitrile + 2 H2O = a carboxylate + NH4(+).
The enzyme from Thiobacillus thioparus catalyzes the first step in the degradation of thiocyanate.
2 H(+) + H2O + thiocyanate = carbonyl sulfide + NH4(+).
H(+) + H2O + riboflavin = lumichrome + ribitol.
Previously known as thiaminase II, this enzyme is involved in the regeneration of the thiamine pyrimidine from degraded products, rather than in thiamine degradation, and participates in thiamine salvage pathways.
4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+).
H2O + thiamine = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole + H(+).
2-aminomuconate is an intermediate in the bacterial biodegradation of nitrobenzene.
The enzyme has been isolated from several species, including Pseudomonas pseudocaligenes JS45, Pseudomonas fluorescens KU-7, Pseudomonas sp. AP3 and Burkholderia cenocepacia J2315.
The reaction is spontaneous in acid conditions.
(2Z,4E)-2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate + NH4(+).
Isomerization of the aldose-ketose type converts the -CH(-NH2)-CH=O group of glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol which then hydrolyzes to yield fructose 6-phosphate and ammonia.
N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme.
alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+).
1-aminocyclopropane-1-carboxylate deaminase
1-aminocyclopropane-1-carboxylate endolyase (deaminating)
1-aminocyclopropane carboxylic acid deaminase
The enzyme, found in certain soil bacteria and fungi, catalyzes the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes.
The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination.
The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH4(+).
The enzyme catalyzes the initial step in biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329.
5-nitroanthranilate + H(+) + H2O = 5-nitrosalicylate + NH4(+).
The enzyme catalyzes the initial step in the biodegradation of 2-nitroimidazole by the soil bacterium Mycobacterium sp. JS330.
2-nitroimidazole + H2O = 1,3-dihydro-2H-imidazol-2-one + H(+) + nitrite.
2-iminobutanoate/2-iminopropanoate deaminase
This enzyme, which has been found in all species and tissues examined, catalyzes the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19 and EC 4.3.1.17.
The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates.
2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+).
2-iminopropanoate + H2O = NH4(+) + pyruvate.
2-aminomuconate deaminase (2-hydroxymuconate-forming)
The enzyme, characterized from the bacterium Comamonas testosteroni CNB-1, converts 2-aminomuconate to 2-hydroxyhexa-2,4-dienedioate, unlike the enzymes from Pseudomonas, which produce (3E)-2-oxohex-3-enedioate (see EC 3.5.99.5).
The enzyme also acts on 2-amino-5-chloromuconate.
(2Z,4E)-2-aminomuconate + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NH4(+).
Specificity varies with the source and with the activating metal ion.
The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9.
H2O + trimetaphosphate = 2 H(+) + triphosphate.
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates.
They differ from ATPases, which specifically hydrolyze ATP, by hydrolyzing both ATP and ADP.
Most of the ecto-ATPases that occur on the cell surface and hydrolyze extracellular nucleotides belong to this enzyme family.
a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate.
a 2'-deoxyribonucleoside 5'-triphosphate + 2 H2O = a 2'-deoxyribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate.
The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate.
Specificity depends on species and isoform.
a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate.
an acyl phosphate + H2O = a carboxylate + H(+) + phosphate.
The enzyme preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates.
In vitro the enzyme also acts as a nucleotidohydrolase on ADP, NAD(+), NADP(+), FAD, and CoA.
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+).
a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+).
The product contains 4 or 5 phosphate residues.
[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate.
[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate.
Also hydrolyzes dCDP to dCMP and phosphate.
adenosine diphosphoribose pyrophosphatase
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+).
Also acts on inosine tetraphosphate and tripolyphosphate but shows little or no activity with other nucleotides or polyphosphates.
adenosine 5'-tetraphosphate + H2O = ATP + H(+) + phosphate.
nucleoside-5-triphosphate phosphohydrolase
nucleoside triphosphate phosphohydrolase
The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate.
CDP-glycerol + H2O = CMP + 2 H(+) + sn-glycerol 3-phosphate.
bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)
diadenosine 5',5'''-P(1),P(4)-tetraphosphate asymmetrical hydrolase
diadenosinetetraphosphatase (asymmetrical)
diguanosinetetraphosphatase (asymmetrical)
dinucleosidetetraphosphatase (asymmetrical)
Also acts on bis(5'-xanthosyl)-tetraphosphate and, more slowly, on bis(5'-adenosyl)-tetraphosphate and bis(5'-uridyl)-tetraphosphate (cf. EC 3.6.1.41).
H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP + 2 H(+).
The plant enzyme also hydrolyzes NAD(+) and NADH; the animal enzyme hydrolyzes NAD(+) and CoA at about half of the rate of hydrolysis of FAD.
Also acts on inosine and uridine compounds.
5'-acylphosphoadenosine + H2O = a carboxylate + AMP + 2 H(+).
Has a distinct specificity from EC 3.6.1.45.
ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate.
nicotinamide adenine dinucleotide pyrophosphatase
This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences.
Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogs of NAD(+) and NADP(+).
H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2 H(+).
H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-ribonucleotide.
desoxyuridine 5'-triphosphate nucleotidohydrolase
Attacks ribonucleoside 5'-nitrophenylphosphates, but is inactive against phosphodiesters.
Hydrolyzes mixed phospho-anhydride bonds.
H2O + triphosphate = diphosphate + phosphate.
CDP-diacylglycerol phosphatidylhydrolase
a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+).
undecaprenyl-diphosphate phosphohydrolase
undecaprenyl pyrophosphate pyrophosphatase
Isolated from the bacteria Micrococcus lysodeikticus, Escherichia coli and Bacillus subtilis.
The product of the reaction, ditrans,octacis-undecaprenyl phosphate, is essential for cell wall polysaccharide biosynthesis in these strains.
di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate.
H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate.
diadenosine 5',5'''-P(1),P(3)-triphosphate hydrolase
H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H(+).
phosphoribosyladenosine triphosphate pyrophosphatase
The Neurospora crassa enzyme also catalyzes the reactions of EC 1.1.1.23 and EC 3.5.4.19.
1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+).
Also acts, more slowly, on dUTP and UTP.
guanosine-5'-triphosphate,3'-diphosphate diphosphatase
guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
guanosine pentaphosphate phosphohydrolase
Also hydrolyzes other guanosine 5'-triphosphate derivatives with at least one unsubstituted phosphate group on the 3'-position, but not GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate.
guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine 3',5'-bis(diphosphate) + H(+) + phosphate.
bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
diadenosine 5',5'''-P(1),P(4)-tetraphosphate pyrophosphohydrolase
diadenosinetetraphosphatase (symmetrical)
dinucleosidetetraphosphatase (symmetrical)
Also acts on bis(5'-guanosyl) tetraphosphate and bis(5'-adenosyl) pentaphosphate, and, more slowly, on some other polyphosphates, forming a nucleoside bisphosphate as one product in all cases (cf. EC 3.6.1.17).
H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+).
H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = 2 GDP + 2 H(+).
H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP + 2 H(+).
Also acts on UDP but not on other nucleoside diphosphates and triphosphates.
a dolichyl diphosphate + H2O = a dolichyl phosphate + H(+) + phosphate.
oligosaccharide-diphosphodolichol diphosphatase
oligosaccharide-diphosphodolichol pyrophosphatase
a dolichyl diphosphooligosaccharide + H2O = a dolichyl phosphate + an oligosaccharide-(1->4)-N-acetyl-beta-D-glucosamine-(1->4)-N-acetyl-alpha-D-glucosamine 1-phosphate + 2 H(+).
nucleosidediphosphate-sugar diphosphatase
nucleosidediphosphate-sugar pyrophosphatase
UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities.
Thus, this enzyme has a specificity distinct from that of EC 3.6.1.21.
Some but not all enzymes of this class also appear to have EC 3.1.3.5 activity.
UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.
diphosphoinositol-polyphosphate diphosphatase
diphosphoinositol-polyphosphate phosphohydrolase
This enzyme hydrolyzes the diphosphate bond, leaving a phospho group where a diphospho group had been.
It can also act on bis(adenosine) diphosphate.
diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + H(+) + phosphate.
3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate + H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 2 H(+) + phosphate.
5-diphospho-1D-myo-inositol 1,3,4,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H(+) + phosphate.
Mn(2+)-dependent ADP-ribose/CDP-alcohol diphosphatase
Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase
ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolyzed.
CDP-choline + H2O = CMP + 2 H(+) + phosphocholine.
UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine diphosphatase
UDP-2,3-diacylglucosamine pyrophosphatase
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate phosphohydrolase
The enzyme catalyzes a step in the biosynthesis of lipid A.
H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP.
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H2O = a lipid X + 2 H(+) + UMP.
7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase
This enzyme hydrolyzes the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA.
It does not hydrolyze 2-hydroxy-dATP (cf. EC 3.6.1.56).
8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+).
(2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase
oxidized purine nucleoside triphosphatase
The enzyme hydrolyzes oxidized purine nucleoside triphosphates such as 2-hydroxy-dATP, thereby preventing their misincorporation into DNA.
It can also recognize 8-oxo-dGTP and 8-oxo-dATP, but with lower efficiency (cf. EC 3.6.1.55).
2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+).
UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase
The enzyme is involved in biosynthesis of pseudaminic acid.
H2O + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose = 2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose + H(+) + UDP.
The enzyme catalyzes the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage.
The preferred in vivo substrate is not known.
The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55).
Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolyzed with broad specificity.
The bifunctional enzyme NUDT5 also hydrolyzes ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13).
The human enzyme NUDT18 also hydrolyzes 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate.
8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate.
8-oxo-GDP + H2O = 8-oxo-GMP + H(+) + phosphate.
5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase
The enzyme removes (decaps) the N(7)-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides.
Decapping is an important process in the control of eukaryotic mRNA degradation.
The enzyme functions to clear the cell of cap structure following decay of the RNA body.
The nematode enzyme can also decap triply methylated substrates, 5'-(N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-[mRNA].
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP.
a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in mRNA + H2O = (N(2),N(2),N(7))-trimethyl-GMP + a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+).
diadenosine hexaphosphate hydrolase (AMP-forming)
A divalent cation is essential for activity.
The enzyme controls intracellular levels of P(1),P(5)-bis(5'-adenosyl)pentaphosphate and P(1),P(6)-bis(5'-adenosyl)hexaphosphate.
Weak activity with P(1),P(4)-bis(5'-adenosyl)tetraphosphate.
Marked preference for adenine over guanine nucleotides.
H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-pentaphosphate + AMP + 2 H(+).
H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = adenosine 5'-tetraphosphate + AMP + 2 H(+).
diadenosine hexaphosphate hydrolase (ATP-forming)
The enzyme hydrolyzes P(1),P(4)-bis(5-guanosyl) tetraphosphate very slowly (cf. EC 3.6.1.17).
H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = 2 ATP + 2 H(+).
H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP + 2 H(+).
5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase
Decapping of mRNA is a critical step in eukaryotic mRNA turnover.
The enzyme is unable to cleave a free cap structure (m(7)GpppG).
The enzyme from Vaccinia virus is synergistically activated in the presence of Mg(2+) and Mn(2+).
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP.
alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate + H(+).
The human enzyme also hydrolyzes GDP and dGDP, and to a lesser extent ITP, dITP and XTP.
The enzyme, characterized from the bacterium Escherichia coli, is specific for the pyrimidine nucleotides CTP and dCTP.
It also acts on 5-methyl-dCTP, 5-hydroxy-dCTP and 8-hydroxy-dGTP.
hypoxanthine/xanthine dNTP pyrophosphatase
The enzymes from the bacterium Escherichia coli and the archaea Methanococcus jannaschii and Archaeoglobus fulgidus are highly specific for XTP, dITP and ITP.
dihydroneopterin triphosphate diphosphatase
dihydroneopterin triphosphate pyrophosphohydrolase
The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants.
7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + diphosphate + H(+).
The enzyme, characterized from roses, is involved in a cytosolic pathway for the biosynthesis of free monoterpene alcohols that contribute to fragrance.
In vitro the enzyme also acts on (2E,6E)-farnesyl diphosphate.
(2E)-geranyl diphosphate + H2O = (2E)-geranyl phosphate + H(+) + phosphate.
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, catalyzes the hydrolysis of both 8-oxo-GTP and 8-oxo-dGTP, thereby preventing transcriptional and translational errors caused by oxidative damage.
Unlike EC 3.6.1.55, it removes only a single phosphate group.
The nucleoside diphosphate products are hydrolyzed further by EC 3.6.1.58.
8-oxo-GTP + H2O = 8-oxo-GDP + H(+) + phosphate.
8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate.
guaosine-5'-diphospho-5'-[DNA] diphosphatase
Aprataxin is a DNA-binding protein that catalyzes (among other activities) the 5' decapping of Gpp-DNA (formed by homologs of RtcB3 from the bacterium Myxococcus xanthus).
The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and eventual release.
The enzyme forms a 5'-phospho terminus that can be efficiently joined by 'classical' ligases.
The enzyme also possesses the activity of EC 3.6.1.71 and EC 3.6.1.72.
a 5'-end guanosine-5'-diphospho-5'-(2'-deoxyribonucleoside)-DNA + H2O = a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + GMP + 2 H(+).
adenosine-5'-diphospho-5'-[DNA] diphosphatase
Aprataxin is a DNA-binding protein involved in different types of DNA break repair.
The enzyme acts (among other activities) on abortive DNA ligation intermediates that contain an adenylate covalently linked to the 5'-phosphate DNA terminus.
It also acts when the adenylate is covalently linked to the 5'-phosphate of a ribonucleotide linked to a DNA strand, which is the result of abortive ligase activty on products of EC 3.1.26.4, an enzyme that cleaves RNA-DNA hybrids on the 5' side of the ribonucleotide found in the 5'-RNA-DNA-3' junction.
Aprataxin binds the adenylate group to a histidine residue within the active site, followed by its hydrolysis from the nucleic acid and eventual release, leaving a 5'-phosphate terminus that can be efficiently rejoined.
The enzyme also possesses the activities of EC 3.6.1.70 and EC 3.6.1.72.
a 5'-end adenosine-5'-diphospho-5'-(2'-deoxyribonucleoside)-DNA + H2O = a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + AMP + 2 H(+).
a 5'-end adenosine-5'-diphospho-5'-ribonucleoside-2'-deoxyribonucleotide-DNA + H2O = a 5'-end 5'-monophospho-ribonucleoside-2'-deoxyribonucleotide-DNA + AMP + 2 H(+).
DNA-3'-diphospho-5'-guanosine diphosphatase
Aprataxin is a DNA-binding protein that catalyzes (among other activities) the 3' decapping of DNA-ppG (formed by EC 6.5.1.8).
The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and its eventual release.
a 3'-end 2'-deoxyribonucleotide-3'-diphospho-5'-guanosine-DNA + H2O = a 3'-end 2'-deoxyribonucleotide 3'-phosphate-DNA + GMP + 2 H(+).
The enzyme, characterized from the bacterium Escherichia coli, preferentially hydrolyzes inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage.
By hydrolyzing these damaged nucleotides, the enzyme prevents their incorporation into RNA.
The enzyme, found in eukaryotes and some plus strand RNA viruses (e.g. alphavirus), is involved in mRNA capping.
Unlike the eukaryotic enzyme, the viral enzyme requires a purine in the first position of the mRNA.
The human enzyme is a multi domain protein that also has the activity of EC 2.7.7.50.
a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate.
The enzyme from Escherichia coli also catalyzes the reaction of EC 3.6.1.n3.
H2O + L-cysteinyl-tRNA(Pro) = H(+) + L-cysteine + tRNA(Pro).
The enzyme from Escherichia coli also catalyzes the reaction of EC 3.6.1.n2.
H2O + L-cysteinyl-tRNA(Cys) = H(+) + L-cysteine + tRNA(Cys).
adenosine 5'-phosphosulfate + H2O = AMP + 2 H(+) + sulfate.
3'-phosphoadenylyl sulfate + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + sulfate.
Acting on acid anhydrides; catalyzing transmembrane movement of substances
Acting on ATP; involved in cellular and subcellular movement
A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments.
They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily.
They include peroxin, which apparently is involved in Zellweger's syndrome.
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle.
Their molecular masses range from 25 to 600 kDa.
non-chaperonin molecular chaperone ATPase
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins.
They comprise a number of heat-shock-cognate proteins.
They are also active in clathrin uncoating and in the oligomerization of actin.
DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA.
Some of them unwind duplex DNA with a 3' to 5' polarity, other show 5' to 3' polarity or unwind DNA in both directions.
Some helicases unwind DNA as well as RNA.
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA.
Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity.
May be identical with EC 3.6.4.12 (DNA helicase).
Acting on GTP; involved in cellular and subcellular movement
This group comprises GTP-hydrolyzing systems, where GTP and GDP alternate in binding.
This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targeting adenylate cyclase and/or K(+) and Ca(2+) channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase.
Golf is instrumental in odor perception, transducin in vision and gustducin in taste recognition.
At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of EC 3.6.1.46.
Involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis.
In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyzes it in prokaryotes.
In eukaryotes, it is eIF-2 (150 kDa) that binds GTP.
In the elongation phase, the GTP-hydrolyzing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa).
EF-Tu and EF-1alpha catalyze binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyze the translocation of peptidyl-tRNA from the A-site to the P-site.
GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
An intrinsic activity of alpha-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others.
The enzyme is required for accurate and efficient protein synthesis under certain stress conditions.
May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly.
Binds to ribosomes in a GTP-dependent manner.
H2O + oxaloacetate = acetate + H(+) + oxalate.
Also acts on other 3,5- and 2,4-dioxo acids.
4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+).
Also acts on 3'-hydroxykynurenine and some other (3-arylcarbonyl)-alanines.
H2O + L-kynurenine = anthranilate + H(+) + L-alanine.
3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + L-alanine.
Also hydrolyzes other C-acylated phenols related to phloretin.
Isolated from the fungus Aspergillus niger and the bacteria Pantoea agglomerans and Eubacterium ramulus.
H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate.
Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate.
a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate.
Highly specific; does not act on pyruvate, oxaloacetate, maleylpyruvate, fumarylpyruvate or acetylacetone.
acetylpyruvate + H2O = acetate + H(+) + pyruvate.
Also acts on the product of the action of EC 1.1.3.18 on polyvinyl alcohols.
Involved in the bacterial degradation of polyvinyl alcohol.
H2O + nonane-4,6-dione = butanoate + H(+) + pentan-2-one.
2,6-dioxo-6-phenylhexa-3-enoate hydrolase
Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 by ring-fission at a -CO-C bond.
Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.
2,6-dioxo-6-phenylhexa-3-enoate + H2O = 2-oxopent-4-enoate + benzoate + H(+).
2-hydroxy-6-(2-hydroxyphenyl)-6-oxo-cis,cis-hexa-2,4-dienoate + H2O = 2-oxopent-4-enoate + salicylate.
2-hydroxymuconate-6-semialdehyde hydrolase
2-hydroxymuconate-semialdehyde hydrolase
The enzyme is involved in the degradation of catechols.
(2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = 2-oxopent-4-enoate + formate + H(+).
Highly specific; does not act on other dione derivatives of cyclohexane, cyclopentane or cycloheptane.
cyclohexane-1,3-dione + H2O = 5-oxohexanoate + H(+).
Highly specific; does not act on cyclohexanone or cyclohexane-1,3-dione as substrate.
cyclohexan-1,2-dione + H2O = 6-oxohexanoate + H(+).
This enzyme hydrolyzes the ring A acetate delta-lactone of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its attached methyl group in the form of acetaldehyde.
This is a key reaction in the contraction of the porphyrin-type tetrapyrrole ring and its conversion to a corrin ring in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway.
Co-precorrin-5A + H2O = acetaldehyde + Co-precorrin-5B + H(+).
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase
This enzyme catalyzes the third step in the aerobic degradation pathway of carbazole.
The effect of the presence of an amino group or hydroxyl group at the 2-position of the substrate is small.
(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = (2E)-2-hydroxypenta-2,4-dienoate + anthranilate + H(+).
2-hydroxy-6-oxonona-2,4-dienedioate hydrolase
This enzyme catalyzes a step in a pathway of phenylpropanoid compounds degradation.
The first step of the enzyme mechanism involves a reversible keto-enol tautomerization.
(2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + H(+) + succinate.
(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate + H(+).
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase
The enzyme is involved in the bacterial degradation of the steroid ring structure, and is involved in degradation of multiple steroids, such as testosterone, cholesterol, and sitosterol.
(1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate + H2O = (2Z,4Z)-2-hydroxyhexa-2,4-dienoate + 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate + H(+).
The bornane ring system is cleaved by a retro-Claisen reaction to give the enol of alpha-campholonate.
When separate from the enzyme the enol is tautomerised to the keto form as a 6:1 mixture of [(1S,3R)-2,2,3-trimethyl-4-oxocyclopentyl]acetate and [(1S,3S)-2,2,3-trimethyl-4-oxocyclopentyl]acetate.
bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate + H(+).
2,6-dihydroxypseudooxynicotine hydrolase
The enzyme, characterized from the soil bacterium Arthrobacter nicotinovorans, participates in nicotine degradation.
2,6-dihydroxypseudooxynicotine + H2O = 2,6-dihydroxypyridine + 4-(methylamino)butanoate + H(+).
The enzyme is involved in bacterial degradation of 5-substituted salicylates, including gentisate (5-hydroxysalicylate), 5-nitrosalicylate and 5-halosalicylates.
3-fumarylpyruvate + H2O = fumarate + H(+) + pyruvate.
6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase
6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase
The enzyme, which participates in the anaerobic benzoyl-CoA degradation pathway in certain organisms, catalyzes the addition of one molecule of water to the double bound of 6-oxocyclohex-1-ene-1-carbonyl-CoA followed by the hydrolytic C-C cleavage of the alicyclic ring.
6-oxocyclohex-1-ene-1-carbonyl-CoA + 2 H2O = 3-hydroxy-6-carboxyhexanoyl-CoA + H(+).
3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (decyclizing)
The enzyme, found in the bacterium Bacillus subtilis, is part of the myo-inositol degradation pathway leading to acetyl-CoA.
3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-D-glucuronate + H(+).
The enzyme, characterized from the bacterium Pseudomonas alcaligenes NCIMB 9867, catalyzes the hydrolysis of 3-maleylpyruvate, the ring-cleavage product of gentisate.
The enzyme can also act on a number of maleylpyruvate derivatives, such as (2E)-2-methyl-4,6-dioxohept-2-enedioate and (2E)-3-methyl-4,6-dioxohept-2-enedioate.
3-maleylpyruvate + H2O = H(+) + maleate + pyruvate.
Isolated from the bacteria Pseudomonas fluorescens, Pseudomonas sp. YGJ3 and Mycobacterium abscessus 103.
It reduces the antibiotic activity of 2,4-diacetylphloroglucinol.
2,4-diacetylphloroglucinol + H2O = 2-acetylphloroglucinol + acetate.
2-hydroxy-6-oxohepta-2,4-dienoate hydrolase
2-hydroxy-5-methylmuconate semialdehyde hydrolase
A bacterial enzyme that participates in the degradation of toluene and 2-nitrotoluene.
(2Z,4E)-2-hydroxy-6-oxohepta-2,4-dienoate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + acetate + H(+).
2,4-didehydro-3-deoxy-L-rhamnonate hydrolase
L-2,4-diketo-3-deoxyrhamnonate hydrolase
The enzyme, characterized from the bacterium Sphingomonas sp. SKA58, participates in an L-rhamnose degradation pathway.
2,4-didehydro-3-deoxy-L-rhamnonate + H2O = (S)-lactate + H(+) + pyruvate.
3-oxoisoapionate-4-phosphate transcarboxylase/hydrolase
The enzyme, which belongs to the RuBisCO-like-protein (RLP) superfamily, has been characterized from several bacterial species.
It participates in the degradation of D-apionate.
The reaction is initiated by decarboxylation to generate a stabilized enediolate intermediate, with the sequestered CO2 carboxylating the adjacent enediolate carbon atom.
The resulting 3-ketose-1-phosphate intermediate is hydrolyzed, as in the authentic RuBisCO-catalyzed reaction, to generate glycolate and 3-phospho-D-glycerate.
Stereospecificity of 3-oxoisoapionate 4-phosphate has not been determined.
3-oxoisoapionate 4-phosphate + H2O = (2R)-3-phosphoglycerate + glycolate + H(+).
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2 (see also EC 3.8.1.9, EC 3.8.1.10 and EC 3.8.1.11).
an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a halide anion + H(+).
a haloacetate + H2O = a halide anion + glycolate + H(+).
chloroacetate + H2O = chloride + glycolate + H(+).
fluoroacetate + H2O = fluoride + glycolate + H(+).
Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.
1-haloalkane + H2O = a halide anion + a primary alcohol + H(+).
1,2-dichloroethane + H2O = 2-chloroethanol + chloride + H(+).
Catalyzes the first step in the degradation of chlorobenzoate in Pseudomonas.
In many microorganisms, this activity comprises three separate enzymes, EC 6.2.1.33, EC 3.8.1.7 and EC 3.1.2.23.
4-chlorobenzoate + H2O = 4-hydroxybenzoate + chloride + H(+).
specific for dehalogenation at the 4-position.
Can dehalogenate substrates bearing fluorine, chlorine, bromine and iodine in the 4-position.
4-chlorobenzoyl-CoA + H2O = 4-hydroxybenzoyl-CoA + chloride + H(+).
Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria.
atrazine + H2O = chloride + H(+) + hydroxyatrazine.
Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2 (see also EC 3.8.1.2, EC 3.8.1.10 and EC 3.8.1.11).
an (R)-2-haloacid + H2O = a (2S)-2-hydroxycarboxylate + a halide anion + H(+).
2-haloacid dehalogenase (configuration-inverting)
DL-2-haloacid dehalogenase (inversion of configuration)
DL-2-haloacid halidohydrolase (inversion of configuration)
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2.
The enzyme from Pseudomonas sp. 113 acts on 2-haloalkanoic acids whose carbon chain lengths are five or less (see also EC 3.8.1.2, EC 3.8.1.9 and EC 3.8.1.11).
2-haloacid dehalogenase (configuration-retaining)
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (S)- and (R)-hydroxyalkanoic acids, respectively, with retention of configuration at C-2 (see also EC 3.8.1.2, EC 3.8.1.9 and EC 3.8.1.10).
an (S)-2-haloacid + H2O = a (2S)-2-hydroxycarboxylate + a halide anion + H(+).
an (R)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a halide anion + H(+).
Also acts on N-phospho-arginine and other phosphoamides.
Possibly identical with EC 3.1.3.9 or EC 3.1.3.16.
H2O + N-phosphocreatine = creatine + phosphate.
The enzyme, characterized from Gram-positive bacteria, hydrolyzes the phosphoramidate (P-N) bond of N(omega)-phospho-L-arginine residues in proteins and peptides that were phosphorylated by EC 2.7.14.1.
H2O + N(omega)-phospho-L-arginyl-[protein] = L-arginyl-[protein] + phosphate.
This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides.
The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most).
The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein.
The enzyme is also active on free phosphoramidate and peptide-bound phospholysine.
H2O + N(tele)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + phosphate.
H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-[protein] + phosphate.
H2O + N-sulfo-D-glucosamine = D-glucosamine + sulfate.
Also readily hydrolyzes aliphatic sulfamates with 3 to 8 carbons.
cyclohexylsulfamate + H2O = cyclohexylamine + sulfate.
2-phosphonoacetylaldehyde phosphonohydrolase
phosphonoacetylaldehyde phosphonohydrolase
This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken.
The mechanism is similar to that used by EC 4.1.2.13 to break a C-C bond.
H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate.
H2O + phosphonoacetate = acetate + H(+) + phosphate.
Highly specific for phosphonopyruvate as substrate.
The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid.
3-phosphonopyruvate + H2O = H(+) + phosphate + pyruvate.
H2O + trithionate = H(+) + sulfate + thiosulfate.
NAD(+) appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add; the reaction is completed when the substrate is rehydrogenated at C-4.
The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-sulfoquinovose.
2'-hydroxybiphenyl-2-sulfinate desulfinase
2-(2'-hydroxyphenyl)benzenesulfinate desulfinase
2-(2-hydroxyphenyl) benzenesulfinate:H2O hydrolase
2-(2-hydroxyphenyl)benzenesulfinate desulfinase
2-(2-hydroxyphenyl)benzenesulfinate hydrolase
2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase
dibenzothiophene desulfurization enzyme B
The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date.
2'-hydroxybiphenyl-2-sulfinate + H2O = biphenyl-2-ol + H(+) + sulfite.
3-sulfinopropanoyl-CoA + H2O = H(+) + propanoyl-CoA + sulfite.
The hyperthermophilic archaeon Acidianus sp. A1-3 obtains energy by the conversion of carbon disulfide to hydrogen sulfide, with carbonyl sulfide as an intermediate.
carbon disulfide + 2 H2O = CO2 + 2 H(+) + 2 hydrogen sulfide.
[CysO sulfur-carrier protein]-S-L-cysteine hydrolase
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in an L-cysteine biosynthesis pathway.
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-Cys + H2O = [CysO sulfur-carrier protein]-C-terminal Gly-Gly + H(+) + L-cysteine.
The enzyme, characterized from the bacterium Thiobacillus thioparus, catalyzes a step in the degradation pathway of thiocyanate.
This activity is also catalyzed by the archaeal EC 3.13.1.5.
carbonyl sulfide + H2O = CO2 + H(+) + hydrogen sulfide.
S-adenosyl-L-methionine hydrolase (adenosine-forming)
The enzyme, found in bacteria and archaea, catalyzes a nucleophilic attack of water at the C5' carbon of S-adenosyl-L-methionine to generate adenosine and L-methionine.
May be involved in regulating SAM levels in the cell.
(R)-S-adenosyl-L-methionine + H2O = adenosine + H(+) + L-methionine.
The enzyme, characterized from the methanogenic archaeon Methanocaldococcus jannaschii, binds an NAD(+) cofactor.
It participates in an alternative pathway for the regeneration of S-adenosyl-L-methionine from S-adenosyl-L-homocysteine that involves the deamination of the latter to S-inosyl-L-homocysteine.
H2O + S-inosyl-L-homocysteine = inosine + L-homocysteine.
a 2-oxocarboxylate + H(+) = an aldehyde + CO2.
(S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase
(2S)-2-acetolactate + H(+) = (R)-acetoin + CO2.
The enzyme has been characterized from the fungus Aspergillus terreus and from human macrophages.
H(+) + phenylglyoxylate = benzaldehyde + CO2.
The enzyme from Pseudomonas ovalis also catalyzes the reaction of EC 2.8.3.3.
H(+) + L-aspartate = beta-alanine + CO2.
Also catalyzes the decarboxylation of aminomalonate and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.
H(+) + L-valine = 2-methylpropan-1-amine + CO2.
The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
H(+) + L-glutamate = 4-aminobutanoate + CO2.
3-hydroxy-L-glutamate + H(+) = 4-amino-3-hydroxybutanoate + CO2.
meso-2,6-diaminoheptanedioate carboxy-lyase
H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine.
phosphoribosylaminoimidazole carboxylase
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
5-amino-1-ribosylimidazole 5-phosphate carboxylase
5-phosphoribosyl-5-aminoimidazole carboxylase
While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18 and EC 5.4.99.18.
5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+) = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2.
The enzyme from higher eukaryotes is identical with EC 2.4.2.10.
H(+) + orotidine 5'-phosphate = CO2 + UMP.
The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
Also acts on other aromatic L-amino acids, including L-tryptophan.
5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin.
3-sulfino-L-alanine + H(+) = CO2 + hypotaurine.
N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase
H(+) + N-[(R)-pantothenoyl]-L-cysteine = (R)-pantetheine + CO2.
This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction.
The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate.
GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate.
ITP + oxaloacetate = CO2 + IDP + phosphoenolpyruvate.
(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate.
3-dehydro-L-gulonate + H(+) = CO2 + L-xylulose.
H(+) + UDP-alpha-D-glucuronate = CO2 + UDP-alpha-D-xylose.
phosphopantothenoylcysteine decarboxylase
N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase
H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2.
4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III.
phosphoenolpyruvate carboxykinase (diphosphate)
phosphoenolpyruvate carboxykinase (pyrophosphate)
Also catalyzes the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.
diphosphate + oxaloacetate = CO2 + phosphate + phosphoenolpyruvate.
ribulose 1,5-bisphosphate carboxylase/oxygenase
ribulose 1,5-diphosphate carboxylase/oxygenase
ribulose bisphosphate carboxylase/oxygenase
ribulose diphosphate carboxylase/oxygenase
Will utilize O2 instead of CO2, forming 3-phospho-D-glycerate and 2-phosphoglycolate.
2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O.
3-hydroxypyruvate + H(+) = CO2 + glycolaldehyde.
carnitine + H(+) = 2-methylcholine + CO2.
3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2.
(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) = (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2.
aminocarboxymuconate-semialdehyde decarboxylase
The product rearranges non-enzymically to picolinate.
2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-aminomuconate 6-semialdehyde + CO2.
2,3-dihydroxybenzoate + H(+) = catechol + CO2.
2 glyoxylate + H(+) = 2-hydroxy-3-oxopropanoate + CO2.
In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.3.27, EC 4.2.1.20 and EC 5.3.1.24).
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O.
ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate.
H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine.
3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase
3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-carboxy-lyase
5-hydroxy-6-methylpyridine-3,4-dicarboxylate + H(+) = 3-hydroxy-2-methylpyridine-5-carboxylate + CO2.
6-methylsalicylate + H(+) = 3-methylphenol + CO2.
Also acts on tyrosine and other aromatic amino acids.
H(+) + L-phenylalanine = 2-phenylethylamine + CO2.
dihydroxyfumarate + H(+) = 2-hydroxy-3-oxopropanoate + CO2.
4,5-dihydroxyphthalate + H(+) = 3,4-dihydroxybenzoate + CO2.
Also decarboxylates other C14 to C16 oxo acids.
3-oxododecanoate + H(+) = 2-undecanone + CO2.
H(+) + L-methionine = 3-(methylsulfanyl)propanamine + CO2.
3,4,5-trihydroxybenzoate + H(+) = 1,2,3-trihydroxybenzene + CO2.
H2O + stipitatonate = CO2 + stipitatate.
4-hydroxybenzoate + H(+) = CO2 + phenol.
2,5-dihydroxybenzoate + H(+) = CO2 + hydroquinone.
3,4-dihydroxybenzoate + H(+) = catechol + CO2.
2,2-dialkylglycine decarboxylase (pyruvate)
L-alanine-alpha-ketobutyrate aminotransferase
Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and 1-aminocyclopentanecarboxylate.
2,2-dialkylglycine + H(+) + pyruvate = CO2 + dialkyl ketone + L-alanine.
a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2.
H(+) + uracil 5-carboxylate = CO2 + uracil.
H(+) + UDP-alpha-D-galacturonate = CO2 + UDP-beta-L-arabinopyranose.
5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase
Part of the 4-hydroxyphenylacetate degradation pathway in Escherichia coli C.
(3E,5R)-5-carboxy-2-oxohept-3-enedioate + H(+) = (4Z)-2-oxohept-4-enedioate + CO2.
3,4-dihydroxyphthalate + H(+) = 3,4-dihydroxybenzoate + CO2.
2-oxoglutarate + H(+) = CO2 + succinate semialdehyde.
(3S)-3-methyl-2-oxopentanoate carboxy-lyase
Acts on a number of 2-oxo acids, with a high affinity toward branched-chain substrates.
The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for biosynthesis of branched-chain fatty acids.
(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2.
3-methyl-2-oxobutanoate + H(+) = 2-methylpropanal + CO2.
4-methyl-2-oxopentanoate + H(+) = 3-methylbutanal + CO2.
(2R,3R)-tartrate + H(+) = (R)-glycerate + CO2.
H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde.
5-guanidino-2-oxopentanoate decarboxylase
2-oxo-5-guanidinopentanoate carboxy-lyase
2-oxo-5-guanidinopentanoate decarboxylase
2-oxo-5-guanidinovalerate alpha-ketoarginine decarboxylase
5-guanidino-2-oxopentanoate + H(+) = 4-guanidinobutanal + CO2.
2-aryl-2-methylmalonate + H(+) = 2-arylpropionate + CO2.
Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols.
The enzyme has been reported to accept multiple tautomeric forms.
However, careful analysis of the stability of the different tautomers, as well as characterization of the enzyme that produces its substrate, EC 5.3.2.6, showed that the actual substrate for the enzyme is (3E)-2-oxohex-3-enedioate.
(3E)-2-oxohex-3-enedioate + H(+) = 2-oxopent-4-enoate + CO2.
The mechanism appears to involve hydration of the acetylene and decarboxylation of the oxaloacetic acid formed, although free oxaloacetate is not an intermediate.
It is thus analogous to EC 4.2.1.71 in its mechanism.
acetylenedicarboxylate + H(+) + H2O = CO2 + pyruvate.
Does not decarboxylate pyruvate or phosphonopyruvate.
The enzyme appears to be oxygen-sensitive.
3-sulfopyruvate + H(+) = CO2 + sulfoacetaldehyde.
Reacts with dopamine to give the benzylisoquinoline alkaloid skeleton.
3-(4-hydroxyphenyl)pyruvate + H(+) = (4-hydroxyphenyl)acetaldehyde + CO2.
Unable to decarboxylate the D-isomer of threonine O-3-phosphate.
The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
H(+) + O-phospho-L-threonine = (R)-1-aminopropan-2-yl phosphate + CO2.
Catalyzes a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis.
Activated by the divalent cations Mg(2+), Ca(2+) and Mn(2+).
Pyruvate and sulfopyruvate can also act as substrates, but more slowly.
3-phosphonopyruvate + H(+) = CO2 + phosphonoacetaldehyde.
The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product.
4-hydroxyphenylacetate + H(+) = 4-methylphenol + CO2.
3,4-dihydroxyphenylacetate + H(+) = 4-methylcatechol + CO2.
L-dopachrome, L- or D-alpha-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12).
D-dopachrome + H(+) = 5,6-dihydroxyindole + CO2.
3-dehydro-L-gulonate-6-phosphate decarboxylase
3-dehydro-L-gulonate-6-phosphate carboxy-lyase
3-keto-L-gulonate 6-phosphate decarboxylase
Along with EC 5.1.3.22, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-phosphate.
N(4)-acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates.
In Acinetobacter baumannii it is cotranscribed with the neighboring dat gene that encodes EC 2.6.1.76, which can supply the substrate for the decarboxylase.
H(+) + L-2,4-diaminobutanoate = CO2 + propane-1,3-diamine.
malonyl-S-acyl-carrier protein decarboxylase
This enzyme comprises the beta and gamma subunits of EC 4.1.1.88 but is not present in EC 4.1.1.89.
It follows on from EC 2.3.1.187 and results in the regeneration of the acetylated form of the acyl-carrier-protein subunit of malonate decarboxylase.
The carboxy group is lost with retention of configuration.
H(+) + malonyl-[ACP] = acetyl-[ACP] + CO2.
biotin-independent malonate decarboxylase
malonate carboxy-lyase (biotin-independent)
Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.
This enzyme is a cytosolic protein that is biotin-independent.
The other type is a biotin-dependent, Na(+)-translocating enzyme that includes both soluble and membrane-bound components (cf. EC 7.2.4.4).
As free malonate is chemically rather inert, it has to be activated prior to decarboxylation.
In both enzymes, this is achieved by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-ACP.
The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side-chain as 2'-(5-triphosphoribosyl)-3'-dephospho-CoA rather than as phosphopantetheine 4'-phosphate.
The individual enzymes involved in carrying out the reaction of this enzyme complex are EC 2.3.1.187, EC 2.3.1.39 and EC 4.1.1.87.
The enzyme can use various vitamin-K derivatives, including menaquinol, but does not contain iron.
The mechanism appears to involve the generation of a strong base by oxygenation of vitamin K.
It catalyzes the post-translational carboxylation of glutamate residues of several proteins of the blood-clotting system.
9-12 glutamate residues are converted to 4-carboxyglutamate (Gla) in a specific domain of the target protein.
The 4-pro-S hydrogen of the glutamate residue is removed and there is an inversion of stereochemistry at this position.
2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol.
In the reverse direction the enzyme catalyzes the regioselective carboxylation of phenol into stoichiometric amounts of salicylate.
The enzyme also catalyzes the reversible decarboxylation of 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2,3-dihydroxybenzoate and 4-aminosalicylate.
H(+) + indole-3-carboxylate = CO2 + indole.
The enzyme catalyzes both the carboxylation and decarboxylation reactions.
However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide.
The enzyme is activated by carboxylic acids.
H(+) + pyrrole-2-carboxylate = 1H-pyrrole + CO2.
H2O + pyrrole-2-carboxylate = 1H-pyrrole + hydrogencarbonate.
The enzyme, which exists in all vertebrates, decarboxylates ethylmalonyl-CoA, a potentially toxic compound that is formed in low amounts by the activity of EC 6.4.1.2 and EC 6.4.1.3.
It prefers the S isomer, and can decarboxylate (R)-ethylmalonyl-CoA with lower efficiency.
(2S)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2.
(2R)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2.
(S)-methylmalonyl-CoA + H(+) = CO2 + propanoyl-CoA.
L-glutamyl-[BtrI acyl-carrier protein] decarboxylase
Has very low activity with substrates not bound to an acyl-carrier protein.
gamma-L-glutamyl-[BtrI ACP] + H(+) = 4-aminobutanoyl-[BtrI ACP] + CO2.
The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae.
The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro.
carboxynorspermidine + H(+) = CO2 + norspermidine.
carboxyspermidine + H(+) = CO2 + spermidine.
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans).
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2.
4-hydroxy-3-polyprenylbenzoate decarboxylase
3-octaprenyl-4-hydroxybenzoate decarboxylase
4-hydroxy-3-solanesylbenzoate decarboxylase
The enzyme catalyzes a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria.
The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism.
It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129.
a 4-hydroxy-3-all-trans-polyprenylbenzoate + H(+) = a 2-all-trans-polyprenylphenol + CO2.
4-hydroxy-3-all-trans-heptaprenylbenzoate + H(+) = 2-all-trans-heptaprenylphenol + CO2.
4-hydroxy-3-all-trans-octaprenylbenzoate + H(+) = 2-all-trans-octaprenylphenol + CO2.
4-hydroxy-3-all-trans-nonaprenylbenzoate + H(+) = 2-all-trans-nonaprenylphenol + CO2.
4-hydroxy-3-all-trans-decaprenylbenzoate + H(+) = 2-all-trans-decaprenylphenol + CO2.
4-hydroxy-3-all-trans-hexaprenylbenzoate + H(+) = 2-all-trans-hexaprenylphenol + CO2.
The enzyme participates in a mevalonate pathway that occurs in halophilic archaea.
The activity is also present in eubacteria of the Chloroflexi phylum.
(R)-5-phosphomevalonate + ATP = ADP + CO2 + isopentenyl phosphate + phosphate.
non-aromatizing prephenate decarboxylase
The enzyme isomerizes only the pro-R double bond in prephenate.
H(+) + prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2.
The enzyme is involved in the malolactic fermentation of wine, which results in a natural decrease in acidity and favorable changes in wine flavors.
It has been purified from several lactic acid bacteria, including Leuconostoc mesenteroides, Lactobacillus plantarum, and Oenococcus oeni.
The enzyme, found in fungi, catalyzes the decarboxylation of phenacrylic acids present in plant cell walls.
(E)-4-coumarate + H(+) = 4-hydroxystyrene + CO2.
(E)-ferulate + H(+) = 2-methoxy-4-vinylphenol + CO2.
The enzyme, characterized from several bacterial strains, is involved in the degradation of gamma-resorcylate.
The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction.
2,6-dihydroxybenzoate + H(+) = CO2 + resorcinol.
3-dehydro-4-phosphotetronate decarboxylase
3-dehydro-4-O-phospho-D-erythronate + H(+) = CO2 + dihydroxyacetone phosphate.
3-dehydro-4-O-phospho-L-erythronate + H(+) = CO2 + dihydroxyacetone phosphate.
The enzyme has been characterized from bacteria, plants, and fungi.
Unlike EC 4.1.1.28 this enzyme is specific for L-typtophan.
This algal enzyme, characterized from the green algae Chlorella variabilis and Chlamydomonas reinhardtii, is dependent on blue light, which photooxidizes its FAD cofactor.
The enzyme acts on fatty acids in the range of C12 to C22, with a higher efficiency for C16 to C17 chains, and forms an alkane product that is one carbon shorter than the substrate.
The enzyme can also act on unsaturated fatty acids, forming the respective alkenes, but does not generate a new double bond.
a long-chain fatty acid + H(+) + hnu = a long-chain alkane + CO2.
H(+) + hexadecanoate + hnu = CO2 + pentadecane.
3,4-dihydroxyphenylacetaldehyde synthase
The enzyme, isolated from the mosquito Aedes aegypti, catalyzes the production of 3,4-dihydroxylphenylacetaldehyde directly from L-dopa.
Dopamine is not formed as an intermediate (cf. EC 4.1.1.28).
The enzyme is specific for L-dopa and does not react with other aromatic amino acids with the exception of a low activity with alpha-methyl-L-dopa.
H(+) + H2O + L-dopa + O2 = 3,4-dihydroxyphenylacetaldehyde + CO2 + H2O2 + NH4(+).
The enzyme, isolated from the the plant Petroselinum crispum (parsley), catalyzes the production of 4-hydroxyphenylacetaldehyde directly from L-tyrosine.
Tyramine is not formed as an intermediate.
The enzyme has a low activity with L-dopa (cf. EC 4.1.1.107).
H(+) + H2O + L-tyrosine + O2 = (4-hydroxyphenyl)acetaldehyde + CO2 + H2O2 + NH4(+).
The enzyme, isolated from the the plants Petunia hybrida and a Rosa hybrid, catalyzes the production of phenylacetaldehyde directly from L-phenylalanine.
The enzyme is specific for L-phenylalanine and does not accept other aromatic amino acids as substrates.
H(+) + H2O + L-phenylalanine + O2 = 2-phenylacetaldehyde + CO2 + H2O2 + NH4(+).
mevalonate 3,5-bisphosphate decarboxylase
The enzyme participates in an alternative mevalonate pathway that takes place in extreme acidophiles of the Thermoplasmatales order.
cf. EC 4.1.1.99, phosphomevalonate decarboxylase.
(R)-3,5-bisphosphomevalonate + H(+) = CO2 + isopentenyl phosphate + phosphate.
The enzyme from archaea is involved in an alternative heme biosynthesis pathway.
The enzyme from denitrifying bacteria is involved in the heme d1 biosynthesis pathway.
2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2.
The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn(2+), while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg(2+).
Unlike EC 7.2.4.2, there is no evidence of the enzyme's involvement in Na(+) transport.
The enzyme, characterized from the smut fungus Ustilago maydis, is involved in an alternative pathway for the biosynthesis of itaconate.
H(+) + trans-aconitate = CO2 + itaconate.
cis-3-alkyl-4-alkyloxetan-2-one decarboxylase
The enzyme, found in certain bacterial species, catalyzes the last step in a pathway for the production of olefins.
a cis-3-alkyl-4-alkyloxetan-2-one = a cis-alkene + CO2.
This glycyl radical enzyme has been isolate from a number of bacterial species.
Skatole contributes to the characteristic smell of animal feces.
(indol-3-yl)acetate + H(+) = CO2 + skatole.
The enzyme, characterized from the bacterium Salmonella typhimurium LT2, is specific for D-ornithine and D-lysine.
2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate decarboxylase
The enzyme, characterized from the bacterium Staphylococcus aureus, participates in the biosynthesis of the siderophore staphyloferrin B.
2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate + H(+) = 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + CO2.
The enzyme, characterized from the bacterium Syntrophorhabdus aromaticivorans, participates in an anaerobic isophthalate degradation pathway.
The enzyme requires a prenylated flavin mononucleotide cofactor.
H(+) + isophthalyl-CoA = benzoyl-CoA + CO2.
This bacterial enzyme, isolated from anoxic, toluene-producing microbial communities, is a glycyl radical enzyme.
It needs to be activated by a dedicated activating enzyme (PhdA).
The activase catalyzes the reductive cleavage of AdoMet, producing a 5'-deoxyadenosyl radical that leads to the production of the glycyl radical in PhdB.
3-oxoisoapionate + H(+) = CO2 + L-erythrulose.
3-oxoisoapionate-4-phosphate decarboxylase
It belongs to the RuBisCO-like-protein (RLP) superfamily.
3-oxoisoapionate 4-phosphate + H(+) = CO2 + L-erythrulose 1-phosphate.
erythrulose-1-phosphate formaldehyde-lyase
L-erythrulose 1-phosphate = dihydroxyacetone phosphate + formaldehyde.
2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase
2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate.
This enzyme is specific for L-threonine and can not utilize L-allo-threonine.
Different from EC 4.1.2.49 and EC 4.1.2.48.
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate D-glyceraldehyde-3-phosphate-lyase
indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase
Forms part of the defense mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyzes one of the steps in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA).
Resembles the alpha-subunit of EC 4.2.1.20 but, unlike tryptophan synthase, its activity is independent of the beta-subunit and free indole is released.
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = D-glyceraldehyde 3-phosphate + indole.
D-xylulose-5-phosphate D-glyceraldehyde-3-phosphate-lyase (phosphate-acetylating)
D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O.
A variety of enzymes from different sources and with different properties.
Active toward a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
(R)-mandelonitrile = benzaldehyde + hydrogen cyanide.
(S)-4-hydroxymandelonitrile hydroxybenzaldehyde-lyase
Does not accept aliphatic hydroxynitriles, unlike EC 4.1.2.10, EC 4.1.2.46 and EC 4.1.2.47.
(S)-4-hydroxymandelonitrile = 4-hydroxybenzaldehyde + hydrogen cyanide.
2-dehydropantoate = 3-methyl-2-oxobutanoate + formaldehyde.
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
fructose-1,6-bisphosphate triosephosphate-lyase
Also acts on (3S,4R)-ketose 1-phosphates.
The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate.
2-dehydro-3-deoxy-phosphogluconate aldolase
2-dehydro-3-deoxy-D-gluconate-6-phosphate D-glyceraldehyde-3-phosphate-lyase
2-keto-3-deoxy-6-phosphogluconate aldolase
phospho-2-dehydro-3-deoxygluconate aldolase
phospho-2-keto-3-deoxygluconate aldolase
The enzyme shows no activity with 2-dehydro-3-deoxy-6-phosphate-D-galactonate (cf. EC 4.1.2.55).
2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-phosphate + pyruvate.
L-fuculose-1-phosphate lactaldehyde-lyase
L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate.
2-dehydro-3-deoxy-L-pentonate glycolaldehyde-lyase
2-dehydro-3-deoxy-L-arabinonate = glycolaldehyde + pyruvate.
L-rhamnulose-1-phosphate lactaldehyde-lyase
L-rhamnulose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate.
2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase
alpha-keto-beta-deoxy-D-glucarate aldolase
2-dehydro-3-deoxy-D-glucarate = 2-hydroxy-3-oxopropanoate + pyruvate.
2-dehydro-3-deoxy-6-phosphogalactonate aldolase
2-dehydro-3-deoxy-D-galactonate-6-phosphate D-glyceraldehyde-3-phosphate-lyase
2-dehydro-3-deoxyphosphogalactonate aldolase
2-oxo-3-deoxygalactonate 6-phosphate aldolase
6-phospho-2-dehydro-3-deoxygalactonate aldolase
6-phospho-2-keto-3-deoxygalactonate aldolase
The enzyme catalyzes the last reaction in a D-galactose degradation pathway.
2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde 3-phosphate + pyruvate.
D-fructose-6-phosphate D-erythrose-4-phosphate-lyase (phosphate-acetylating)
keto-D-fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose 4-phosphate + H2O.
3-deoxy-D-manno-octulosonate D-arabinose-lyase
3-deoxy-alpha-D-manno-oct-2-ulosonate = D-arabinose + pyruvate.
N,N-dimethylaniline-N-oxide formaldehyde-lyase
N,N-dimethylaniline N-oxide = formaldehyde + N-methylaniline.
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase
The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis.
The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8).
The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81.
The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15.
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.
L-threo-3-phenylserine benzaldehyde-lyase
L-threo-3-phenylserine = benzaldehyde + glycine.
sphinganine-1-phosphate palmitaldehyde-lyase
sphinganine 1-phosphate = hexadecanal + phosphoethanolamine.
sphing-4-enine 1-phosphate = (2E)-hexadecenal + phosphoethanolamine.
2-dehydro-3-deoxy-D-arabinonate = glycolaldehyde + pyruvate.
5-dehydro-2-deoxyphosphogluconate aldolase
5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase
phospho-5-dehydro-2-deoxygluconate aldolase
phospho-5-keto-2-deoxygluconate aldolase
6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate + dihydroxyacetone phosphate.
trimethylamine-N-oxide formaldehyde-lyase
H(+) + trimethylamine N-oxide = dimethylamine + formaldehyde.
(24R,24'R)-fucosterol-epoxide acetaldehyde-lyase
The insect enzyme is involved in the conversion of sitosterol into cholesterol.
(24R,24(1)R)-fucosterol epoxide = acetaldehyde + desmosterol.
4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase
(3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-carboxybenzaldehyde-lyase
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate 2-formylbenzoate-lyase
Involved, with EC 1.13.11.38, in the metabolism of phenanthrene in bacteria.
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H2O = 2-formylbenzoate + pyruvate.
2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase
D-tagatose-1,6-bisphosphate triosephosphate lyase
Enzyme activity is stimulated by certain divalent cations.
Involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria.
D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate.
Activated by divalent metal cations (e.g. Co(2+), Ni(2+), Mn(2+) or Mg(2+)).
The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine.
Several other D-beta-hydroxy-alpha-amino acids, such as D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4-dihydroxyphenylserine, can also act as substrate.
D-allothreonine = acetaldehyde + glycine.
D-arabino-3-hexulose 6-phosphate formaldehyde-lyase
Specific for formaldehyde and D-ribulose 5-phosphate as substrates.
Ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate.
This enzyme, along with EC 5.3.1.27, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds.
The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyzes the reactions of this enzyme and EC 5.3.1.27.
D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose 6-phosphate.
The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii.
The enzyme converts 2,3-epoxy-2,3-dihydrobenzoyl-CoA to its oxepin form prior to the ring-opening and the formation of a dialdehyde intermediate.
2,3-epoxy-2,3-dihydrobenzoyl-CoA + 2 H2O = (3Z)-6-oxohex-3-enoyl-CoA + formate + H(+).
trans-o-hydroxybenzylidenepyruvate hydratase-aldolase
The enzyme catalyzes a retro-aldol reaction in vitro, and it accepts a broad range of aldehydes and 4-substituted 2-oxobut-3-enoates as substrates.
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate + H2O = pyruvate + salicylaldehyde.
The enzyme catalyzes the stereoselective synthesis of aliphatic (R)-cyanohydrins.
No activity toward mandelonitrile and 4-hydroxymandelonitrile.
Natural substrates for the (R)-oxynitrilase from Linum usitatissimum are acetone and butan-2-one, which are the building blocks of the cyanogen glycosides in Linum, linamarin and lotaustralin, or linustatin and neolinustatin, respectively.
(2R)-2-hydroxy-2-methylbutanenitrile = butan-2-one + hydrogen cyanide.
(S)-cyanohydrin producing hydroxynitrile lyase
Hydroxynitrile lyases catalyzes the the cleavage of hydroxynitriles into cyanide and the corresponding aldehyde or ketone.
In nature the liberation of cyanide serves as a defense mechanism against herbivores and microbial attack in plants.
In vitro the enzymes from Manihot esculenta and Hevea brasiliensis accept a broad range of aliphatic and aromatic carbonyl compounds as substrates and catalyze the formation of (S)-hydroxynitriles.
a monosubstituted aliphatic (S)-hydroxynitrile = an aldehyde + hydrogen cyanide.
a disubstituted aliphatic (S)-hydroxynitrile = a ketone + hydrogen cyanide.
an aromatic (S)-hydroxynitrile = an aromatic aldehyde + hydrogen cyanide.
The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine.
The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine.
The enzyme can also catalyze the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis.
Different from EC 4.1.2.5 and EC 4.1.2.49.
L-allo-threonine = acetaldehyde + glycine.
This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine.
Different from EC 4.1.2.5 and EC 4.1.2.48.
A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1.
Isolated from the bacteria Bacillus subtilis and Escherichia coli.
The reaction is part of the biosynthesis pathway of queuosine.
The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin.
7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate.
The enzyme from the archaeon Picrophilus torridus is involved in D-glucose and D-galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway.
In the direction of aldol synthesis the enzyme catalyzes the formation of 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at a similar ratio.
It shows no activity with 2-dehydro-3-deoxy-D-gluconate 6-phosphate.
2-dehydro-3-deoxy-D-gluconate = D-glyceraldehyde + pyruvate.
The enzyme is also able to catalyze the aldol cleavage of 4-hydroxy-2-oxopentanoate and 4-hydroxy-2-oxohexanoate, and can use 2-oxobutanoate as carbonyl donor, with lower efficiency.
In the reverse direction, is able to condense a range of aldehyde acceptors with pyruvate.
The enzyme from the bacterium Escherichia coli produces a racemic mixture of (4R)- and (4S)-hydroxy-2-oxoheptanedioate.
4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde.
The enzyme can also use 2-oxo-3-deoxy-L-mannonate, 2-oxo-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) as substrates.
2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate.
2-dehydro-3-deoxy-L-galactonate = L-glyceraldehyde + pyruvate.
2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
In the archaeon Sulfolobus solfataricus the enzyme is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway.
It utilizes 2-dehydro-3-deoxy-6-phosphate-D-gluconate and 2-dehydro-3-deoxy-6-phosphate-D-galactonate with similar catalytic efficiency.
In vitro the enzyme can also catalyze the cleavage of the non-phosphorylated forms 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with much lower catalytic efficiency.
2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate synthase
Part of the pathway for the biosynthesis of grixazone, a mixture of yellow pigments produced by the bacterium Streptomyces griseus.
2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate = dihydroxyacetone phosphate + L-aspartate 4-semialdehyde.
6-deoxy-6-sulfo-D-fructose 1-phosphate = (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate.
2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase
2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate = (2S)-3-sulfolactaldehyde + pyruvate.
The enzyme participates in methanopterin biosynthesis the archaeon Pyrococcus furiosus.
The enzyme is specific for 7,8-dihydroneopterin 3'-phosphate.
7,8-dihydroneopterin 3'-phosphate = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde phosphate.
The enzyme, which participates in a pathway for folate biosynthesis, is found in the Stramenopiles, a large group that includes oomycetes, various microalgae and brown algae, as well as in several bacterial phyla.
It provides a bypass mechanism compensating for the lack of EC 4.1.2.25.
In the malaria parasite Plasmodium falciparum the enzyme is bifunctional and also catalyzes the activity of EC 4.2.3.12.
7,8-dihydroneopterin 3'-triphosphate = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde triphosphate.
The enzyme is a member of the enoyl-CoA hydratase/isomerase superfamily.
It catalyzes a two-step process involving first the hydration of the double bond of feruloyl-CoA and then the cleavage of the resultant beta-hydroxy thioester by retro-aldol reaction.
(E)-caffeoyl-CoA and (E)-4-coumaroyl-CoA are also substrates.
(E)-feruloyl-CoA + H2O = acetyl-CoA + vanillin.
(E)-4-coumaroyl-CoA + H2O = 4-hydroxybenzaldehyde + acetyl-CoA.
(E)-caffeoyl-CoA + H2O = 3,4-dihydroxybenzaldehyde + acetyl-CoA.
(E)-feruloyl-CoA + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA.
5-(methylthio)ribulose-1-phosphate aldolase
The enzyme, originally characterized from the bacterium Rhodospirillum rubrum, is involved in degradation pathways for 5'-deoxyadenosine and S-methyl-5'-thioadenosine, which are formed from S-adenosyl-L-methionine (SAM, AdoMet) by radical SAM enzymes and other types of SAM-dependent enzymes, respectively.
The enzyme requires a divalent metal cation, with Co(2+) producing the highest activity.
5-deoxy-D-ribulose 1-phosphate = acetaldehyde + dihydroxyacetone phosphate.
S-methyl-5-thio-D-ribulose 1-phosphate = 2-(methylsulfanyl)acetaldehyde + dihydroxyacetone phosphate.
This peroxisomal enzyme, found in animals, is involved in the alpha-oxidation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids.
a 2-hydroxy-3-methyl fatty acyl-CoA = a 2-methyl-branched fatty aldehyde + formyl-CoA.
an (R)-2-hydroxy-long-chain-fatty acyl-CoA = a long-chain fatty aldehyde + formyl-CoA.
2-hydroxyphytanoyl-CoA = 2,6,10,14-tetramethylpentadecanal + formyl-CoA.
2-hydroxy-3-methylhexadecanoyl-CoA = 2-methylpentadecanal + formyl-CoA.
The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate.
D-threo-isocitrate = glyoxylate + succinate.
This enzyme is involved in the degradation of N-acetylneuraminate.
It is specific for the open form of the sugar.
It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
aceneuramate = N-acetyl-D-mannosamine + pyruvate.
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase
(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA.
Can be dissociated into components, two of which are identical with EC 2.8.3.10 and EC 4.1.3.34.
EC 3.1.2.16 deacetylates and inactivates the enzyme.
3-oxalomalate = glyoxylate + oxaloacetate.
erythro-3-hydroxy-Ls-aspartate glyoxylate-lyase
(3R)-3-hydroxy-L-aspartate = glycine + glyoxylate.
4-hydroxy-2-oxoglutarate glyoxylate-lyase
The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate.
(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate.
(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate.
4-hydroxy-4-methyl-2-oxoglutarate aldolase
4-carboxy-4-hydroxy-2-oxoadipate aldolase
4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase
This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), phthalate, syringate and gallate.
The enzyme from Pseudomonas ochraceae can also cleave 4-hydroxy-2-oxoglutarate to glyoxylate and pyruvate, and also catalyzes the reaction of EC 4.1.1.3.
4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate.
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate.
Can be dissociated into components, two of which are identical with EC 2.8.3.11 and EC 4.1.3.25.
(3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase
The enzymes from Rhodobacter species catalyze a step in the ethylmalonyl-CoA pathway for acetate assimilation.
The enzyme from halophilic bacteria participate in the methylaspartate cycle and catalyze the reaction in the direction of malyl-CoA formation.
The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25.
(S)-malyl-CoA = acetyl-CoA + glyoxylate.
(2R,3S)-beta-methylmalyl-CoA = glyoxylate + propanoyl-CoA.
The enzyme from the bacterium Clostridium tetanomorphum is a component of EC 4.1.3.22.
It also acts on (3S)-citramalyl thioacyl-carrier protein.
The enzyme from the bacterium Chloroflexus aurantiacus also has the activity of EC 4.1.3.24.
It has no activity with (3R)-citramalyl-CoA (cf. EC 4.1.3.46).
(3S)-citramalyl-CoA = acetyl-CoA + pyruvate.
3-hydroxy-3-isohexenylglutaryl-CoA lyase
3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase
Also acts on the hydroxy derivative of farnesoyl-CoA.
3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 7-methyl-3-oxooct-6-enoyl-CoA + acetate.
The enzyme, found in plants, fungi and bacteria is composed of two parts, a glutaminase subunit and a lyase subunit.
The glutaminase produces ammonia that is channeled to the lyase subunit.
In the absence of the glutaminase, the lyase can convert ammonia and chorismate into anthranilate.
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.2.1.20, and EC 5.3.1.24).
chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate.
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase
Acts on threo-Ds-2-methylisocitrate, but not on threo-Ds-isocitrate, threo-DL-isocitrate or erythro-Ls-isocitrate.
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.
(2R,3S)-2,3-dimethylmalate pyruvate-lyase
(2R,3S)-2,3-dimethylmalate = propanoate + pyruvate.
Also acts on (3S)-citryl thioacyl-carrier protein.
(3S)-citryl-CoA = acetyl-CoA + oxaloacetate.
(1-hydroxycyclohexan-1-yl)acetyl-CoA lyase
(1-hydroxycyclohexan-1-yl)acetyl-CoA cyclohexanone-lyase
(1-hydroxycyclohexan-1-yl)acetyl-CoA = acetyl-CoA + cyclohexanone.
o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)
This enzyme is involved in the synthesis of 1,4-dihydroxy-2-naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K2, in bacteria), phylloquinone (vitamin K1 in plants), and many plant pigments.
The coenzyme A group is subsequently removed from the product by EC 3.1.2.28.
2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O.
4-amino-4-deoxychorismate pyruvate-lyase
Forms part of the folate biosynthesis pathway.
Acts on 4-amino-4-deoxychorismate, the product of EC 2.6.1.85, to form p-aminobenzoate.
4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
4-hydroxy-2-oxopentanoate pyruvate-lyase
The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH.
In some bacterial species, the enzyme forms a bifunctional complex with EC 1.2.1.10.
The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43.
(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate.
Catalyzes the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria.
The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine.
chorismate = 4-hydroxybenzoate + pyruvate.
The enzyme, purified from the bacterium Paracoccus denitrificansy IFO 13301, is strictly D-specific as to the alpha-position of the substrate, but accepts both the threo and erythro forms at the beta-position.
The erythro form is a far better substrate (about 100 fold).
The enzyme can also accept D-allothreonine, D-threonine, erythro-3-phenyl-D-serine and threo-3-phenyl-D-serine.
Requires a divalent cation, such as Mg(2+), Mn(2+) or Co(2+).
(3S)-3-hydroxy-D-aspartate = glycine + glyoxylate.
(3R)-3-hydroxy-D-aspartate = glycine + glyoxylate.
The enzyme from the bacterium Escherichia coli is specific for the (S) enantiomer.
That enzyme is trifunctional, and also catalyzes the reactions of EC 4.1.1.3 and EC 4.1.2.14.
The enzyme from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39.
The enzymes form a bifunctional complex with EC 1.2.1.89 with a tight channel connecting the two subunits.
(S)-4-hydroxy-2-oxohexanoate = propanal + pyruvate.
tRNA 4-demethylwyosine synthase (AdoMet-dependent)
This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters.
Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine.
The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine.
The enzyme, found in several bacterial species is involved in biosynthesis of secondary products.
The enzyme from the bacterium Xanthomonas campestris pv. campestris also has the activity of EC 4.1.3.40.
chorismate = 3-hydroxybenzoate + pyruvate.
The enzyme, purified from the bacterium Chloroflexus aurantiacus, has no activity with (3S)-citramalyl-CoA (cf. EC 4.1.3.25).
(3R)-citramalyl-CoA = acetyl-CoA + pyruvate.
The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
Also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine and other 3-substituted amino acids.
H2O + L-tryptophan = indole + NH4(+) + pyruvate.
The enzyme cleaves a carbon-carbon bond, releasing phenol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
The enzyme also slowly catalyzes similar reactions with D-tyrosine, S-methyl-L-cysteine, L-cysteine, L-serine and D-serine.
H2O + L-tyrosine = NH4(+) + phenol + pyruvate.
A flavoprotein containing a second chromophore group.
Catalyzes the reactivation by light of irradiated DNA.
A similar reactivation of irradiated RNA is probably due to a separate enzyme.
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).
cyclobutadithymidine in DNA = a thymidine dimer in DNA.
Involved in the biosynthesis of alkanes.
The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C15 to C17 alkanes.
The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents.
The substrate for this enzyme is formed by EC 1.2.1.80.
a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-chain alkane + formate + H2O + 2 NADP(+).
H(+) + 2 NADPH + O2 + octadecanal = formate + H2O + heptadecane + 2 NADP(+).
A glycyl radical enzyme that is inhibited by benzyl alcohol, benzaldehyde, phenylhydrazine and is inactivated by oxygen.
3,4-dihydroxy-2-butanone-4-phosphate synthase
L-3,4-dihydroxybutan-2-one-4-phosphate synthase
The reaction involves an intramolecular skeletal rearrangement, with the bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4 being broken, C-4 being removed as formate and reconnection of C-3 and C-5.
The phosphorylated four-carbon product (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the biosynthesis of riboflavin.
D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+).
The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent.
In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.
This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack.
In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH(-)) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures.
The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases.
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).
a thymidine(6-4)thymidine in DNA = a thymidine dimer in DNA.
a cytidine(6-4)cytidine in DNA = a cytidine dimer in DNA + H(+).
a thymidine(6-4)cytidine in DNA = a thymine-cytidine dinucleotide in DNA.
a cytidine(6-4)thymidine in DNA = a cytidine-thymine dinucleotide in DNA.
The cluster is coordinated by 3 cysteines and an exchangeable SAM molecule.
The 5'-deoxy-adenosine radical formed after electron transfer from the [4Fe-4S] cluster to the S-adenosyl-L-methionine, initiates the repair by abstracting the C-6 hydrogen of the spore photoproduct lesion.
During the second part of the repair process the SAM molecule is regenerated.
(5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine in DNA = a thymidine dimer in DNA.
Geosmin is the cause of the characteristic smell of moist soil.
The N-terminal part of the enzyme is EC 4.2.3.22, germacradienol synthase, and forms germacradienol from FPP.
The C-terminal part of the enzyme catalyzes the conversion of germacradienol to geosmin via (1S,4aS,8aS)-8,10-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene.
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O = (-)-geosmin + acetone.
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol = (1S,4aS)-1,4a-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene + acetone.
(1S,4aS)-1,4a-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene + H2O = (-)-geosmin.
Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule.
The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate.
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + CO + formate + 3 H(+) + L-methionine.
The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce methionine and a 5-deoxyadenosin-5-yl radical that is crucial for the conversion of the substrate.
L-tyrosine + NADPH + S-adenosyl-L-methionine = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP(+).
The reaction is suggested to take place in several steps.
Schiff base formation, double bond migration and dephosphorylation followed by ring opening and closing to form a pyrrolidine ring, and finally dehydration to form the product 3-amino-4-hydroxybenzoate.
In the bacterium Streptomyces griseus the enzyme is involved in biosynthesis of grixazone, a yellow pigment that contains a phenoxazinone chromophore.
2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate = 3-amino-4-hydroxybenzoate + H(+) + 2 H2O + phosphate.
The enzyme catalyzes an early step in the biosynthesis of the molybdenum cofactor (MoCo).
The enzyme belongs to the superfamily of radical S-adenosyl-L-methionine (radical SAM) enzymes.
AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine.
The enzyme, purified from bacteria, is part of the anaerobic pathway for cobalamin biosynthesis.
It binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule.
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + AH2 + S-adenosyl-L-methionine = 5'-deoxyadenosine + 5-hydroxybenzimidazole + A + formate + 2 H(+) + L-methionine + NH4(+) + phosphate.
The enzymes from the bacteria Pseudomonas aeruginosa and Xenorhabdus nematophila are involved in the biosynthesis of paerucumarin and rhabduscin, respectively.
According to the proposed mechanism, the enzyme forms an imine intermediate composed of linked L-tyrosine and D-ribulose 5-phosphate, followed by loss of the phosphate group and formation of a beta-keto imine and keto-enol tautomerization.
This is followed by a C-C bond cleavage, the release of acetol, and a retro aldol type reaction that releases formaldehyde and forms the final product.
D-ribulose 5-phosphate + L-tyrosine = (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + formaldehyde + H(+) + H2O + hydroxyacetone + phosphate.
The enzymes from cyanobacteria that belong to the Stigonematales order participate in the biosynthesis of hapalindole-type alkaloids.
According to the proposed mechanism, the enzyme forms an imine intermediate composed of linked L-tryptophan and D-ribulose 5-phosphate, followed by loss of the phosphate group and formation of a beta-keto imine and keto-enol tautomerization.
Cf. EC 4.1.99.24, L-tyrosine isonitrile synthase.
D-ribulose 5-phosphate + L-tryptophan = (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + formaldehyde + H(+) + H2O + hydroxyacetone + phosphate.
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase
The reaction occurs in the right-to-left direction.
The other activity of the enzyme is EC 1.3.98.7.
[mycofactocin precursor peptide]-C-terminal glycyl-N-{[2-(4-hydroxyphenyl)ethenyl]-3-methylbutanamide} + AH2 + S-adenosyl-L-methionine = 5'-deoxyadenosine + [mycofactocin precursor peptide]-C-terminal glycyl-N-{5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-oxopyrrolidin-3-yl}acetamide + A + H(+) + L-methionine.
The enzyme catalyzes the reversible hydration of gaseous CO2 to carbonic acid, which spontaneously converts to hydrogencarbonate under neutral pH.
It is widespread and found in archaea, bacteria, and eukaryotes.
Three distinct classes exist, and appear to have evolved independently.
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate.
The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate.
cis-aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate.
D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H2O.
The enzyme shows no activity with D-gluconate.
D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O.
D-altronate = 2-dehydro-3-deoxy-D-gluconate + H2O.
D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O.
(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.
(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-oxopentanoate + H2O.
3-dehydroquinate = 3-dehydroshikimate + H2O.
(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate.
6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O.
With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74).
a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O.
a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O.
(Z)-2,3-didehydroadipyl-CoA + H2O = 3-hydroxyadipyl-CoA.
(3S)-hydroxy-3-methylglutaryl-CoA = 3-methyl-(2E)-glutaconyl-CoA + H2O.
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.
The alpha-subunit catalyzes the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8).
The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan.
In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24.
In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122).
That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan.
A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta-substituted alpha-L-amino acids and a variety of mercaptans.
L-homocysteine + L-serine = H2O + L,L-cystathionine.
The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430.
The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis.
In humans, the enzyme is a primary target for the environmental toxin Pb.
The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.
2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen.
L-arabinonate = 2-dehydro-3-deoxy-L-arabinonate + H2O.
The reaction is effectively irreversible, favoring oxopropanoate (malonic semialdehyde) and its tautomers.
Also acts on but-3-ynoate forming acetoacetate.
The mechanism appears to involve hydration of the acetylene to 3-hydroxypropenoate, which will spontaneously tautomerize to 3-oxopropanoate.
It is thus analogous to EC 4.1.1.78 in its mechanism.
Two different forms of the enzyme have been described.
One form requires a cobamide coenzyme, while the other is a glycyl radical enzyme.
The cobamide-dependent enzyme has been shown to also dehydrate ethylene glycol to acetaldehyde.
Exists in an inactive low-molecular form, which is converted into active enzyme in the presence of Fe(2+) and thiol (cf. EC 4.2.1.81).
Forms part of the leucine-biosynthesis pathway.
Brings about the interconversion of the two isomers of isopropylmalate.
(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.
(3R)-citramalate = 2-methylmaleate + H2O.
2-methylmaleate + H2O = (2R,3S)-3-methylmalate.
2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase
The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyze the reaction shown above but cannot catalyze the previously described reaction, i.e. formation of homocitrate by hydration of cis-homoaconitate.
The enzyme responsible for the conversion of cis-homoaconitate into homocitrate in T.thermophilus is unknown at present but the reaction can be catalyzed in vitro using EC 4.2.1.3 from pig.
(2R,3S)-homoisocitrate = cis-homoaconitate + H2O.
The enzyme shows no activity with D-galactonate.
D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O.
D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O.
5-dehydro-4-deoxy-D-glucarate + H(+) = 2,5-dioxopentanoate + CO2 + H2O.
The enzyme from the bacterium Escherichia coli is specific for galactarate, while the enzyme from Salmonella typhimurium also has activity with L-talarate (cf. EC 4.2.1.156).
galactarate = 5-dehydro-4-deoxy-D-glucarate + H2O.
2-dehydro-3-deoxy-L-arabinonate dehydratase
2-keto-3-deoxy-L-arabinonate dehydratase
2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O.
scyllo-inosose = 3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O.
CDP-D-glucose = CDP-4-dehydro-6-deoxy-D-glucose + H2O.
dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.
guanosine 5'-diphosphate-D-mannose oxidoreductase
guanosine diphosphomannose 4,6-dehydratase
guanosine diphosphomannose oxidoreductase
Forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-alpha-L-fucose.
In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281.
GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O.
Also acts on various derivatives of D-glutamate.
4-imidazolone-5-propanoate = H2O + trans-urocanate.
L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + H2O.
H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O.
(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O.
A bacterial enzyme that is involved in propanoate fermentation (also known as the acrylate pathway).
Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein.
(3R)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O.
(3S)-citramalyl-CoA = H2O + itaconyl-CoA.
Also acts on dimethylacryloyl-CoA and farnesoyl-CoA.
3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + H2O.
3-hydroxyacyl-[acyl-carrier-protein] dehydratase
(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase
3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase
beta-hydroxyoctanoyl-acyl carrier protein dehydrase
beta-hydroxyoctanoyl thioester dehydratase
D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase
This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria.
The enzyme uses fatty acyl thioesters of ACP in vivo.
Different forms of the enzyme may have preferences for substrates with different chain length.
For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length.
Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14.
Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0).
FabZ, but not FabA, can also accept unsaturated substrates.
a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O.
5alpha-ergosta-7,22-diene-3beta,5-diol = ergosterol + H2O.
D-fuconate = 2-dehydro-3-deoxy-D-fuconate + H2O.
L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O.
While the enzymes from Tetrahymena pyriformis and Agrobacterium tumefaciens produce pseudouridine 5'-phosphate the enzyme from Escherichia coli functions as a pseudouridine-5'-phosphate glycosidase in vivo.
D-ribose 5-phosphate + uracil = H2O + psi-UMP.
protoaphin-aglucone dehydratase (cyclizing)
The product is converted non-enzymically to erythroaphin, an aphid pigment.
protoaphin aglucone = H2O + xanthoaphin.
The best substrate for the porcine enzyme is oct-2-enoyl-CoA.
Unlike EC 4.2.1.17 does not act on crotonoyl-CoA.
a medium-chain (3S)-3-hydroxyacyl-CoA = a medium-chain (2E)-enoyl-CoA + H2O.
hydroxymethylbilane hydro-lyase (cyclizing)
In the presence of EC 2.5.1.61, forms uroporphyrinogen III from porphobilinogen.
hydroxymethylbilane = H2O + uroporphyrinogen III.
UDP-alpha-D-glucose = H2O + UDP-4-dehydro-6-deoxy-alpha-D-glucose.
trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O.
The reaction makes a 6-membered ring by forming a bond between C-6 of the 3,4-dihydroxyphenyl group of the dopamine and C-1 of the aldehyde in the imine formed between the substrates.
The product is the precursor of the benzylisoquinoline alkaloids in plants.
Will also catalyze the reaction of 4-(2-aminoethyl)benzene-1,2-diol + (3,4-dihydroxyphenyl)acetaldehyde to form (S)-norlaudanosoline, but this alkaloid has not been found to occur in plants.
(4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine + H2O.
2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
Specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate.
Can also use cis-aconitate as a substrate but more slowly.
Both this enzyme and EC 4.2.1.3 are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate.
(2S,3S)-2-methylcitrate = 2-methyl-cis-aconitate + H2O.
The enzyme is involved in the catechol meta-cleavage pathway, a major mechanism for degradation of aromatic compounds.
Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer.
The enzyme was named when it was thought that the substrate is 2-oxopent-4-enoate.
However, it was later found that the actual substrate is its tautomer (2Z)-2-hydroxypenta-2,4-dienoate.
In some organisms the enzyme forms a complex with EC 4.1.1.77.
(S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-dienoate + H2O.
D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O.
This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), syringate and gallate, catalyzing the reaction in the opposite direction.
It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate.
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = 4-carboxy-2-hydroxy-cis,cis-muconate + H2O.
Acts on short-chain aliphatic nitriles, converting them into the corresponding acid amides.
Does not act on these amides or on aromatic nitriles (cf. EC 3.5.5.1).
(2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O.
The enzyme-catalyzed reaction is believed to be dehydration to an enamine, which is spontaneously hydrolyzed to an aldehyde and ammonia.
(R)-octopamine = (4-hydroxyphenyl)acetaldehyde + NH4(+).
Removal of H2O from (R)-synephrine produces a 2,3-enamine, which hydrolyzes to the products shown in the reaction above.
The enzyme from Arthrobacter synephrinum is highly specific.
(R)-synephrine = (4-hydroxyphenyl)acetaldehyde + methylamine.
L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O.
Also acts on prephenate and D-prephenyllactate.
H(+) + L-arogenate = CO2 + H2O + L-phenylalanine.
Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides.
The product of the above reaction is unstable and is acted upon by EC 5.3.99.6 to form the cyclopentenone derivative (15Z)-12-oxophyto-10,15-dienoate (OPDA), which is the first cyclic and biologically active metabolite in the jasmonate biosynthesis pathway.
(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O.
ATP-dependent NAD(P)H-hydrate dehydratase
Acts equally well on hydrated NADH and hydrated NADPH.
NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, to a 60:40 ratio.
Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H.
The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136).
(6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate.
(6S)-NADPHX + ATP = ADP + H(+) + NADPH + phosphate.
Involved with EC 1.1.1.252 in the biosynthesis of melanin in pathogenic fungi.
scytalone = 1,3,8-trihydroxynaphthalene + H2O.
The enzyme from Fusarium sp. hydrates the methylbutenyl side chain of the isoflavonoid phytoalexins, thus reducing their toxicity.
4a-hydroxytetrahydrobiopterin dehydratase
4alpha-hydroxy-tetrahydropterin dehydratase
In concert with EC 1.5.1.34 the enzyme recycles 4a-hydroxytetrahydrobiopterin back to tetrahydrobiopterin, a cosubstrate for several enzymes, including aromatic amino acid hydroxylases.
The enzyme is bifunctional, and also acts as a dimerization cofactor of hepatocyte nuclear factor-1alpha (HNF-1).
(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin = (6R)-L-erythro-6,7-dihydrobiopterin + H2O.
The enzyme from Fusarium solani, which is distinct from EC 4.2.1.95, hydrates the methylbutenyl side-chain of the isoflavonoid phytoalexin, phaseollidin.
phaseollidin hydrate = H2O + phaseollidin.
16alpha-hydroxyprogesterone dehydroxylase
16alpha-Hydroxypregnenolone is also a substrate.
16alpha-hydroxyprogesterone = 16,17-didehydroprogesterone + H2O.
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase
The enzyme from the fungus Yarrowia lipolytica does not act on isocitrate.
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O.
cyclohexa-1,5-dienecarbonyl-CoA hydratase
cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
cyclohexa-1,5-diene-1-carboxyl-CoA hydratase
Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.8.6, EC 1.3.7.8 and EC 4.2.1.55.
cyclohexa-1,5-diene-1-carbonyl-CoA + H2O = 6-hydroxycyclohex-1-ene-1-carbonyl-CoA.
The enzyme from Pseudomonas putida strain N19-2 can also catalyze the hydration of other isonitriles to the corresponding N-substituted formamides.
H(+) + N-cyclohexylformamide = cyclohexyl isocyanide + H2O.
This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen.
The reaction can be considered as the reverse of 'carbamate = cyanate + H2O', where this is assisted by reaction with bicarbonate and carbon dioxide, and hence is classified in sub-subclass 4.2.1.
Bicarbonate functions as a recycling substrate.
cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+).
Catalyzes the final step in the formation of the isoflavonoid skeleton.
(2R,3S)-2,4',7-trihydroxyisoflavanone = daidzein + H(+) + H2O.
2-hydroxy-2,3-dihydrogenistein = genistein + H(+) + H2O.
This enzyme, characterized from the gut bacterium Clostridium scindens (previously known as Eubacterium sp. strain VPI 12708), participates in the 7-dehydroxylation process associated with bile acid degradation.
7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oyl-CoA = 12alpha-hydroxy-3-oxochola-4,6-dien-24-oyl-CoA + H2O.
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase
Forms part of the rat peroxisomal multifunctional enzyme perMFE-2, which also exhibits a dehydrogenase activity.
Involved in the beta-oxidation of the cholesterol side chain in the cholic-acid biosynthesis pathway.
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-en-26-oyl-CoA + H2O.
Ectoine is an osmoprotectant that is found in halophilic eubacteria.
This enzyme is part of the ectoine biosynthesis pathway and only acts in the direction of ectoine formation.
(2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine.
methylthioribulose 1-phosphate dehydratase
This enzyme forms part of the methionine salvage pathway.
S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O.
1,5-anhydro-D-fructose dehydratase (microthecin-forming)
This enzyme catalyzes two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose.
Aldose-2-uloses such as 2-dehydroglucose can also act as substrates, but more slowly.
This is a bifunctional enzyme that acts as both a lyase and as an isomerase.
Differs from EC 4.2.1.111, which can carry out only reaction 1, is inhibited by its product and requires metal ions for activity.
1,5-anhydro-D-fructose = H2O + microthecin.
1,5-anhydro-D-arabino-hex-2-ulose dehydratase
Catalyzes one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose.
The other enzymes involved in this pathway are EC 4.2.1.110, EC 4.2.2.13 and EC 5.3.2.7.
Unlike EC 4.2.1.110 the enzyme is specific for 1,5-anhydro-D-fructose as substrate and shows no activity toward aldose-2-uloses such as 2-dehydroglucose; in addition, it is inhibited by its end-product ascopyrone M and it cannot convert the end-product ascopyrone M into microthecin, as can EC 4.2.1.110.
1,5-anhydro-D-fructose = ascopyrone M + H2O.
The tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct hydrophobic pocket.
Forms part of the vitamin-K biosynthesis pathway.
(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O.
Catalyzes several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea.
In contrast to EC 4.2.1.36, this enzyme can catalyze both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate.
In addition to cis-homoaconitate, the enzyme can also catalyze the hydration of the physiological substrates dihomoaconitate and trihomoaconitate as well as the non-physiological substrate tetrahomoaconitate.
cis-Aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme.
(2R)-homocitrate = (2R,3S)-homoisocitrate.
cis-(homo)2aconitate + H2O = (2R,3S)-iso(homo)2citrate.
cis-(homo)3aconitate + H2O = (2R,3S)-iso(homo)3citrate.
UDP-N-acetylglucosamine 4,6-dehydratase (inverting)
UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase
The first enzyme in the biosynthetic pathway of pseudaminic acid, a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin.
Plays a critical role in H.pylori's pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides.
Completely inhibited by UDP-alpha-D-galactose.
The reaction results in the chirality of the C-5 atom being inverted.
It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water.
UDP-N-acetyl-alpha-D-glucosamine = H2O + UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose.
The enzyme from Metallosphaera sedula acts nearly equally as well on (S)-3-hydroxybutanoyl-CoA but not (R)-3-hydroxybutanoyl-CoA.
3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O.
(3S)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O.
2-methylcitrate dehydratase (2-methyl-trans-aconitate forming)
Catalyzes the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate (unlike EC 4.2.1.79, which forms only the cis isomer).
Part of a propanoate degradation pathway.
The enzyme from Shewanella oneidensis can also accept citrate and cis-aconitate, but activity with (2S,3S)-2-methylcitrate was approximately 2.5-fold higher.
2-methylisocitrate and isocitrate were not substrates.
(2S,3S)-2-methylcitrate = 2-methyl-trans-aconitate + H2O.
Catalyzes an early step in the biosynthesis of petrobactin, a siderophore produced by many bacteria, including the human pathogen Bacillus anthracis.
3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O.
This enzyme catalyzes a hydration step in peroxisomal beta-oxidation.
The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units.
The enzymes from Aeromonas caviae and Arabidopsis thaliana are monofunctional enzymes.
2-enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2.
a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O.
The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation, Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation, and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea.
4-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O.
It catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid.
It forms also (8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid (i.e. colnelenate) from (9Z,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate.
The corresponding 13-hydroperoxides are poor substrates.
The divinyl ethers colneleate and colnelenate have antimicrobial activity.
(9S)-hydroperoxy-(10E,12Z)-octadecadienoate = colneleate + H2O.
(9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoate = colnelenate + H2O.
Most mesophilic bacteria have a multimeric tryptophan synthase complex (EC 4.2.1.20) that forms L-tryptophan from L-serine and 1-C-(indol-3-yl)glycerol 3-phosphate via an indole intermediate.
This intermediate, which is formed by the alpha subunits, is transferred in an internal tunnel to the beta units, which convert it to tryptophan.
In thermophilic organisms the high temperature enhances diffusion and causes the loss of indole.
This enzyme, which does not combine with the alpha unit to form a complex, salvages the lost indole back to L-tryptophan.
It has a much lower Km for indole than the beta subunit of EC 4.2.1.20.
arabidiol = (S)-2,3-epoxysqualene + H2O.
2,3-oxidosqualene (20S)-dammarenediol cyclase
dammarenediol-II = (S)-2,3-epoxysqualene + H2O.
N-acetylmuramic acid 6-phosphate etherase
This enzyme, along with EC 2.7.1.170, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria.
H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate.
In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyze in vitro two reactions, the dehydration of linalool to myrcene and the isomerization of geraniol to linalool (the latter activity is classified as EC 5.4.4.4).
The recombinant enzyme from Arabidopsis thaliana gives a 1:1 mixture of lupeol and lupan-3beta,20-diol with small amounts of beta-amyrin, germanicol, taraxasterol and psi-taraxasterol.
lupan-3beta,20-diol = (S)-2,3-epoxysqualene + H2O.
The enzyme produces the cyclization products hopene (cf. EC 5.4.99.17) and hopanol from squalene at a constant ratio of 5:1.
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step.
The other known route for this conversion is the two-step GSH-dependent pathway catalyzed by EC 4.4.1.5 and EC 3.1.2.6.
H2O + methylglyoxal = (R)-lactate + H(+).
In Rubrivivax gelatinosus and Thiocapsa roseopersicina both products are formed, whereas Rhodobacter capsulatus only gives 1-hydroxy-1,2-dihydrolycopene.
Also acts on neurosporene giving 1-hydroxy-1,2-dihydroneurosporene with both organisms but 1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene only with Rubrivivax gelatinosus.
1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene = H2O + rhodopin.
1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene = 1-hydroxy-all-trans-1,2-dihydro-neurosporene + H2O.
1-hydroxy-all-trans-1,2-dihydro-neurosporene = all-trans-neurosporene + H2O.
This enzyme catalyzes a late step in the bacterial steroid degradation pathway.
The product, 4-hydroxy-2-oxohexanoate, forms a 2-hydroxy-4-hex-2-enolactone under acidic conditions.
(2Z,4Z)-2-hydroxyhexa-2,4-dienoate + H2O = 4-hydroxy-2-oxohexanoate.
The enzyme was characterized from the plant Cistus creticus subsp. creticus.
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = 8-hydroxycopalyl diphosphate.
very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
This is the third component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long chain acyl CoAs.
a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O.
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)
This is the first enzyme in the biosynthetic pathway of N,N'-diacetylbacillosamine, the first carbohydrate in the glycoprotein N-linked heptasaccharide in Campylobacter jejuni.
This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes.
UDP-N-acetyl-alpha-D-glucosamine = H2O + UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose.
ADP-dependent NAD(P)H-hydrate dehydratase
(6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ADP-hydrolyzing; NADH-forming)
(6S)-beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ADP-hydrolyzing)
NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers.
The enzyme from bacteria consists of two domains, one of which acts as an NAD(P)H-hydrate epimerase that interconverts the two isomers to a 60:40 ratio (cf. EC 5.1.99.6), while the other catalyzes the dehydration.
Hence the enzyme can restore the complete mixture of isomers into NAD(P)H.
The enzyme has no activity with ATP, contrary to the enzyme from eukaryotes (cf. EC 4.2.1.93).
(6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate.
(6S)-NADPHX + ADP = AMP + H(+) + NADPH + phosphate.
Similar sesquarterpenoids are present in a number of Bacillus species.
sporulenol = (R)-tetraprenyl-beta-curcumene + H2O.
A multifunctional enzyme which also forms (+)-beta-caryophyllene from farnesyl diphosphate (EC 4.2.3.89).
(+)-(E)-beta-caryophyllene + H2O = (+)-caryolan-1-ol.
2',7-dihydroxy-4'-methoxyisoflavanol dehydratase
7,2'-dihydroxy-4'-methoxyisoflavanol dehydratase
The enzyme catalyzes the formation of the additional ring in pterocarpan, the basic structure of phytoalexins produced by leguminous plants, including (-)-medicarpin, (+)-medicarpin, (-)-maackiain and (+)-maackiain.
The enzyme requires that the hydroxyl group at C-4 of the substrate is in the (4R) configuration.
The configuration of the hydrogen atom at C-3 determines whether the pterocarpan is the (+)- or (-)-enantiomer.
The enzyme contains amino acid motifs characteristic of dirigent proteins.
a (4R)-4,2'-dihydroxyisoflavan = a pterocarpan + H2O.
(3R,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol = (-)-medicarpin + H2O.
(3S,4R)-7,2'-dihydroxy-4'-methoxyisoflavanol = (+)-medicarpin + H2O.
(3R,4R)-3-(6-hydroxy-1,3-benzodioxol-5-yl)-3,4-dihydro-2H-chromene-4,7-diol = (-)-maackiain + H2O.
(3R,4R)-7,2',4'-trihydroxyisoflavanol = (6aR,11aR)-3,9-dihydroxypterocarpan + H2O.
The enzyme is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway in Picrophilus torridus and via the branched variant of the Entner-Doudoroff pathway in Sulfolobus solfataricus.
In vitro it utilizes D-gluconate with 6-10 fold higher catalytic efficiency than D-galactonate.
2-dehydro-3-deoxy-D-arabinonate dehydratase
The enzyme participates in pentose oxidation pathways that convert pentose sugars to the tricarboxylic acid cycle intermediate 2-oxoglutarate.
2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O.
The enzyme also catalyzes the conversion of versiconal to versicolorin B (EC 4.2.1.143).
(S)-5'-oxoaverantin + H(+) = (1'S,5'S)-averufin + H2O.
(2S-3S)-versiconal hemiacetal = H2O + versicolorin B.
The enzyme from the bacterium Amycolatopsis mediterranei participates in the pathway for rifamycin B biosynthesis.
The enzyme also functions as a transaminase earlier in the pathway, producing UDP-alpha-D-kanosamine.
5-deoxy-5-amino-3-dehydroshikimate = 3-amino-5-hydroxybenzoate + H(+) + H2O.
(2S,3S)-hydroxyarginine = (2S,3R)-capreomycidine + H2O.
The enzyme takes part in a D-galacturonate degradation pathway in the fungi Trichoderma reesei (Hypocrea jecorina) and Aspergillus niger.
L-galactonate = 2-dehydro-3-deoxy-L-galactonate + H2O.
5,6,7,8-tetrahydromethanopterin hydro-lyase
Found in methylotrophic bacteria and methanogenic archaea.
5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O.
erythro-beta-methylmalonyl-CoA hydrolyase
The enzyme from the bacterium Chloroflexus aurantiacus is part of the 3-hydroxypropanoate cycle for carbon assimilation.
(2R,3S)-beta-methylmalyl-CoA = 2-methylfumaryl-CoA + H2O.
The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency.
(R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O.
The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents.
It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA.
a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain (2E)-enoyl-CoA + H2O.
chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O.
hydroperoxy icosatetraenoate dehydratase
The mammalian enzymes accept a range of hydroperoxy icosatetraenoates (HPETE).
The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency.
The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE).
The enzymes also catalyze the reaction of EC 5.4.4.7.
a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate + H2O.
(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-(5Z,9E,11Z,14Z)-eicosatetraenoate + H2O.
(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = 8-oxo-(5Z,9E,11Z,14Z)-eicosatetraenoate + H2O.
(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O.
(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O.
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O.
(3S)-citramalyl-CoA = 3-methylfumaryl-CoA + H2O.
H(+) + tetracenomycin F2 = H2O + tetracenomycin F1.
The enzyme is involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton.
Isolated from the bacterium Ruegeria pomeroyi.
3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + CO2 + CoA + methanethiol.
The enzyme, isolated from the bacteria Salmonella typhimurium and Polaromonas sp. JS666, also has activity with galactarate (cf. EC 4.2.1.42).
L-altrarate = 5-dehydro-4-deoxy-D-glucarate + H2O.
The enzyme, isolated from the bacterium Peptoclostridium difficile, is involved in the reductive branch of L-leucine fermentation.
It catalyzes an alpha/beta-dehydration, which depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI.
(R)-2-hydroxy-4-methylpentanoyl-CoA = 4-methylpent-2-enoyl-CoA + H2O.
galactarate dehydratase (D-threo-forming)
The enzyme has been characterized from the bacterium Oceanobacillus iheyensis.
galactarate = (2S,3R)-dihydroxy-5-oxohexanedioate + H2O.
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase
The enzyme participates in the biosynthesis of several deoxysugars, including beta-L-4-epi-vancosamine, alpha-L-megosamine, L- and D-olivose, D-oliose, D-mycarose, forosamine and beta-L-digitoxose.
In vitro the intermediate can undergo a spontaneous decomposition to maltol.
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O.
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one isomerase/dehydratase
The enzyme participates in a folate biosynthesis pathway in Chlamydia.
2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate = 7,8-dihydroneopterin 3'-phosphate + H2O.
In this pathway it catalyzes the introduction of hydroxyl groups to C3'' and C3''' of bisanhydrobacterioruberin to generate bacterioruberin.
bacterioruberin = bisanhydrobacterioruberin + 2 H2O.
6-deoxy-6-sulfo-D-gluconate = 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2O.
Part of a 4-hydroxyphenylacetate degradation pathway in Escherichia coli C.
(4Z)-2-oxohept-4-enedioate + H2O = (4S)-4-hydroxy-2-oxoheptanedioate.
dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase
TDP-4-keto-2,6-dideoxy-D-glucose 3-dehydrase
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized [2Fe-2S]-[ferredoxin].
The enzyme, together with EC 1.3.7.15 and EC 1.1.1.396, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a.
The enzyme catalyzes the hydration of a vinyl group on ring A, converting it to a hydroxyethyl group.
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a = chlorophyllide a + H2O.
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a = 3-deacetyl-3-vinylbacteriochlorophyllide a + H2O.
The enzyme, characterized from the bacterium Streptomyces viridochromogenes, is involved in bialaphos biosynthesis.
The similar enzyme EC 4.2.1.3 cannot catalyze this reaction.
phosphinomethylmalate = phosphinomethylisomalate.
The enzymes from the bacteria Acidaminococcus fermentans and Clostridium symbiosum are involved in the fermentation of L-glutamate.
The enzyme contains [4Fe-4S] clusters, FMNH2 and riboflavin.
It must be activated by a an activator protein.
Once activated, it can catalyze many turnovers.
(R)-2-hydroxyglutaryl-CoA = (2E)-glutaconyl-CoA + H2O.
GDP-4-dehydro-6-deoxy-alpha-D-mannose 3-dehydratase
This enzyme, involved in beta-L-colitose biosynthesis, is a unique vitamin-B6-dependent enzyme.
In the first step of catalysis, the bound pyridoxal phosphate (PLP) cafactor is transaminated to the pyridoxamine 5'-phosphate (PMP) form of vitamin B6, using L-glutamate as the amino group donor.
The PMP cofactor then forms a Schiff base with the sugar substrate and the resulting adduct undergoes a 1,4-dehydration to eliminate the 3-OH group.
Hydrolysis of the product from the enzyme restores the PLP cofactor and results in the release of an unstable enamine intermediate.
This intermediate tautomerizes to form an imine form, which hydrolyzes spontaneously, releasing ammonia and forming the final product.
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate = 2-oxoglutarate + GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NH4(+).
3-vinylbacteriochlorophyllide d 3(1)-hydratase
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is involved in the biosynthesis of bacteriochlorophylls c, d and e.
It acts it the direction of hydration, and the hydroxyl group that is formed is essential for the ability of the resulting bacteriochlorophylls to self-aggregate in the chlorosomes, unique light-harvesting antenna structures found in these organisms.
a bacteriochlorophyllide d = a 3-vinylbacteriochlorophyllide d + H2O.
2-(omega-methylthio)alkylmalate dehydratase
By catalyzing a dehydration of a 2-(omega-methylsulfanyl)alkylmaleate, followed by a hydration at a different position, the enzyme achieves the isomerization of its substrates.
The enzyme is a heterodimer comprising a large and a small subunits.
The large subunit can also bind to an alternative small subunit, forming EC 4.2.1.33, which participates in L-leucine biosynthesis.
a 2-(omega-methylsulfanyl)alkylmalate = a 2-(omega-methylsulfanyl)alkylmaleate + H2O.
a 3-(omega-methylsulfanyl)alkylmalate = a 2-(omega-methylsulfanyl)alkylmaleate + H2O.
2-(2-methylsulfanyl)ethylmalate = 2-(2-methylsulfanyl)ethylmaleate + H2O.
3-(2-methylsulfanyl)ethylmalate = 2-(2-methylsulfanyl)ethylmaleate + H2O.
2-(3-methylsulfanyl)propylmalate = 2-(2-methylsulfanyl)propylmaleate + H2O.
3-(3-methylsulfanyl)propylmalate = 2-(2-methylsulfanyl)propylmaleate + H2O.
cis-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O.
The enzyme has been characterized from the bacterium Peptoclostridium difficile.
The active form contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (SAM) and a [4Fe-4S] cluster.
trans-4-hydroxy-L-proline = (S)-1-pyrroline-5-carboxylate + H(+) + H2O.
ent-8alpha-hydroxylabd-13-en-15-yl diphosphate synthase
Isolated from the plant Salvia miltiorrhiza (red sage).
ent-8alpha-hydroxylabd-13-en-15-yl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + H2O.
Isolated from the plant Marrubium vulgare (white horehound).
peregrinol diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + H2O.
It is a heterodimeric protein consisting of the FldB and FldC polypeptides, both of which contain an [4Fe-4S] cluster, and forms a complex with EC 2.8.3.17.
In order to catalyze the reaction, the enzyme requires one high-energy electron that transiently reduces the electrophilic thiol ester carbonyl of the substrate to a nucleophilic ketyl radical anion, facilitating the elimination of the hydroxyl group.
This electron, which is provided by by EC 5.6.1.9, needs to be supplied only once, before the first reaction takes place, as it is regenerated at the end of each reaction cycle.
The enzyme acts on (R)-3-(aryl)lactoyl-CoAs produced by FldA, and regenerates the CoA donors used by that enzyme.
(R)-3-phenyllactoyl-CoA = (E)-cinnamoyl-CoA + H2O.
(R)-3-(4-hydroxyphenyl)lactoyl-CoA = (E)-4-coumaroyl-CoA + H2O.
(R)-3-(indol-3-yl)lactoyl-CoA = (E)-3-(indol-3-yl)acryloyl-CoA + H2O.
The enzyme, characterized from several bacterial species, is involved in an L-lyxonate degradation pathway.
L-lyxonate = 2-dehydro-3-deoxy-L-arabinonate + H2O.
The enzyme, characterized from the bacterium Klebsiella oxytoca, participates in (2S)-2,3-dihydroxypropane-1-sulfonate degradation.
The active form of the enzyme contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (AdoMet) and a [4Fe-4S] cluster.
(2S)-3-sulfopropanediol = 3-oxopropane-1-sulfonate + H2O.
The enzyme participates in an inulin degradation pathway, in which it forms inulobiose from difructose anhydride III.
A conformational change in the enzyme from the bacterium Pseudarthrobacter chlorophenolicus results in it also catalyzing the activity of EC 4.2.2.18.
inulobiose = alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,3'-dianhydride + H2O.
bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase
The enzyme, studied in the fungus Aspergillus fumigatus, may participate in an inulin degradation pathway in which it converts the product of EC 4.2.2.17 to inulobiose, though in vitro activity was higher in the direction of DFA-I formation.
bis-D-fructose 2',1:2,1'-dianhydride + H2O = inulobiose.
The enzyme catalyzes the degradation of hyaluronan by a beta-elimination reaction.
The product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose.
[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + H2O.
alpha-1,4-D-endopolygalacturonic acid lyase
endo-alpha-1,4-polygalacturonic acid lyase
Favors pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10).
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
The enzyme catalyzes the degradation of alginate by a beta-elimination reaction.
It cleaves the (1->4) bond between beta-D-mannuronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at the reducing end.
Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to four residues, with preference for shorter products.
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate.
In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region.
The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA.
GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS.
Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source.
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Also catalyzes eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.
4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate.
Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages.
Elimination of sulfate, appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.
exopolygalacturonic acid-trans-eliminase
The enzyme catalyzes the eliminative cleavage of an unsaturated disaccharide from the reducing end of homogalacturonan (the backbone of smooth regions of pectate, also known as de-esterified pectin).
[(1->4)-alpha-D-galacturonosyl](n) = 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate + [(1->4)-alpha-D-galacturonosyl](n-2).
Favors pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2).
Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
It cleaves the (1->4) bond between alpha-L-guluronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at the reducing end.
Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products.
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end.
Eliminative cleavage of the terminal beta-D-mannosyl-(1->4)-beta-D-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain.
alpha-1,4-glucan 1,5-anhydro-D-fructose eliminase
Catalyzes the sequential degradation of (1->4)-alpha-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose.
Thus, for an alpha-glucan containing n (1->4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose.
Maltose, maltosaccharides and amylose are all completely degraded.
Does not degrade (1->6)-alpha-gucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin.
Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110, EC 4.2.1.111 and EC 5.3.2.7.
linear alpha-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose.
Eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing)
Also acts on N-glycolylneuraminate glycosides.
Elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
levan fructotransferase (DFA-IV-forming)
2,6-beta-D-fructan D-fructosyl-D-fructosyltransferase (forming di-beta-D-fructofuranose 2,6':2',6-dianhydride)
This enzyme, like EC 4.2.2.17 and EC 4.2.2.18 eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride.
These enzymes have long been known as fructotransferases, so this is retained in the description (official name).
Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in enzyme class 4.-.-.-.
Produces di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
inulin fructotransferase (DFA-I-forming)
inulin D-fructosyl-D-fructosyltransferase (1,2':1',2-dianhydride-forming)
inulin D-fructosyl-D-fructosyltransferase (forming alpha-D-fructofuranose beta-D-fructofuranose 1,2':1',2-dianhydride)
inulin fructotransferase (depolymerizing, difructofuranose-1,2':2',1-dianhydride-forming)
inulin fructotransferase (DFA-I-producing)
This enzyme, like EC 4.2.2.16 and EC 4.2.2.18 eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride.
Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
inulin fructotransferase (DFA-III-forming)
inulin D-fructosyl-D-fructosyltransferase (1,2':2,3'-dianhydride-forming)
inulin D-fructosyl-D-fructosyltransferase (forming alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride)
inulin fructotransferase (depolymerizing, difructofuranose-1,2':2,3'-dianhydride-forming)
inulin fructotransferase (depolymerizing)
inulin fructotransferase (DFA-III-producing)
This enzyme, like EC 4.2.2.16 and EC 4.2.2.17 eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride.
Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
This is the only lyase that is known to be specific for dermatan sulfate as substrate.
The minimum substrate length required for catalysis is a tetrasaccharide.
Eliminative cleavage of dermatan sulfate containing (1->4)-beta-D-hexosaminyl and (1->3)-beta-D-glucurosonyl or (1->3)-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAc-4S).
Degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type.
Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate.
Keratan sulfate, heparan sulfate and heparin are not substrates.
The related enzyme EC 4.2.2.21 has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20.
Endolytic cleavage of (1->4)-beta-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta(4)-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta(4)-unsaturated tetra- and disaccharides.
The related enzyme EC 4.2.2.20 has the same substrate specificity but produces a mixture of oligosaccharides of different sizes that are ultimately degraded to tetra- and disaccharides.
Both enzymes act by the removal of a relatively acidic C-5 proton of the uronic acid followed by the elimination of a 4-linked hexosamine, resulting in the formation of an unsaturated C4-C5 bond on the hexuronic acid moiety of the products.
Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.
Differs in specificity from EC 4.2.2.9 as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end.
Disaccharides and tetrasaccharides may also be removed.
eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate.
alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase
The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168 and Aspergillus aculeatus.
Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosaccharides containing alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
The enzyme is highly specific to gellan, especially deacetylated gellan.
Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp.
The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left.
The enzyme catalyzes a beta-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
Cleavage of 4-deoxy-alpha-L-erythro-hex-4-enopyranuronoside oligosaccharides into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides.
The enzyme, isolated from the fungus Aspergillus giganteus, acts on the non-reducing end of methyl-esterified polygalacturonan, releasing either 4-deoxy(-)-L-threo-hex-4-enopyranuronate or 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate.
The enzyme is stimulated by divalent cations, with Co(2+) having the strongest effect.
It is able to act on substrates as short as a disaccharide, and was active on substrates with degrees of methyl esterification ranging between 34% and 90%.
[(1->4)-alpha-D-galacturonosyl methyl ester](n) = 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate + [(1->4)-alpha-D-galacturonosyl methyl ester](n-1).
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
peptidoglycan lytic endotransglycosylase
Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
H2O + O-phospho-L-homoserine = L-threonine + phosphate.
Also acts on D- (or L)-1-aminopropan-2-ol O-phosphate.
H2O + phosphoethanolamine = acetaldehyde + NH4(+) + phosphate.
Does not act on D-glyceraldehyde 3-phosphate.
dihydroxyacetone phosphate = methylglyoxal + phosphate.
The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products.
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate.
5-enolpyruvylshikimate-3-phosphate phospholyase
The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH.).
Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate.
(2E,6E)-farnesyl diphosphate = diphosphate + trichodiene.
The 9si hydrogen of farnesyl diphosphate undergoes a 1,2-hydride shift where it becomes the 1alpha hydrogen of pentalenene.
(2E,6E)-farnesyl diphosphate = diphosphate + pentalenene.
The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene.
(2E,6E,10E)-geranylgeranyl diphosphate = casbene + diphosphate.
trans,trans-farnesyl diphosphate aristolochene-lyase
The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene.
While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti (see also EC 4.2.3.23).
Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi.
(2E,6E)-farnesyl diphosphate = (+)-aristolochene + diphosphate.
(3R)-Linalyl diphosphate is an intermediate in the reaction.
(2E)-geranyl diphosphate + H2O = (1S,2S,4R)-endo-fenchol + diphosphate.
Both cis- and trans- isomers of sabinene hydrate are formed.
(2E)-geranyl diphosphate + H2O = diphosphate + sabinene hydrate.
Catalyzes triphosphate elimination and an intramolecular redox reaction.
The product is 6-pyruvoyltetrahydrobiopterin.
Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 3.5.4.16.
7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate.
The sesquiterpenoid (+)-delta-cadinene is an intermediate in phytoalexin biosynthesis.
(2E,6E)-farnesyl diphosphate = (1S,8aR)-delta-cadinene + diphosphate.
Mg(2+) is essentially ineffective as the divalent metal ion cofactor.
(2E)-geranyl diphosphate = beta-myrcene + diphosphate.
(2E)-geranyl diphosphate = (4S)-limonene + diphosphate.
This is the committed step in the biosynthesis of the diterpenoid antineoplastic drug Taxol (paclitaxel).
The cyclization involves a 1,5-hydride shift.
(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + taxa-4,11-diene.
Part of a bifunctional enzyme involved in the biosynthesis of abietadiene.
(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate.
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene.
ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene.
Forms the first step of carvone biosynthesis in caraway.
(2E)-geranyl diphosphate = (4R)-limonene + diphosphate.
vetispiradiene-forming farnesyl pyrophosphate cyclase
The initial internal cyclization produces the monocyclic intermediate germacrene A.
(2E,6E)-farnesyl diphosphate = (-)-vetispiradiene + diphosphate.
H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol.
Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate.
Both products are formed from a common intermediate.
The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16), a widely occurring metabolite of many streptomycetes, bacteria and fungi.
Also catalyzes the reaction of EC 4.2.3.75.
(2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate.
While germacrene A is an enzyme-bound intermediate in the biosynthesis of a number of phytoalexins, e.g. EC 4.2.3.9 from some species and EC 4.2.3.21, it is the sole sesquiterpenoid product formed in chicory.
(2E,6E)-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
A key enzyme in the biosynthesis of the antimalarial endoperoxide artemisinin.
Catalyzes the formation of both olefinic and oxygenated sesquiterpenes, with amorpha-4,11-diene being the major product.
When geranyl diphosphate is used as a substrate, no monoterpenes are produced.
(2E,6E)-farnesyl diphosphate = (+)-amorpha-4,11-diene + diphosphate.
Neither (S)- nor (R)-linalyl diphosphate can act as substrate for the enzyme from Clarkia breweri.
Unlike many other monoterpene synthases, only a single product, (3S)-linalool, is formed.
(2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate.
Geranyl diphosphate cannot be replaced by isopentenyl diphosphate, prenyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as substrate.
Unlike many other monoterpene synthases, only a single product, (3R)-linalool, is formed.
(2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate.
Located in the chloroplast of isoprene-emitting plants, such as poplar and aspen, and may be activitated by light-dependent changes in chloroplast pH and Mg(2+) concentration.
dimethylallyl diphosphate = diphosphate + isoprene.
This class I diterpene cyclase produces ent-cassa-12,15-diene, a precursor of the rice phytoalexins (-)-phytocassanes A-E. Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation.
ent-copalyl diphosphate = diphosphate + ent-cassa-12,15-diene.
ent-sandaracopimara-8(14),15-diene synthase
ent-sandaracopimaradiene is a precursor of the rice oryzalexins A-F.
Phytoalexins are diterpenoid secondary metabolites that are involved in the defense mechanism of the plant, and are produced in response to pathogen attack through the perception of elicitor signal molecules such as chitin oligosaccharide, or after exposure to UV irradiation.
As a minor product, this enzyme also forms ent-pimara-8(14),15-diene, which is the sole product of EC 4.2.3.30.
Ent-pimara-8(14),15-diene is not a precursor in the biosynthesis of either gibberellins or phytoalexins.
ent-copalyl diphosphate = diphosphate + ent-sandaracopimara-8(14),15-diene.
Unlike EC 4.2.3.29 which can produce both ent-sandaracopimaradiene and ent-pimara-8(14),15-diene, this diterpene cyclase produces only ent-pimara-8(14),15-diene.
ent-copalyl diphosphate = diphosphate + ent-pimara-8(14),15-diene.
Involved in the biosynthesis of the diterpenoid viguiepinol.
ent-copalyl diphosphate = diphosphate + ent-pimara-9(11),15-diene.
In Ginkgo, the enzyme catalyzes the initial cyclization step in the biosynthesis of ginkgolides, a structurally unique family of diterpenoids that are highly specific platelet-activating-factor receptor antagonists.
Levopimaradiene is widely distributed in higher plants.
In some species the enzyme also forms abietadiene, palustradiene, and neoabietadiene.
(+)-copalyl diphosphate = abieta-8(14),12-diene + diphosphate.
This diterpene cyclase produces stemar-13-ene, a putative precursor of the rice phytoalexin oryzalexin S.
9alpha-copalyl diphosphate = diphosphate + stemar-13-ene.
Catalyzes the committed step in the biosynthesis of the stemodane family of diterpenoid secondary metabolites, some of which possess mild antiviral activity.
Also produces stemod-12-ene and stemar-13-ene as minor products.
9alpha-copalyl diphosphate = diphosphate + stemod-13(17)-ene.
9beta-pimara-7,15-diene is a precursor of momilactones A and B, rice diterpenoid phytoalexins that are produced in response to attack (by a pathogen, elicitor or UV irradiation) and are involved in the defense mechanism of the plant.
Momilactone B can also act as an allochemical, being constitutively produced in the root of the plant and secreted to the rhizosphere where it suppresses the growth of neighboring plants and soil microorganisms.
9alpha-copalyl diphosphate = 9beta-pimara-7,15-diene + diphosphate.
Following on from EC 5.5.1.15, this enzyme completes the transformation of geranylgeranyl diphosphate (GGDP) into terpentetriene, which is a precursor of the diterpenoid antibiotic terpentecin.
Farnesyl diphosphate can also act as a substrate.
terpentedienyl diphosphate = diphosphate + terpentetriene.
The displacement of the diphosphate group of farnesyl diphosphate occurs with retention of configuration.
In the soil-dwelling bacterium Streptomyces coelicolor A3(2), the product of this reaction is used by EC 1.14.13.106 to produce the sesquiterpene antibiotic albaflavenone.
(2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene + diphosphate.
While unlikely to encounter geranyl diphosphate (GDP) in vivo as it is localized to plastids, the enzyme can use GDP as a substrate in vitro to produce (+)-(4R)-limonene (cf. EC 4.2.3.20).
Induced as part of a defense mechanism in the grand fir Abies grandis as a response to stem wounding.
(2E,6E)-farnesyl diphosphate = (E,R)-alpha-bisabolene + diphosphate.
Similar to many other plant terpenoid synthases, this enzyme produces many products from a single substrate.
The predominant product is the cyclic sesquiterpenoid alcohol, 8-epi-cedrol, with minor products including cedrol and the olefins alpha-cedrene, beta-cedrene, (E)-beta-farnesene and (E)-alpha-bisabolene.
(2E,6E)-farnesyl diphosphate + H2O = diphosphate + epi-cedrol.
This sesquiterpenoid enzyme is constitutively expressed in the root, hydathodes and stigma of the plant Arabidopsis thaliana.
If the leaves of the plant are wounded, e.g. by cutting, the enzyme is also induced close to the wound site.
The sesquiterpenoids (E)-nerolidol and alpha-bisabolol are also produced by this enzyme as minor products.
(2E,6E)-farnesyl diphosphate = (Z)-gamma-bisabolene + diphosphate.
Also able to use farnesyl diphosphate and geranyl diphosphate.
geranylgeranyl diphosphate = diphosphate + elisabethatriene.
A bifunctional enzyme which also has EC 5.5.1.14 activity.
Aphidicolan-16beta-ol is a precursor of aphidicolin, a specific inhibitor of EC 2.7.7.7.
9alpha-copalyl diphosphate + H2O = aphidicolan-16beta-ol + diphosphate.
A multifunctional enzyme with EC 2.5.1.29 activity.
geranylgeranyl diphosphate = diphosphate + fusicocca-2,10(14)-diene.
The enzyme only gave isopimara-7,15-diene.
(+)-copalyl diphosphate = diphosphate + isopimara-7,15-diene.
(+)-copalyl diphosphate + H2O = diphosphate + phyllocladan-16alpha-ol.
(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene + diphosphate.
(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate.
The enzyme catalyzes a step in the formation of 4,8-dimethyl-1,3(E),7-nonatriene, a key signal molecule in induced plant defense mediated by the attraction of enemies of herbivores.
Nerolidol is a naturally occurring sesquiterpene found in the essential oils of many types of plants.
(2E,6E)-farnesyl diphosphate + H2O = (3S,6E)-nerolidol + diphosphate.
The enzyme catalyzes a step in the formation of (3E)-4,8-dimethyl-1,3,7-nonatriene, a key signal molecule in induced plant defense mediated by the attraction of enemies of herbivores.
(2E,6E)-farnesyl diphosphate + H2O = (3R,6E)-nerolidol + diphosphate.
(+)-alpha-santalene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
The enzyme synthesizes a mixture of sesquiterpenoids from (2Z,6Z)-farnesyl diphosphate.
Following dephosphorylation of (2Z,6Z)-farnesyl diphosphate, the (2Z,6Z)-farnesyl carbocation is converted to either the (6R)- or the (6S)-bisabolyl cations depending on the stereochemistry of the 6,1 closure.
The (6R)-bisabolyl cation will then lead to the formation of (+)-alpha-santalene (EC 4.2.3.50), while the (6S)-bisabolyl cation will give rise to (+)-endo-beta-bergamotene (see EC 4.2.3.53) as well as (-)-endo-alpha-bergamotene (see EC 4.2.3.54).
Small amounts of (-)-epi-beta-santalene are also formed from the (6R)-bisabolyl cation and small amounts of (-)-exo-alpha-bergamotene are formed from the (6S)-bisabolyl cation.
(2Z,6Z)-farnesyl diphosphate = (+)-alpha-santalene + diphosphate.
beta-phellandrene synthase (neryl-diphosphate-cyclizing)
The enzyme from Solanum lycopersicum has very poor affinity with geranyl diphosphate as substrate.
Catalyzes the formation of the acyclic myrcene and ocimene as major products in addition to beta-phellandrene.
neryl diphosphate = beta-phellandrene + diphosphate.
(4S)-beta-phellandrene synthase (geranyl-diphosphate-cyclizing)
Some (-)-alpha-phellandrene is also formed.
The reaction involves a 1,3-hydride shift.
(2E)-geranyl diphosphate = (-)-beta-phellandrene + diphosphate.
(+)-endo-beta-bergamotene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
The (6R)-bisabolyl cation will then lead to the formation of (+)-alpha-santalene (see EC 4.2.3.50), while the (6S)-bisabolyl cation will give rise to (-)-endo-alpha-bergamotene (see EC 4.2.3.54), as well as (+)-endo-beta-bergamotene.
(2Z,6Z)-farnesyl diphosphate = (+)-endo-beta-bergamotene + diphosphate.
(-)-endo-alpha-bergamotene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
The (6R)-bisabolyl cation will then lead to the formation of (+)-alpha-santalene (see EC 4.2.3.50), while the (6S)-bisabolyl cation will give rise to (+)-endo-beta-bergamotene (EC 4.2.3.53) as well as (-)-endo-alpha-bergamotene.
(2Z,6Z)-farnesyl diphosphate = (1S,5S,6S)-alpha-bergamotene + diphosphate.
The synthesis of (S)-beta-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps.
The first step is the cyclization to (S)-beta-bisabolene.
The second step is the isomerization to (S)-beta-macrocarpene (cf. EC 5.5.1.17, (S)-beta-macrocarpene synthase).
(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene + diphosphate.
(2E,6E)-farnesyl diphosphate = diphosphate + gamma-humulene.
(2E,6E)-farnesyl diphosphate = diphosphate + sibirene.
(2E,6E)-farnesyl diphosphate = diphosphate + longifolene.
(2E,6E)-farnesyl diphosphate = beta-himachalene + diphosphate.
(2E,6E)-farnesyl diphosphate = diphosphate + gamma-himachalene.
(2E,6E)-farnesyl diphosphate = alpha-himachalene + diphosphate.
Widely distributed in higher plants, cf. EC 4.2.3.89.
(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate.
As well as 61% longifolene the enzyme gives 15% of alpha-longipinene, 6% longicyclene and traces of other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate.
(2E,6E)-farnesyl diphosphate = diphosphate + germacrene C.
Initial cyclization gives (+)-germacrene A in an enzyme bound form which is not released to the medium.
(2E,6E)-farnesyl diphosphate = (+)-5-epi-aristolochene + diphosphate.
(-)-gamma-cadinene synthase [(2Z,6E)-farnesyl diphosphate cyclizing]
(2Z,6E)-farnesyl diphosphate = (-)-gamma-cadinene + diphosphate.
(2E,6E)-farnesyl diphosphate = (+)-cubenene + diphosphate.
In the bacteria Streptomyces and the liverwort Heteroscyphus the (+)-isomer is formed in contrast to higher plants where the (-)-isomer is formed.
(2E,6E)-farnesyl diphosphate + H2O = (+)-epicubenol + diphosphate.
(2E,6E)-farnesyl diphosphate = alpha-zingiberene + diphosphate.
(2E,6E)-farnesyl diphosphate = (+)-beta-selinene + diphosphate.
The recombinant enzyme from black peppermint (Mentha x piperita) gave a mixture of cis-muurola-3,5-diene (45%) and cis-muurola-4(14),5-diene (43%).
(2E,6E)-farnesyl diphosphate = cis-muurola-3,5-diene + diphosphate.
(2E,6E)-farnesyl diphosphate = cis-muurola-4(14),5-diene + diphosphate.
The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% beta-eudesmol, 16.8% 10-epi-gamma-eudesmol (cf. EC 4.2.3.84), 10% alpha-eudesmol (cf. EC 4.2.3.85), and 5.6% aristolene.
(2E,6E)-farnesyl diphosphate + H2O = beta-eudesmol + diphosphate.
The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% alpha-barbatene, 17.8% thujopsene (cf. EC 4.2.3.79) and 9.9% beta-chamigrene (cf. 4.2.3.78) plus traces of other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = (+)-alpha-barbatene + diphosphate.
(2E,6E)-farnesyl diphosphate + H2O = diphosphate + patchoulol.
(2E,6E)-farnesyl diphosphate = (1E,4E)-germacrene B + diphosphate.
Initial cyclization probably gives biyclogermacrene in an enzyme bound form which is not released to the medium.
The enzyme from Solidago canadensis also forms a small amount of (+)-gamma-gurjunene.
(2E,6E)-farnesyl diphosphate = (-)-alpha-gurjunene + diphosphate.
The recombinant enzyme from Vitis vinifera gave 49.5% (+)-valencene and 35.5% (-)-7-epi-alpha-selinene.
(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate.
Presilphiperfolan-8beta-ol is the precursor of botrydial, a phytotoxic sesquiterpene metabolite secreted by the fungus Botryotinia fuckeliana (Botrytis cinerea), the causal agent of gray mold disease in plants.
(2E,6E)-farnesyl diphosphate + H2O = diphosphate + presilphiperfolan-8beta-ol.
In Solidago canadensis the biosynthesis results in the pro-R hydrogen at C-1 of the farnesy diphosphate ending up at C-11 of the (-)-germacrene D.
With Streptomyces coelicolor the pro-S hydrogen at C-1 ends up at C-11 of the (-)-germacrene D.
(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate.
Initial cyclization gives germacrene C in an enzyme bound form which is not released to the medium.
(2E,6E)-farnesyl diphosphate = (+)-delta-selinene + diphosphate.
The formation of (+)-germacrene D involves a 1,2-hydride shift whereas for (-)-germacrene D there is a 1,3-hydride shift (see EC 4.2.3.75).
(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate.
The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% (+)-alpha-barbatene, 17.8% (+)-thujopsene and 9.9% (+)-beta-chamigrene plus traces of other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = (+)-beta-chamigrene + diphosphate.
(2E,6E)-farnesyl diphosphate = (+)-thujopsene + diphosphate.
The enzyme from Norway spruce produces longifolene as the main product (cf. EC 4.2.3.58).
alpha-longipinene constitutes about 15% of the total products.
(2E,6E)-farnesyl diphosphate = alpha-longipinene + diphosphate.
The enzyme synthesizes a mixture of sesquiterpenoids from (2E,6E)-farnesyl diphosphate.
As well as (-)-exo-alpha-bergamotene (74%) there were (E)-nerolidol (10%), (Z)-alpha-bisabolene (6%), (E)-beta-farnesene (5%) and beta-sesquiphellandrene (1%).
(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene + diphosphate.
As well as (+)-alpha-santalene, (-)-beta-santalene and (-)-exo-alpha-bergamotene are formed with traces of (+)-epi-beta-santalene.
(2E,6E)-farnesyl diphosphate = (+)-alpha-santalene + diphosphate.
As well as (-)-beta-santalene (+)-alpha-santalene and (-)-exo-alpha-bergamotene are formed with traces of (+)-epi-beta-santalene.
(2E,6E)-farnesyl diphosphate = (-)-beta-santalene + diphosphate.
The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% beta-eudesmol, 16.8% 10-epi-gamma-eudesmol, 10% alpha-eudesmol, and 5.6% aristolene.
(2E,6E)-farnesyl diphosphate + H2O = 10-epi-gamma-eudesmol + diphosphate.
(2E,6E)-farnesyl diphosphate + H2O = alpha-eudesmol + diphosphate.
The recombinant enzyme from Vitis vinifera forms 49.5% (+)-valencene (cf. EC 4.2.3.73) and 35.5% (-)-7-epi-alpha-selinene.
(2E,6E)-farnesyl diphosphate = (-)-7-epi-alpha-selinene + diphosphate.
The enzyme from Pogostemon cablin gives 13% alpha-guaiene as well as 37% (-)-patchoulol (see EC 4.2.3.70), 13% delta-guaiene (see EC 4.2.3.93), and traces of at least ten other sesquiterpenoids.
In Aquilaria crassna three clones of the enzyme gave about 80% delta-guaiene and 20% alpha-guaiene, with traces of alpha-humulene.
A fourth clone gave 54% delta-guaiene and 45% alpha-guaiene.
(2E,6E)-farnesyl diphosphate = alpha-guaiene + diphosphate.
Viridiflorene is the only product of this enzyme from Solanum lycopersicum.
(2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene.
A multifunctional enzyme which also converts the (+)-beta-caryophyllene to (+)-caryolan-1-ol (see EC 4.2.1.138).
(2E,6E)-farnesyl diphosphate = (+)-(E)-beta-caryophyllene + diphosphate.
The enzyme forms 5-epi-alpha-selinene possibly via germecrene A or a 1,6-hydride shift mechanism.
(2E,6E)-farnesyl diphosphate = 5-epi-alpha-selinene + diphosphate.
The enzyme gives 28% cubebol, 29% (-)-germacrene D, 10% (+)-delta-cadinene and traces of several other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate + H2O = cubebol + diphosphate.
The cloned enzyme from the melon, Cucumis melo, gave mainly delta- and gamma-cadinene with traces of several other sesquiterpenoids cf. EC 4.2.3.62 and EC 4.2.3.13.
(2E,6E)-farnesyl diphosphate = (+)-gamma-cadinene + diphosphate.
In Aquilaria crassna three clones of the enzyme gave about 80% delta-guaiene and 20% alpha-guaiene (see also EC 4.2.3.87).
The enzyme from Pogostemon cablin gives 13% delta-guaiene as well as 37% (-)-patchoulol (see EC 4.2.3.70), 13% alpha-guaiene (see EC 4.2.3.87), and traces of at least ten other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = delta-guaiene + diphosphate.
One of five sesquiterpenoid synthases in Pogostemon cablin (patchouli).
(2E,6E)-farnesyl diphosphate = diphosphate + gamma-curcumene.
The enzyme from Coprinus cinereus produces (-)-alpha-cuprenene with high selectivity.
(2E,6E)-farnesyl diphosphate = (-)-alpha-cuprenene + diphosphate.
The recombinent enzyme gives avermitilol (85%) plus traces of germacrene A, germacrene B and viridiflorol.
The (1S)-hydrogen of farnesyl diphosphate is retained.
(2E,6E)-farnesyl diphosphate + H2O = avermitilol + diphosphate.
The cyclization mechanism involves an intermediate nerolidyl diphosphate leading to a helminthogermacradienyl cation.
Following a 1,3-hydride shift of the original 1-pro-S hydrogen of (2E,6E)-farnesyl diphosphate, cyclization and deprotonation gives (-)-delta-cadinene.
(2E,6E)-farnesyl diphosphate = (-)-delta-cadinene + diphosphate.
After a 1,3-hydride shift of the original 1-pro-S hydrogen of farnesyl diphosphate, cyclization and deprotonation result in (+)-T-muurolol.
(2E,6E)-farnesyl diphosphate + H2O = (+)-T-muurolol + diphosphate.
The enzyme from rice (Oryza sativa), expressed in Escherichia coli, also produces ent-sandaracopimara-8(14),15-diene from ent-copalyl diphosphate, another naturally occurring copalyl isomer in rice (cf. EC 4.2.3.29).
9alpha-copalyl diphosphate = (12E)-9alpha-labda-8(17),12,14-triene + diphosphate.
The enzyme from oregano (Origanum vulgare) gives mainly bicyclogermacrene with Mn(2+) as a cofactor.
With Mg(2+) a more complex mixture is produced.
(2E,6E)-farnesyl diphosphate = bicyclogermacrene + diphosphate.
The enzyme from Zea mays, variety B73, gives mainly 7-epi-sesquithujene with (S)-beta-bisabolene and traces of other sesquiterpenoids, cf. EC 4.2.3.55.
The product ratio is dependent on which metal ion is present.
7-epi-sesquithujene is an attractant for the emerald ash borer beetle.
(2E,6E)-farnesyl diphosphate = 7-epi-sesquithujene + diphosphate.
The enzyme from Zea mays, variety Delprim, gives mainly sesquithujene with (S)-beta-bisabolene and (E)-beta-farnesene plus traces of other sesquiterpenoids, cf. EC 4.2.3.55 and EC 4.2.3.47.
The exact product ratio is dependent on which metal ion is present.
(2E,6E)-farnesyl diphosphate = diphosphate + sesquithujene.
Two enzymes of the rice sub-species Oryza sativa subsp. indica, OsKSL5 and OsKSL6, produce ent-isokaurene.
A variant of OsKSL5 from the sub-species Oryza sativa subsp. japonica produces ent-pimara-8(14),15-diene instead (cf. EC 4.2.3.30).
ent-copalyl diphosphate = diphosphate + ent-isokaurene.
The enzyme from Zingiber zerumbet, shampoo ginger, also gives traces of beta-caryophyllene.
(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate.
The enzyme from Solanum lycopersicum (tomato) gives a mixture of tricyclene, camphene, beta-myrcene, limonene, and traces of several other monoterpenoids.
(2E)-geranyl diphosphate = diphosphate + tricyclene.
Widely distributed in plants, which release beta-ocimene when attacked by herbivorous insects.
(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate.
The enzyme reacts with (3S)-linalyl diphosphate twice as rapidly as geranyl diphosphate, but 25 times as rapidly as (3R)-linalyl diphosphate.
It is assumed that (3S)-linalyl diphosphate is normally formed as an enzyme bound intermediate in the reaction.
In the reaction the 5-pro-R hydrogen of geranyl diphosphate is eliminated during cyclopropane ring formation.
In Picea abies (Norway spruce) and Picea sitchensis (Sitka spruce) terpinolene is also formed.
(+)-car-3-ene is associated with resistance of Picea sitchensis (Sitka spruce) to white pine weevil.
(2E)-geranyl diphosphate = (+)-car-3-ene + diphosphate.
1,8-cineole is the main product from the enzyme with just traces of other monoterpenoids.
The reaction proceeds via linalyl diphosphate and alpha-terpineol, the stereochemistry of both depends on the organism.
However neither intermediate can substitute for geranyl diphosphate.
The reaction in Salvia officinalis (sage) proceeds via (-)-(3R)-linalyl diphosphate while that in Arabidopsis (rock cress) proceeds via (+)-(3S)-linalyl diphosphate.
(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate.
Isolated from Pinus contorta (lodgepole pine) as cyclase I and from Conocephalum conicum (liverwort).
(2E)-geranyl diphosphate = (1S,5S)-sabinene + diphosphate.
Isolated from Salvia officinalis (sage).
The recombinant enzyme gave 63% (+)-sabinene, 21% gamma-terpinene, and traces of other monoterpenoids.
(2E)-geranyl diphosphate = (1R,5R)-sabinene + diphosphate.
The enzyme has been characterized from Vitis vinifera (grape).
Also forms some 1,8-cineole and traces of other monoterpenoids.
(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate.
The enzyme has been characterized from Santalum album (sandalwood).
Also forms some (-)-limonene and traces of other monoterpenoids.
(2E)-geranyl diphosphate + H2O = (R)-alpha-terpineol + diphosphate.
Mn(2+) is less effective as cofactor than Mg(2+) and product ratio changes.
(2E)-geranyl diphosphate = diphosphate + terpinolene.
Isolated from Thymus vulgaris (thyme), Citrus limon (lemon), Citrus unshiu (satsuma) and Origanum vulgare (oregano).
The reaction involves a 1,2-hydride shift.
The 5-pro-S hydrogen of geranyl diphosphate is lost.
Traces of several other monoterpenoids are formed in addition to gamma-terpinene.
(2E)-geranyl diphosphate = diphosphate + gamma-terpinene.
The enzyme has been characterized from Dysphania ambrosioides (American wormseed).
The enzyme will also use (3R)-linalyl diphosphate.
The 1-pro-S hydrogen of geranyl diphosphate is lost.
(2E)-geranyl diphosphate = alpha-terpinene + diphosphate.
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-camphene and (+)-alpha-pinene.
(3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate.
(2E)-geranyl diphosphate = (1R,4S)-camphene + diphosphate.
(-)-Camphene is the major product in Abies grandis (grand fir) with traces of other monoterpenoids.
In Pseudotsuga menziesii (Douglas-fir) there are about equal parts of (-)-camphene and (-)-alpha-pinene with traces of four other monoterpenoids.
In Solanum lycopersicum (tomato) tricyclene, beta-myrcene, limonene, and traces of several other monoterpenoids are also formed.
(2E)-geranyl diphosphate = (1S,4R)-camphene + diphosphate.
The product, 2-methylisoborneol, is a characteristc odiferous compound with a musty smell produced by soil microorganisms.
(E)-2-methylgeranyl diphosphate + H2O = 2-methylisoborneol + diphosphate.
Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids.
(3S)-linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate.
The 4-pro-S hydrogen of geranyl diphosphate is lost.
The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-alpha-pinene and (-)-beta-pinene.
However the clone ag11 gave 35% (-)-limonene, 24% (-)-alpha-pinene and 20% (-)-beta-phellandrene.
Synthase I from Pinus taeda (loblolly pine) produces (-)-alpha-pinene with traces of (-)-beta-pinene.
The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-alpha-pinene and 30% (-)-beta-pinene.
The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-alpha-pinene and (-)-camphene plus traces of other monoterpenoids.
(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate.
Cyclase II of Salvia officinalis (sage) produces about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids.
The enzyme can also use (3S)-Linalyl diphosphate (preferred to (3R)-linalyl diphosphate).
The enzyme from Abies grandis (grand fir) produces roughly equal parts of (-)-alpha-pinene and (-)-beta-pinene.
Cyclase IV from Pinus contorta (lodgepole pine) produces 63% (-)-beta-pinene, 26% 3-carene, and traces of alpha-pinene.
Synthase III from Pinus taeda (loblolly pine) forms (-)-beta-pinene with traces of alpha-pinene.
A cloned enzyme from Artemisia annua (sweet wormwood) gave (-)-beta-pinene with traces of (-)-alpha-pinene.
The enzyme from Picea sitchensis (Sika spruce) forms 30% (-)-beta-pinene and 70% (-)-alpha-pinene.
(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate.
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-alpha-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-alpha-pinene and (+)-beta-pinene.
The 4-pro-R hydrogen of geranyl diphosphate is lost.
With synthase II of Pinus taeda (loblolly pine) (+)-beta-pinene was the only product.
(2E)-geranyl diphosphate = (1R,5R)-alpha-pinene + diphosphate.
Cyclase III from Salvia officinalis (sage) gives roughly equal parts of (+)-beta-pinene and (+)-alpha-pinene.
(2E)-geranyl diphosphate = (1R,5R)-beta-pinene + diphosphate.
(2E,6E)-farnesyl diphosphate = beta-sesquiphellandrene + diphosphate.
Requires an NAD(+) cofactor, which is transiently reduced during the reaction.
The enzyme from the bacterium Bacillus circulans forms a complex with the glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase (EC 4.3.3.6), which appears to stabilize the complex.
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate.
The enzyme has been characterized from the fungus Coprinus cinereus.
Also gives germacrene A and gamma-muurolene, see EC 4.2.3.23 and EC 4.2.3.126.
(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate.
Also gives germacrene A and alpha-muurolene, see EC 4.2.3.23 and EC 4.2.3.125.
(2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene.
Isolated from the fungus Coprinus cinereus.
The enzyme also forms (+)-delta-cadinene, beta-cubebene, (+)-sativene and traces of several other sequiterpenoids.
beta-copaene is formed in the presence of Mg(2+) but not Mn(2+).
(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate.
The enzyme also forms (+)-delta-cadinene, beta-copaene, (+)-sativene and traces of several other sequiterpenoids.
It is found in many higher plants such as Magnolia grandiflora (Southern Magnolia) together with germacrene A.
(2E,6E)-farnesyl diphosphate = beta-cubebene + diphosphate.
The enzyme also forms (+)-delta-cadinene, beta-copaene, beta-cubebene, and traces of several other sequiterpenoids.
(2E,6E)-farnesyl diphosphate = (+)-sativene + diphosphate.
This sesquarterpene is present in a number of Bacillus species.
all-trans-heptaprenyl diphosphate = (R)-tetraprenyl-beta-curcumene + diphosphate.
Isolated from the plants Rosmarinus officinalis (rosemary) and Salvia miltiorrhiza.
The enzyme from the plant Selaginella moellendorffii is mutifunctional and also catalyzes EC 5.5.1.12.
(+)-copalyl diphosphate = diphosphate + miltiradiene.
Isolated from Abies grandis (grand fir).
This class I enzyme forms about equal proportions of abietadiene, levopimaradiene and neoabietadiene; see also EC 4.2.3.18 and EC 4.2.3.32.
An X-ray study of this multifunctional enzyme showed that the class I activity is in the alpha domain, while EC 5.5.1.12 activity (a class II activity) is in the beta and gamma domains.
In Pinus taeda (loblolly pine) the major product is levopimaradiene, with less abietadiene and neoabietadiene.
(+)-copalyl diphosphate = diphosphate + neoabietadiene.
Isolated from Helianthus annuus (sunflower).
The enzyme also produces beta-caryophyllene, delta-cadinene and traces of other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate.
5-phosphohydroxy-L-lysine ammoniophospholyase
Has no activity with phosphoethanolamine (cf. EC 4.2.3.2).
(5R)-5-phosphooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate + NH4(+) + phosphate.
Isolated from the fungus Armillaria gallica.
Delta(6)-Protoilludene is the first step in the biosynthesis of the melleolides.
(2E,6E)-farnesyl diphosphate = Delta(6)-protoilludene + diphosphate.
Isolated from the roots of the plant Matricaria chamomilla var. recutita (chamomile).
The enzyme also produced traces of five other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = (-)-alpha-isocomene + diphosphate.
Isolated from the plant Selaginella moellendorfii.
The enzyme also gives two other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate = (E)-2-epi-beta-caryophyllene + diphosphate.
Isolated from the plant Phyla dulcis (Aztec sweet herb).
(+)-epi-alpha-bisabolol is the precursor of the sweetener hernandulcin.
(2E,6E)-farnesyl diphosphate + H2O = (+)-epi-alpha-bisabolol + diphosphate.
Isolated from the plant Valeriana officinalis (valerian).
(2E,6E)-farnesyl diphosphate = diphosphate + valerena-4,7(11)-diene.
Isolated from the plants Abies balsamea (balsam fir) and Nicotiana tabacum (tobacco).
8-hydroxycopalyl diphosphate = cis-abienol + diphosphate.
Isolated from the plant Salvia sclarea (clary sage).
Originally thought to be synthesized in one step from geranylgeranyl diphosphate it is now known to require two enzymes, EC 4.2.1.133 and EC 4.2.3.141.
8-hydroxycopalyl diphosphate + H2O = diphosphate + sclareol.
7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
Isolated from the plant Solanum habrochaites.
7-epizingiberene is a whitefly repellant.
(2E,6E)-farnesyl diphosphate = 7-epizingiberene + diphosphate.
Isolated from the root of the plant Thapsia garganica.
The enzyme also produces germacrene D, bicyclogermacrene and traces of other sesquiterpenoids.
(2E,6E)-farnesyl diphosphate + H2O = diphosphate + kunzeaol.
The enzyme is a component of the herbivore-induced indirect defense system.
The product, (E,E)-geranyllinalool, is a precursor to the volatile compound 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT), which is released by many plants in response to damage.
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (6E,10E)-geranyllinalool + diphosphate.
Isolated from the fungus Aspergillus clavatus.
The product is a sesterterpenoid (C25 terpenoid).
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + H2O = diphosphate + ophiobolin F.
Isolated from the bacterium Streptomyces melanosporofaciens, where it is part of the biosynthesis of cyclooctatin, a potent inhibitor of lysophospholipase.
geranylgeranyl diphosphate + H2O = cyclooctat-9-en-7-ol + diphosphate.
Isolated from the plants Pinus banksiana (jack pine) and Pinus contorta (lodgepole pine).
(+)-copalyl diphosphate = diphosphate + pimara-8(14),15-diene.
Isolated from the bacterium Streptomyces sp. SANK 60404.
This bifunctional enzyme also produces (R)-nephthenol (cf. EC 4.2.3.149).
(2E,6E,10E)-geranylgeranyl diphosphate = cembrene C + diphosphate.
Two isozymes with this activity were isolated from the bacterium Streptomyces sp. SANK 60404.
The enzyme encoded by the DtcycA gene also produces cembrene C (see 4.2.3.148), while the enzyme encoded by the DtcycB gene also produces (R)-cembrene A and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol (cf. EC 4.2.3.150 and EC 4.2.3.151).
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (R)-nephthenol + diphosphate.
This trifunctional enzyme also produces (R)-nephthenol and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol (cf. EC 4.2.3.149 and EC 4.2.3.151).
(2E,6E,10E)-geranylgeranyl diphosphate = (R)-cembrene A + diphosphate.
pentamethylcyclopentadecatrienol synthase
This trifunctional enzyme also produces (R)-nephthenol and (R)-cembrene A (cf. EC 4.2.3.149 and EC 4.2.3.150).
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol + diphosphate.
The enzyme is highly specific for alpha-D-sedoheptulopyranose 7-phosphate.
It requires a divalent metal ion (Zn(2+) or Co(2+)) and an NAD(+) cofactor, which is transiently reduced during the reaction.
The enzyme is involved in the biosynthesis of C7N-aminocyclitol natural products, such as the valienamine moiety of the antidiabetic drug acarbose and the crop protectant validamycin A.
D-sedoheptulose 7-phosphate = 2-epi-5-epi-valiolone + phosphate.
(5-formylfuran-3-yl)methyl phosphate synthase
The enzyme catalyzes the reaction in the direction of producing (5-formylfuran-3-yl)methyl phosphate, an intermediate in the biosynthesis of methanofuran.
The sequence of events starts with the removal of a phosphate group, followed by aldol condensation and cyclization.
Methanofuran is a carbon-carrier cofactor involved in the first step of the methanogenic reduction of carbon dioxide by methanogenic archaea.
2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate.
The enzyme, characterized from the cyanobacterium Nostoc punctiforme PCC 73102, is involved in the biosynthesis of the sunscreen compound shinorine.
D-sedoheptulose 7-phosphate = (R)-demethyl-4-deoxygadusol + H(+) + H2O + phosphate.
The enzyme, characterized from the bacteria Actinosynnema mirum and Stigmatella aurantiaca DW4/3-1, produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis.
D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate.
This enzyme, isolated from the bacteria Rhodopseudomonas palustris and Zymomonas mobilis, participates, along with EC 2.5.1.103 and EC 1.17.18.1, in the conversion of all-trans-farnesyl diphosphate to squalene.
H2O + presqualene diphosphate = diphosphate + hydroxysqualene.
(+)-Isoafricanol is a sesquiterpene alcohol.
Its synthesis has been shown to occur in the bacteria Streptomyces violaceusniger and S.malaysiensis.
(2E,6E)-farnesyl diphosphate + H2O = (+)-isoafricanol + diphosphate.
The enzyme, which forms the diterpene (-)-spiroviolene, has been characterized from the bacterium Streptomyces violens.
(2E,6E,10E)-geranylgeranyl diphosphate = (-)-spiroviolene + diphosphate.
The synthesis of the diterpene tsukubadiene has been shown to occur in the Actinobacterium Streptomyces tsukubaensis.
(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + tsukubadiene.
(2S,3R,6S,9S)-(-)-protoillud-7-ene synthase
The enzyme has been described from the slime-mold Dictyostelium discoideum.
It is specific for (2E,6E)-farnesyl diphosphate.
While the major product is the sequiterpene (2S,3R,6S,9S)-(-)-protoillud-7-ene, traces of pentalenene are also formed.
(2E,6E)-farnesyl diphosphate = (2S,3R,6S,9S)-(-)-protoillud-7-ene + diphosphate.
(3S)-(+)-asterisca-2(9),6-diene synthase
The sequiterpene (3S)-(+)-asterisca-2(9),6-diene has been shown to be synthezised in the slime-mold Dictyostelium discoideum.
The enzyme is specific for (2E,6E)-farnesyl diphosphate.
(2E,6E)-farnesyl diphosphate = (3S)-(+)-asterisca-2(9),6-diene + diphosphate.
The enzyme, found in the bacterium Streptomyces viridochromogenes, is specific for (2E,6E)-farnesyl diphosphate and produces only (-)-alpha-amorphene.
(2E,6E)-farnesyl diphosphate = (-)-alpha-amorphene + diphosphate.
The enzyme, which forms the sesquiterpene (+)-corvol ether B, has been reported from the bacterium Kitasatospora setae.
(2E,6E)-farnesyl diphosphate + H2O = (+)-corvol ether B + diphosphate.
The enzyme has been identified in the myxobacterium Sorangium cellulosum and in the fungus Fusarium fujikuroi.
(2E,6E)-farnesyl diphosphate = (+)-eremophilene + diphosphate.
(2E,6E)-farnesyl diphosphate = (1R,4R,5S)-(-)-guaia-6,10(14)-diene + diphosphate.
(+)-(1(10)E,4E,6S,7R)-germacradien-6-ol synthase
The enzyme has been identified in the bacterium Streptomyces pratensis.
(2E,6E)-farnesyl diphosphate + H2O = (+)-(1(10)E,4E,6S,7R)-germacradien-6-ol + diphosphate.
Isolated from an ecotype of the plant Arabidopsis thaliana from Cape Verde Islands.
The enzyme also gives (3E,7E)-dolathalia-3,7,11-triene and traces of other terpenoids.
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (3E,7E)-dolabella-3,7-dien-18-ol + diphosphate.
The enzyme also gives (3E,7E)-dolabella-3,7-dien-18-ol and traces of other terpenoids.
(2E,6E,10E)-geranylgeranyl diphosphate = (3E,7E)-dolathalia-3,7,11-triene + diphosphate.
The enzyme, found in the bacterium Streptomyces viridochromogenes, is specific for (2E,6E)-farnesyl diphosphate.
(2E,6E)-farnesyl diphosphate + H2O = 7-epi-alpha-eudesmol + diphosphate.
The enzyme, found in the bacterium Streptosporangium roseum, is specific for (2E,6E)-farnesyl diphosphate.
(2E,6E)-farnesyl diphosphate + H2O = 4-epi-cubebol + diphosphate.
The enzyme, which forms the sesquiterpene (+)-corvol ether A, has been reported from the bacterium Kitasatospora setae.
(2E,6E)-farnesyl diphosphate + H2O = (+)-corvol ether A + diphosphate.
Isolated from the plant Inula hupehensis.
The enzyme also gives gives tau-cadinol and traces of other terpenoids, see EC 4.2.3.173.
(2E,6E)-farnesyl diphosphate + H2O = 10-epi-juneol + diphosphate.
(2E,6E)-farnesyl diphosphate + H2O = diphosphate + tau-cadinol.
Isolated from the plant Camellia brevistyla.
(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-hedycaryol + diphosphate.
Isolated from the bacterium Sorangium cellulosum So ce56.
The enzyme is also responsible for the formation of trace amounts of many other sesquiterpenes, mainly cadinanes and cubebanes.
(2E,6E)-farnesyl diphosphate + H2O = 10-epi-cubebol + diphosphate.
Isolated from the fungus Neosartorya fischeri.
(2E,6E,10E,14E)-geranylfarnesyl diphosphate + H2O = diphosphate + sesterfisherol.
Isolated from the plant Cananga odorata var. fruticosa (ylang ylang).
The enzyme forms roughly equal proportions of beta-thujene, sabinene, beta-pinene and alpha-terpinene see EC 4.2.3.109/EC 4.2.3.110, EC 4.2.3.120/4.2.3.122, EC 4.2.3.115.
(2E)-geranyl diphosphate = beta-thujene + diphosphate.
Isolated from the fungus Aspergillus stellatus.
(2E,6E,10E,14E)-geranylfarnesyl diphosphate = diphosphate + stellata-2,6,19-triene.
Isolated from the plant Xanthium strumarium (rough cocklebur).
(2E,6E)-farnesyl diphosphate = diphosphate + guaia-4,6-diene.
Isolated from the plant Pseudolarix amabilis (golden larch).
The product is oxidized to pseudolaric acid B, a microtubule-destabilizing agent.
(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + pseudolaratriene.
Isolated from the bacteria Streptomyces pristinaespiralis and S.somaliensis.
(2E,6E)-farnesyl diphosphate = diphosphate + selina-4(15),7(11)-diene.
Isolated from the bacterium Streptomyces pristinaespiralis.
(2E,6E)-farnesyl diphosphate + H2O = (+)-(2S,3R,9R)-pristinol + diphosphate.
Isolated from the plant Isodon rubescens.
(+)-copalyl diphosphate + H2O = diphosphate + nezukol.
Isolated from the liverwort Marchantia polymorpha.
(2E,6E)-farnesyl diphosphate + H2O = 5-hydroxy-alpha-gurjunene + diphosphate.
ent-copalyl diphosphate = diphosphate + ent-atiserene.
ent-8alpha-hydroxylabd-13-en-15-yl diphosphate = diphosphate + ent-13-epi-manoyl oxide.
Isolated from the bacterium Kitasatospora setae.
The stereochemistry suggests the farnesyl diphosphate rearranges to nerolidyl diphosphate or an equivalent intermediate before cyclization.
(2E,6E)-farnesyl diphosphate + H2O = (2Z,6E)-hedycaryol + diphosphate.
Isolated from the bacterium Bacillus clausii.
The enzyme acts on a range of polyprenyl diphosphates.
(2E,6E,10E,14E)-geranylfarnesyl diphosphate = beta-geranylfarnesene + diphosphate.
all-trans-hexaprenyl diphosphate = beta-hexaprene + diphosphate.
all-trans-heptaprenyl diphosphate = beta-heptaprene + diphosphate.
Isolated from the plant Marrubium vulgare (white horehound) and Vitex agnus-castus (chaste tree).
peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene + diphosphate.
This enzyme has been isolated from the plants, Grindelia hirsutula (gum weed), Plectranthus barbatus (forskohlii) and Marrubium vulgare (white horehound).
8-hydroxycopalyl diphosphate = (13R)-manoyl oxide + diphosphate.
Isolated from the fungus Sordaria araneosa.
Cycloaraneosene is a precursor of the antibiotic sordarin.
(2E,6E,10E)-geranylgeranyl diphosphate = cycloaraneosene + diphosphate.
Isolated from the bacterium Streptomyces clavuligerus.
(13E)-labda-7,13-dien-15-yl diphosphate = diphosphate + labda-7,13(16),14-triene.
Isolated from the bacterium Streptomyces cyslabdanicus.
(+)-copalyl diphosphate = (12E)-labda-8(17),12,14-triene + diphosphate.
Isolated from the plants Valeriana officinalis (valerian) and Persicaria hydropiper (water pepper).
The enzyme does not act on farnesol or drimenol diphosphate.
Using 18-oxygen labeled water 18-oxygen was incorporated suggesting involvement of a stabilized carbocation or an equivalent species.
(2E,6E)-farnesyl diphosphate + H2O = (5S,9S,10S)-drim-7-en-11-ol + diphosphate.
The enzyme was identified in the roots of the plant Arabidopsis thaliana (thale cress).
The product is a semivolatile diterpene that acts as a local antifeedant in belowground direct defense against root-feeding insects.
(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + rhizathalene A.
The enzyme, which has been characterized from maize, is involved in the biosynthesis of dolabralexins (type of antifungal phytoalexins).
ent-copalyl diphosphate = diphosphate + dolabradiene.
Isolated from the plant Zea mays (maize).
(2E,6E)-farnesyl diphosphate + 2 H2O = 7-epi-ent-eudesmane-5,11-diol + diphosphate.
The enzyme from the plant Ocimum basilicum (sweet basil) also produces beta-selinene while that from Liquidambar formosana (Formosan sweet gum) also produces traces of aromadendrene.
(2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate.
The plant Salvia miltiorrhiza (danshen) produces three different forms of the enzyme, encoded by paralogous genes, that exhibit different spatial expression patterns and respond differently to hormone treatment.
(2E,6E)-farnesyl diphosphate = (-)-5-epi-eremophilene + diphosphate.
Isolated from the slime mold Dictyostelium discoideum.
The 1-proR hydrogen atom of geranylgeranyl diphosphate is lost in the reaction.
(2E,6E,10E)-geranylgeranyl diphosphate = beta-pinacene + diphosphate.
The enzyme also produces hydropyrenol, isoelisabethatriene and traces of other diterpenoids.
(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + hydropyrene.
The enzyme also produces hydropyrene, isoelisabethatriene and traces of other diterpenoids.
(2E,6E,10E)-geranylgeranyl diphosphate + H2O = diphosphate + hydropyrenol.
The 1-proR hydrogen atom of geranylgeranyl diphosphate is involved in a 1,3-hydride shift to the side-chain.
The enzyme also produces hydropyrene, hydropyrenol, and traces of other diterpenoids.
(2E,6E,10E)-geranylgeranyl diphosphate = diphosphate + isoelisabethatriene.
The enzyme was characterized from the trees Camellia hiemalis and Camellia sinensis (black tea).
The enzyme from Camellia hiemalis produces (2Z,6E)-hedycaryol as a minor product.
(2E,6E)-farnesyl diphosphate + H2O = diphosphate + valerianol.
The enzyme has been characterized from the bacterium Serratia plymuthica.
pre-sodorifen diphosphate = diphosphate + sodorifen.
carboxymethoxysuccinate = fumarate + glycolate.
DNA-(apurinic or apyrimidinic site) lyase
deoxyribonuclease (apurinic or apyrimidinic)
endodeoxyribonuclease (apurinic or apyrimidinic)
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis.
This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2.
2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+).
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase
6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase
It had previously been thought that the reactions carried out by this enzyme and EC 2.2.1.9 were carried out by a single enzyme but this has since been disproved.
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate + pyruvate.
This enzyme is part of the pathway of salicylate formation from chorismate, and forms an integral part of pathways that produce salicylate-derived siderophores, such as pyochelin and yersiniabactin.
6-O-(4 -hydroxy-2 -methylenebutyryl)-D-glucose acyltransferase (lactone-forming)
Isolated from the plant Tulipa gesneriana (tulip).
The reaction is an intramolecular transesterification producing the lactone.
The enzyme also has a weak activity with 6-tuliposide B and 6-O-benzoyl-D-glucose.
6-tuliposide A = D-glucose + tulipalin A.
The enzyme, characterized from pollen of the plant Tulipa gesneriana (tulip), catalyzes the intramolecular transesterification of 6-tuliposide B to form the antibiotic aglycon tulipalin B as a sole product.
It does not catalyze the hydrolysis of 6-tuliposide B to form a hydroxy acid.
The enzyme has marginal activity with 6-tuliposide A.
6-tuliposide B = D-glucose + tulipalin B.
Isolated from the plant Papaver somniferum (opium poppy).
The reaction occurs spontaneously when the pH is between 8-9, but the enzyme is required at the physiological pH, which is close to 7.
(7S)-O-acetylsalutaridinol = acetate + H(+) + thebaine.
(2S,3S)-3-methyl-L-aspartate = mesaconate + NH4(+).
Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.23, EC 4.3.1.24 and EC 4.3.1.25.
Catalyzes the first step in the degradation of histidine and the product, urocanic acid, is further metabolized to glutamate.
formimidoyltetrahydrofolate cyclodeaminase
formiminotetrahydrofolate cyclodeaminase
In eukaroytes, occurs as a bifunctional enzyme that also has EC 2.1.2.5 activity.
5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-methenyltetrahydrofolate + NH4(+).
beta-alanyl-CoA = acryloyl-CoA + NH4(+).
2-amino-2-deoxy-D-gluconate ammonia-lyase
2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating)
The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product.
2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH4(+).
H2O + L-serine O-sulfate = H(+) + NH4(+) + pyruvate + sulfate.
The enzyme is a member of the mu-crystallin protein family.
The reaction is stimulated by the presence of ADP or ATP and is inhibited by O2.
The enzyme cleaves a carbon-oxygen bond, releasing CO2, ammonia, and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and a second ammonia molecule.
H(+) + H2O + O-carbamoyl-L-serine = CO2 + 2 NH4(+) + pyruvate.
Hydroxylamine can replace ammonia as a substrate.
Crotonoyl-pantetheine can replace crotonoyl-CoA but it is a poorer substrate.
(3S)-3-aminobutanoyl-CoA = (2E)-butenoyl-CoA + NH4(+).
alpha,beta-diaminopropionate ammonia-lyase
Active toward both D- and L-diaminopropionate.
(S)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate.
(R)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate.
threo-3-hydroxy-L-aspartate ammonia-lyase
The enzyme, purified from the bacterium Pseudomonas sp. T62, is highly specific, and does not accept any other stereoisomer of 3-hydroxyaspartate.
Different from EC 4.3.1.20 and EC 4.3.1.27.
Requires a divalent cation such as Mn(2+), Mg(2+), or Ca(2+).
(3S)-3-hydroxy-L-aspartate = NH4(+) + oxaloacetate.
The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13) followed by tautomerization to an imine form and hydrolysis of the C-N bond.
The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10.
This reaction is also carried out by EC 4.3.1.19 from a number of sources.
The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond.
The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17.
erythro-3-hydroxy-L-aspartate ammonia-lyase
erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating)
erythro-beta-hydroxyaspartate dehydratase
The enzyme, which was characterized from the bacterium Paracoccus denitrificans NCIMB 8944, is highly specific for the L-isomer of erythro-3-hydroxyaspartate.
Different from EC 4.3.1.16 and EC 4.3.1.27.
(3R)-3-hydroxy-L-aspartate = NH4(+) + oxaloacetate.
3,4-dihydroxyphenylalanine reductive deaminase
Forms part of the L-phenylalanine-catabolism pathway in the anoxygenic phototrophic bacterium Rhodobacter sphaeroides OU5.
NADPH is oxidized more slowly than NADH.
H(+) + L-dopa + NADH = 3-(3,4-dihydroxyphenyl)propanoate + NAD(+) + NH4(+).
Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3, EC 4.3.1.24 and EC 4.3.1.25.
Far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides.
Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 and EC 4.3.1.23 and EC 4.3.1.25.
The enzyme from some species is highly specific for phenylalanine.
L-phenylalanine = (E)-cinnamate + NH4(+).
Member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3, EC 4.3.1.23 and EC 4.3.1.24.
The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency.
threo-3-hydroxy-D-aspartate ammonia-lyase
The enzyme, purified from the bacterium Delftia sp. HT23, also has activity against L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate, and D-serine.
Different from EC 4.3.1.20 and EC 4.3.1.16.
Requires a divalent cation such as Mn(2+), Co(2+) or Ni(2+).
(3R)-3-hydroxy-D-aspartate = NH4(+) + oxaloacetate.
The enzyme produces the non-proteinogenic amino acid L-pipecolate, which is incorporated into multiple secondary metabolite products, including rapamycin, tobulysin, virginiamycin and pristinamycin.
D-glucosaminate-6-phosphate ammonia lyase
The enzyme, from the bacterium Salmonella typhimurium, is involved in the degradation pathway of 2-amino-2-deoxy-D-gluconate.
2-amino-2-deoxy-D-gluconate 6-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH4(+).
dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase
The enzyme, which is a member of the 'AdoMet radical' (radical SAM) family, is involved in biosynthesis of TDP-alpha-D-desosamine.
The reaction starts by the transfer of an electron from the reduced form of the enzyme's [4Fe-4S] cluster to S-adenosyl-L-methionine, spliting it into methionine and the radical 5-deoxyadenosin-5'-yl, which attacks the sugar substrate.
AH2 + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose + S-adenosyl-L-methionine = 5'-deoxyadenosine + A + dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucose + H(+) + L-methionine + NH4(+).
The enzyme, characterized from the bacterium Rubrivivax benzoatilyticus JA2, requires no cofactors.
It acts on L-phenylalanine and L-glutamate with about 60% of the activity with L-tryptophan, and on L-tyrosine, glycine, and L-alanine with about 30% of the activity.
L-tryptophan = (E)-3-(indol-3-yl)acrylate + NH4(+).
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
The enzyme produces the F0 precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria.
F0 is also produced by some cyanobacteria and eukaryotes.
The enzyme, which forms a complex with EC 2.5.1.147, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to catalyze the condensation reaction.
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine + NH4(+).
omega-N-(L-arginino)succinate arginine-lyase
2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.
Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate.
(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate.
This microbial enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation.
Not to be confused with EC 3.5.1.116 which releases ammonia rather than urea.
(S)-ureidoglycolate = glyoxylate + urea.
Also acts on 2,6-diamino-5-formamido-3,4-dihydro-4-oxopyrimidine residues.
Brings about the reclosure of the imidazole rings of purine residues damaged by gamma-rays.
DNA 4,6-diamino-5-formamidopyrimidine = DNA adenine + H2O.
alpha-hydroxyglycine amidating dealkylase
Acts on the product of the reaction catalyzed by EC 1.14.17.3, thus removing a terminal glycine residue and leaving a des-glycine peptide amide.
a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-terminal amide + glyoxylate.
gamma-L-glutamyl-butirosin B gamma-glutamyl cyclotransferase
The enzyme catalyzes the last step in the biosynthesis of the aminoglycoside antibiotic butirosin B.
The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the terminal gamma-L-glutamate of the side chain, releasing it as the cyclic 5-oxoproline.
gamma-L-glutamyl-butirosin B = 5-oxo-L-proline + butirosin B.
glutathione-specific gamma-glutamylcyclotransferase
The enzyme, found in bacteria, fungi and animals, is specific for glutathione (cf. EC 4.3.2.9).
The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline.
glutathione = 5-oxo-L-proline + L-cysteinylglycine.
The enzyme, found in vertebrates, has no activity toward alpha-(gamma-L-glutamyl)-L-amino acids (cf. EC 4.3.2.9).
The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the gamma-L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline.
epsilon-(gamma-L-glutamyl)-L-lysine = 5-oxo-L-proline + L-lysine.
The enzyme, found in animals and plants, acts on derivatives of L-glutamate, L-2-aminobutanoate, L-alanine and glycine.
an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid.
The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis.
The enzymes from archaea and bacteria are heterodimeric.
A glutaminase component (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products.
The glutminase subunit is only active within the dimeric complex.
In fungi and plants the two subunits are combined into a single polypeptide.
5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate.
Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine or 4-nitrophenol from 4-nitrophenyl-alpha-D-3-dehydroglucoside.
Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum.
4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one.
Catalyzes a a Pictet-Spengler reaction between the aldehyde group of secologanin and the amino group of tryptamine.
Involved in the biosynthesis of the monoterpenoid indole alkaloids.
3alpha(S)-strictosidine + H2O = secologanin + tryptamine.
The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.4.
The product is rapidly converted to demethylisoalangiside.
deacetylisoipecoside + H2O = dopamine + secologanin.
The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.3.
The product is rapidly converted to demethylalangiside.
deacetylipecoside + H2O = dopamine + secologanin.
The enzyme is a glycosylase, and acts in the reverse direction to that shown.
It has a wide substrate range, and was shown to glycosylate several substrates, including the staurosporine aglycone, EJG-III-108A, J-104303, 6-N-methyl-arcyriaflavin C and indolo-[2,3-a]-carbazole.
4'-demethylrebeccamycin + H2O = beta-D-glucose + dichloroarcyriaflavin A.
pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)
The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel.
The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate.
The enzyme complex is found in aerobic bacteria, archeae, fungi and plants.
aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate.
4-hydroxy-tetrahydrodipicolinate synthase
The reaction can be divided into three consecutive steps: Schiff base formation with pyruvate, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product.
The product of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate, and the enzyme was classified accordingly as EC 4.2.1.52.
Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual product of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate synthase.
However, the identity of the product is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all.
L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O.
The S-adenosyl-L-methionine is catalytic as it is regenerated at the end of the reaction.
6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+).
The enzyme utilizes a glycine radical to break the C-N bond in choline.
Found in choline-degrading anaerobic bacteria.
choline = acetaldehyde + trimethylamine.
The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia.
Also catalyzes the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine + NH4(+).
H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) + pyruvate.
The enzyme cleaves a carbon-sulfur bond, releasing hydrogen sulfide and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia.
H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen sulfide + NH4(+).
S,S-dimethyl-beta-propiothetin = acrylate + dimethyl sulfide + H(+).
an S-alkyl-L-cysteine S-oxide = 2-aminoprop-2-enoate + an S-alkyl sulfenate.
alliin = 2-aminoprop-2-enoate + allylsulfenate.
(R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing)
Also acts on 3-phosphoglycerol-glutathione.
(R)-S-lactoylglutathione = glutathione + methylglyoxal.
hydrogen cyanide + L-cysteine = 3-cyano-L-alanine + H(+) + hydrogen sulfide.
Can use a second molecule of cysteine (producing lanthionine) or other alkyl thiols as replacing agents.
L-cysteine + sulfite = hydrogen sulfide + L-cysteate.
The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia.
The enzyme is involved in L-methionine catabolism.
H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+).
L-cysteine-S-conjugate thiol-lyase (deaminating)
The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions.
The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases.
an S-substituted L-cysteine + H2O = a thiol + NH4(+) + pyruvate.
1-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropane-1-carboxylic acid synthase
S-adenosyl-L-methionine methylthioadenosine-lyase
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine.
D-cysteine + H2O = H(+) + hydrogen sulfide + NH4(+) + pyruvate.
Dithiothreitol or 2-sulfanylethan-1-ol (2-mercaptoethanol) can act as the reducing agent in the reaction.
The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7).
AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine.
In the reverse direction, the enzyme catalyzes the attachment of heme to two cysteine residues in the protein, forming thioether links.
holo-[cytochrome c] = apo-[cytochrome c] + heme b.
The enzyme from Methanococcus jannaschii catalyzes the Michael addition of sulfite to phosphoenolpyruvate.
It specifically requires phosphoenolpyruvate and its broad alkaline pH optimum suggests that it uses sulfite rather than hydrogensulfite.
(2R)-O-phospho-3-sulfolactate = H(+) + phosphoenolpyruvate + sulfite.
leukotriene A4:glutathione S-leukotrienyltransferase
The reaction proceeds in the direction of addition.
leukotriene C4 = glutathione + leukotriene A4.
The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density.
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine.
glutathione-dependent formaldehyde-activating enzyme
The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, in the formaldehyde-detoxification pathway.
S-(hydroxymethyl)glutathione = formaldehyde + glutathione.
Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts.
The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile.
Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane).
This enzyme forms component I of a four-component enzyme system (comprising EC 4.4.1.23 (component I), EC 1.8.1.5 (component II), EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
(R)-2-hydroxypropyl-coenzyme M = (R)-1,2-epoxypropane + coenzyme M.
(2S)-2-hydroxypropyl-coenzyme M = (S)-1,2-epoxypropane + coenzyme M.
This inducible enzyme participates in cysteate degradation in Paracoccus pantotrophus NKNCYSA and in 3-sulfolactate degradation in Chromohalobacter salexigens.
The enzyme is specific for the (R) isomer.
(2R)-3-sulfolactate = H(+) + pyruvate + sulfite.
The enzyme cleaves a carbon-sulfur bond, releasing bisulfite and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
D-Cysteine can also act as a substrate, but more slowly.
It is converted into pyruvate, sulfide and ammonia.
The inducible enzyme from Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.
H2O + L-cysteate = H(+) + NH4(+) + pyruvate + sulfite.
3,5,7-trioxododecanoyl-CoA = CoA + H(+) + olivetolate.
The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1).
It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
The same reaction can also be catalyzed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1).
phycobiliprotein cysteine-84 phycobilin lyase
The enzyme, found in cyanobacteria and red algae, catalyzes the attachment of phycobilin chromophores to cysteine 84 of several phycobiliproteins (the numbering used here corresponds to the enzyme from Anabaena, in other organisms the number may vary slightly).
It can attach phycocyanobilin to the beta subunits of C-phycocyanin and phycoerythrocyanin and to both subunits of allophycocyanin.
In addition, it can attach phycoerythrobilin to both subunits of C-phycoerythrin.
phycocyanobilin-L-cysteinyl(84)-[C-phycocyanin beta-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(84)-[C-phycocyanin beta-subunit].
phycocyanobilin-L-cysteinyl(84)-[phycoerythrocyanin beta-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(84)-[phycoerythrocyanin beta-subunit].
phycocyanobilin-L-cysteinyl(84)-[allophycocyanin alpha-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(84)-[allophycocyanin alpha-subunit].
phycocyanobilin-L-cysteinyl(84)-[allophycocyanin beta-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(84)-[allophycocyanin beta-subunit].
phycoerythrobilin-L-cysteinyl(84)-[C-phycoerythrin alpha-subunit] = (2R,3E)-phycoerythrobilin + apo-L-cysteinyl(84)-[C-phycoerythrin alpha-subunit].
phycoerythrobilin-L-cysteinyl(84)-[C-phycoerythrin beta-subunit] = (2R,3E)-phycoerythrobilin + apo-L-cysteinyl(84)-[C-phycoerythrin beta-subunit].
phycobiliprotein beta-cysteine-155 phycobilin lyase
The enzyme, found in cyanobacteria and red algae, catalyzes the attachment of the phycobilin chromophore phycocyanobilin to cysteine 155 of the beta subunits of the phycobiliproteins C-phycocyanin and phycoerythrocyanin.
The numbering used here corresponds to the enzyme from Anabaena, and could vary slightly in other organisms.
phycocyanobilin-L-cysteinyl(155)-[C-phycocyanin beta-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(155)-[C-phycocyanin beta-subunit].
phycocyanobilin-L-cysteinyl(155)-[phycoerythrocyanin beta-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(155)-[phycoerythrocyanin beta-subunit].
phycoerythrocyanin alpha-cysteine-84 phycoviolobilin lyase/isomerase
phycoviolobilin phycoerythrocyanin-alpha84-cystein-lyase
The enzyme, characterized from the cyanobacteria Nostoc sp. PCC 7120 and Mastigocladus laminosus, catalyzes the covalent attachment of the phycobilin chromophore phycocyanobilin to cysteine 84 of the beta subunit of the phycobiliprotein phycoerythrocyanin and its isomerization to phycoviolobilin.
phycoviolobilin-L-cysteinyl(84)-[phycoerythrocyanin alpha-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(84)-[phycoerythrocyanin alpha-subunit].
C-phycocyanin alpha-cysteine-84 phycocyanobilin lyase
The enzyme, characterized from the cyanobacterium Synechococcus elongatus PCC 7942, catalyzes the covalent attachment of the phycobilin chromophore phycocyanobilin to cysteine 84 of the alpha subunit of the phycobiliprotein C-phycocyanin.
phycocyanobilin-L-cysteinyl(84)-[C-phycocyanin alpha-subunit] = (2R,3E)-phycocyanobilin + apo-L-cysteinyl(84)-[C-phycocyanin alpha-subunit].
R-phycocyanin alpha-cysteine-84 phycourobilin lyase/isomerase
The enzyme, characterized from the cyanobacterium Synechococcus sp. WH8102, catalyzes the covalent attachment of the phycobilin chromophore phycoerythrobilin to cysteine 84 of the alpha subunit of the phycobiliprotein R-phycocyanin and its isomerization to phycourobilin.
phycourobilin-L-cysteinyl(84)-[R-phycocyanin alpha-subunit] = (2R,3E)-phycoerythrobilin + apo-L-cysteinyl(84)-[R-phycocyanin alpha-subunit].
isoprene-epoxide--glutathione S-transferase
The enzyme can catalyze the glutathione-dependent ring opening of various epoxides, but the highest activity is with (3R)-3,4-epoxy-3-methylbut-1-ene, which is derived from isoprene by EC 1.14.13.69.
2-glutathionyl-2-methylbut-3-en-1-ol = (3R)-3,4-epoxy-3-methylbut-1-ene + glutathione.
The enzyme cleaves a carbon-sulfur bond, releasing L-thiocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
The enzyme from Brassica oleracea var. italica (broccoli) does not act on cysteine or cystathionine.
H2O + L-cystine = NH4(+) + pyruvate + S-sulfanyl-L-cysteine.
The enzyme, characterized from the bacterium Mycobacterium smegmatis, cayalyzes the last step in the pathway of ergothioneine biosynthesis.
The enzyme forms a 2-sulfenohercynine intermediate, which is reduced to ergothioneine non-enzymically by a thiol.
AH2 + H(+) + S-(hercyn-2-yl)-L-cysteine S-oxide = A + ergothioneine + NH4(+) + pyruvate.
pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase
pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase
This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor.
The process starts when one enzyme molecule adenylates pyridinium-3,5-dicarboxylate mononucleotide (P2CMN) and covalently binds the adenylated product to an intrinsic cysteine residue.
Next, the enzyme cleaves the carbon-sulfur bond, liberating pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide (PCTMN) and leaving a 2-aminoprop-2-enoate (dehydroalanine) residue attached to the protein.
Since the cysteine residue is not regenerated in vivo, the enzyme is inactivated during the process.
A second enzyme molecule then repeats the process with PCTMN, adenylating it and covalently binding it to the same cysteine residue, followed by liberation of pyridinium-3,5-bisthiocarboxylate mononucleotide (P2TMN) and the inactivation of the second enzyme molecule.
[LarE protein]-L-cysteine + ATP + pyridinium-3,5-dicarboxylate mononucleotide = [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide.
[LarE protein]-L-cysteine + ATP + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide = [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3,5-bisthiocarboxylate mononucleotide.
The enzyme, characterized from the human gut bacterium Bilophila wadsworthia, participates in a taurine degradation pathway that leads to sulfide production.
The active form of the enzyme contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (SAM) and a [4Fe-4S] cluster.
2-hydroxyethane-1-sulfonate = acetaldehyde + H(+) + sulfite.
C-phycoerythrin alpha-cysteine-82 phycoerythrobilin lyase
The enzyme, characterized from the cyanobacterium Microchaete diplosiphon, catalyzes the attachment of the phycobilin chromophore (3E)-phycoerythrobilin (PEB) to cysteine 82 of the alpha subunit of the phycobiliprotein C-phycoerythrin.
The numbering used here corresponds to the enzyme from Microchaete diplosiphon, and could vary slightly in other organisms.
Activity is greatly enhanced in the presence of the chaperone-like protein CpeZ.
The reaction could also be catalyzed by EC 4.4.1.29, but much less efficiently.
phycoerythrobilin-L-cysteinyl(82)-[C-phycoerythrin alpha-subunit] = (2R,3E)-phycoerythrobilin + apo-L-cysteinyl(82)-[C-phycoerythrin alpha-subunit].
C-phycoerythrin beta-cysteine-48/59 phycoerythrobilin lyase
The enzyme, characterized from the cyanobacterium Microchaete diplosiphon, catalyzes the attachment of the phycobilin chromophore (3E)-phycoerythrobilin (PEB) to cysteine 48 and 59 of the beta subunits of the phycobiliprotein C-phycoerythrin.
The enzyme first ligates the A ring of PEB to cysteine-48, followed by the attachment of the D ring to cysteine-59.
The reaction requires the presence of the chaperone-like protein CpeZ.
phycoerythrobilin-L-cysteinyl(48)/L-cysteinyl(59)-[C-phycoerythrin beta-subunit] = (2R,3E)-phycoerythrobilin + apo-L-cysteinyl(48)/L-cysteinyl(59)-[C-phycoerythrin beta-subunit].
The enzyme, characterized from the human gut bacterium Bilophila wadsworthia, contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (AdoMet) and a [4Fe-4S] cluster.
(2S)-3-sulfopropanediol = H(+) + hydroxyacetone + sulfite.
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride + H(+).
The enzyme cleaves a carbon-chlorine bond, releasing a chloride and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
The enzyme's activity can also result in beta-replacement reactions, e.g. in the presence of hydrogen sulfide it can convert 3-chloro-D-alanine into D-cysteine and chloride.
3-chloro-D-alanine + H2O = chloride + H(+) + NH4(+) + pyruvate.
dichloromethane + H2O = 2 chloride + formaldehyde + 2 H(+).
L-2-amino-4-chloropent-4-enoate dehydrochlorinase
H2O + L-2-amino-4-chloropent-4-enoate = 2-oxopent-4-enoate + chloride + H(+) + NH4(+).
3-chloro-L-alanine + thioglycolate = chloride + H(+) + S-carboxymethyl-L-cysteine.
Also acts on dATP to form 3',5'-cyclic dAMP.
Activated by NAD(+) in presence of EC 2.4.2.31.
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP.
phosphatidylinositol diacylglycerol-lyase
1-phosphatidylinositol phosphodiesterase
Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11.
a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) = 1D-myo-inositol 1,2-cyclic phosphate + a 1,2-diacyl-sn-glycerol.
glycosylphosphatidylinositol diacylglycerol-lyase
(glycosyl)phosphatidylinositol-specific phospholipase C
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
glycosyl inositol phospholipid anchor-hydrolyzing enzyme
glycosylphosphatidylinositol-phospholipase C
glycosylphosphatidylinositol-specific phospholipase C
variant-surface-glycoprotein phospholipase C
It therefore cleaves proteins from the lipid part of the glycosylphostphatidylinositol (GPI) anchors.
In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group.
In other cases, the diacylglycerol is replaced by ceramide.
The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown.
Substitution on O-2 of the inositol blocks action of this enzyme.
an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol = 6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + a 1,2-diacyl-sn-glycerol.
While FAD was the best substrate tested the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion.
The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.
FAD = AMP + H(+) + riboflavin cyclic-4',5'-phosphate.
The enzyme catalyzes the final stage in the maturation of tRNA molecules.
pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
cyclic pyranopterin monophosphate synthase
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate.
Specifically cleaves at the 3'-side of pyrimidine (uracil or cytosine) phosphate bonds in RNA.
The reaction takes place in two steps, with the 2',3'-cyclic phosphodiester intermediates released from the enzyme at the completion of the first step.
Hydrolysis of these cyclic compounds occurs at a much slower rate through a reversal of the first step, in which the -OH group of water substitutes for the 2'-OH group of the ribose used in the first step, and does not take place until essentially all the susceptible 3',5'-phosphodiester bonds have been cyclised.
The enzyme can act as an endo- or exo ribonuclease.
an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].
A widely distributed family of related enzymes found in protozoans, plants, bacteria, animals and viruses that cleave ssRNA 3'-phosphate group with little base specificity.
The enzyme catalyzes a two-stage endonucleolytic cleavage.
The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with a 2',3'-cyclic phosphodiester, which are released from the enzyme.
The enzyme then hydrolyzes the cyclic products in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised.
The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose.
The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+).
The enzyme secreted by the fungus Ustilago sphaerogena cleaves at the 3'-phosphate group of purines, and catalyzes a two-stage endonucleolytic cleavage.
The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphodiester, which are released from the enzyme.
The enzyme then hydrolyzes these cyclic compounds in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised.
[RNA] containing adenosine + H2O = an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment].
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment].
Homopolymers of A, U or G are not hydrolyzed.
CpG bonds are hydrolyzed less well and there is no detectable hydrolysis between two purines or two pyrimidines.
The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending a with 2',3'-cyclic phosphodiester, which are released from the enzyme.
RNA containing adenosine-cytidine + H2O = an [RNA fragment]-3'-cytidine-3'-phosphate + a 5'-a hydroxy-adenosine -3'-[RNA fragment].
This enzyme catalyzes endonucleolytic cleavage to 2',3'-cyclic nucleotides.
The cyclic products may be hydrolyzed to the corresponding 3'-phosphates by EC 3.1.4.16.
The enzyme from Bacillus subtilis is inhibited by ATP.
RNA = a 5'-hydroxy-ribonucleotide + n nucleoside-2',3'-cyclophosphates.
Ribotoxins are rRNA endonucleases that catalyze the cleavage of the phosphodiester bond between guanosine and adenosine residues at one specific position in 28S rRNA.
The enzyme secreted by Aspergillus giganteus specifically cleaves rat 28S rRNA between G(4325) and A(4326) and displays cytotoxic activity toward animal cells.
The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with 2',3'-cyclic phosphodiester, which are released from the enzyme.
a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment].
A family of related enzymes found in some fungi and bacteria.
The enzyme is specific for cleavage at the 3'-phosphate group of guanosine in single stranded RNA, and catalyzes a two-stage endonucleolytic cleavage.
The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending in Gp with 2',3'-cyclic phosphodiester, which are released from the enzyme.
bacteriophage T4 restriction endoribonuclease RegB
The enzyme from bacteriophage T4 cleaves early mRNAs between Ap and Gp at one specific specific GpGpApGp site, favoring their further transition to middle-phase mRNA.
The activity is enhanced by Ribosomal S1 protein.
a [pre-mRNA]-containing guanosine-adenosine + H2O = a 5' hydroxy-guanosine-[pre-mRNA fragment] + a [pre-mRNA fragment]-3'-adenosine-3'-phosphate.
alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase
This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate.
The enzyme from the bacterium Escherichia coli can act on additional alpha-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. alpha-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and alpha-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).
AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine = 5'-deoxyadenosine + A + alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H(+) + L-methionine + methane.
The enzyme, characterized from the bacterium Kutzneria sp. 744, is one of very few enzymes known to result in the formation of an N-N bond.
(3S)-1,2-diazinane-3-carboxylate (piperazate) is known to be incorporated into assorted secondary products that are produced by nonribosomal peptide synthetase or nonribosomal peptide synthetase/polyketide synthase hybrid pathways, such as the kutznerides, padanamides, himastatins, and sanglifehrins.
N(5)-hydroxy-L-ornithine = (3S)-1,2-diazinane-3-carboxylate + H(+) + H2O.
The enzyme from Pseudomonas chlororaphis contains Ca(2+) and protoheme IX, the iron of which must be in the form iron(II) for activity.
The enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate.
No activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime.
an aliphatic aldoxime = a nitrile + H2O.
(indol-3-yl)acetaldehyde-oxime hydro-lyase
(E)-(indol-3-yl)acetaldehyde oxime = (indol-3-yl)acetonitrile + H2O.
(Z)-phenylacetaldehyde-oxime hydro-lyase
The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity.
(Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom.
In this way, the oxidation state of the heme controls the coordination stucture of the substrate--heme complex, which regulates enzyme activity.
The enzyme is active toward several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as toward arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime.
However, it is inactive with phenylacetaldoximes that have a substituent group at an alpha-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime.
The activity of the enzyme is inhibited completely by the heavy-metal cations Cu(+), Cu(2+), Ag(+) and Hg(+) whereas Fe(2+) and Sn(2+) have an activatory effect.
(Z)-phenylacetaldehyde oxime = H2O + phenylacetonitrile.
The enzyme catalyzes the terminal step in the heme biosynthesis pathways of eukaryotes and Gram-negative bacteria.
The reaction is catalyzed only in the reverse direction.
2 H(+) + heme b = Fe(2+) + protoporphyrin IX.
Acts on CH3Hg(+) and a number of other alkylmercury compounds, in the presence of cysteine or other thiols, liberating mercury as a mercaptide.
an alkylmercury + H(+) = an alkane + Hg(2+).
This enzyme, which forms part of the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway, is a type II chelatase.
It is ATP-independent and exists as either a monomer (CbiX) or a homodimer (CibK).
CbiK from Salmonella enterica uses precorrin-2 as the substrate to yield cobalt-precorrin-2.
The enzyme contains two histidines at the active site that are thought to be involved in the deprotonation of the tetrapyrrole substrate as well as in metal binding.
CbiX from Bacillus megaterium inserts cobalt at the level of sirohydrochlorin (factor-II) rather than precorrin-2.
See EC 6.6.1.2 for the cobaltochelatase that participates in the aerobic cobalamin biosynthesis pathway.
Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin.
Co-precorrin-2 + 3 H(+) = Co(2+) + precorrin-2.
This enzyme catalyzes the third of three steps leading to the formation of siroheme from uroporphyrinogen III.
The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107) and the second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76).
In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
2 H(+) + siroheme = Fe(2+) + sirohydrochlorin.
This heme detoxifying enzyme is found in Plasmodium parasites and converts toxic heme to crystalline hemozoin.
These organisms lack the mammalian heme oxygenase for elimination of heme.
It can also catalyze the reaction of EC 4.99.1.1 at a much lower level.
Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+).
SGR has very low activity with chlorophyllide a and none with chlorophyll b.
It acts on chlorophyll a both in its free form and in protein complex.
SGRL, on the other hand, is more active with chlorophyllide a than with chlorophyll a.
The magnesium formed is scavenged by MCS (metal-chelating substance).
chlorophyll a + 2 H(+) = Mg(2+) + pheophytin a.
chlorophyllide a + 2 H(+) = Mg(2+) + pheophorbide a.
The enzyme, studied from the methanogenic archaeon Methanosarcina acetivorans, participates in the biosynthesis of the nickel-containing tetrapyrrole cofactor coenzyme F430, which is required by EC 2.8.4.1.
It catalyzes the insertion of the nickel ion into sirohydrochlorin.
2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin.
pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase
It catalyzes the insertion of Ni(2+) into the cofactor forming a covalent bond between a carbon atom and the nickel atom.
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide.
The enzyme is involved in a lysine catabolic pathway.
(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate.
Also interconverts trans-4-hydroxy-D-proline and cis-4-hydroxy-L-proline.
trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline.
an L-alpha-amino acid = a D-alpha-amino acid.
phenylalanine racemase (ATP-hydrolyzing)
ATP + H2O + L-phenylalanine = AMP + D-phenylalanine + diphosphate + H(+).
Also acts, at half the rate, on L-alanine.
The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the monolactam antibiotic nocardicin A.
It catalyzes the epimerization of the amino group at position 9' from (S) configuration to (R).
The enzyme can act on both isonocardicin A and isonocardicin C, but the in vivo substrate appears to be the latter.
alpha-amino-epsilon-caprolactam racemase
Also interconverts 2-aminopentano-5-lactam (alpha-amino-delta-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4).
It does not catalyze the racemisation of alpha-amino acids but has some transaminase activity with them.
L-2-aminohexano-6-lactam = D-2-aminohexano-6-lactam.
The enzyme specifically interconverts the configuration of Ser-46 of the peptide omega-agatoxin-KT, found in the venom of the funnel web spider, Agelenopsis aperta, but not that of the other serine residue, Ser-28.
Epimerization at C-5 of the 5-amino-5-carboxypentanoyl group to form penicillin N is required to make a substrate for EC 1.14.20.1, to produce cephalosporins.
Highly selective for L-serine as substrate.
D-Serine is found in type-II astrocytes in mammalian brain, where it appears to be an endogenous ligand of the glycine site of N-methyl-D-aspartate (NMDA) receptors.
The reaction can also occur in the reverse direction but does so more slowly at physiological serine concentrations.
The enzyme employs a two-base mechanism, with a thiolate-thiol pair in the active site.
It participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species.
The enzyme, characterized from the bacteria Escherichia coli and Bacillus subtilis, is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component.
In vitro the enzyme from E.coli epimerizes several L-Ala-L-X dipeptides with broader specificity than the enzyme from B.subtilis.
L-alanyl-L-glutamate = L-alanyl-D-glutamate.
The enzyme, characterized from the bacterium Lactobacillus buchneri, specifically catalyzes racemization of nonpolar amino acids at the C-2 position.
The enzyme, characterized from the bacteria Pelagibaca bermudensis and Paracoccus denitrificans, specifically catalyzes racemization of trans-4-hydroxy-L-proline betaine and L-proline betaine at the C-2 position.
trans-4-hydroxy-L-proline betaine = cis-4-hydroxy-D-proline betaine.
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate epimerase
The enzyme, characterized from the bacterium Xanthomonas oryzae, catalyzes epimerization of the terminal L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
The reaction proceeds only in one direction and involves an adenylated intermediate.
The combined activity of this enzyme and EC 6.3.2.53 provides an alternative route for incorporating D-glutamate into peptidoglycan, replacing the more common combination of EC 5.1.1.3 and EC 6.3.2.9.
ATP + H2O + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate = AMP + diphosphate + H(+) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate.
The enzyme has been characterized from the bacterium Lactobacillus plantarum and appears to be restricted to lactic acid bacteria.
It contains a unique nickel-containing cofactor, pyridinium-3-thioamide-5-thiocarboxylate mononucleotide Ni pincer complex.
(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA.
(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate is the commonly occurring isomer of isocitrate.
D-threo-isocitrate = D-erythro-isocitrate.
The enzyme, present in bacteria, is involved in a degradation pathway of D-galacturonate.
keto-D-tagaturonate = keto-D-fructuronate.
Also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate.
D-ribulose 5-phosphate = D-xylulose 5-phosphate.
uridine diphosphate galactose 4-epimerase
UDP-alpha-D-glucose = UDP-alpha-D-galactose.
Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose.
This enzyme catalyzes the first step in galactose metabolism by converting beta-D-galactose into alpha-D-galactose, which is the substrate for EC 2.7.1.6.
alpha-L-arabinopyanose = beta-L-arabinopyranose.
L-ribulose 5-phosphate = D-xylulose 5-phosphate.
UDP-beta-L-arabinopyranose = UDP-alpha-D-xylose.
UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate.
uridine diphosphoacetylglucosamine epimerase
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine.
an N-acyl-D-glucosamine = an N-acyl-D-mannosamine.
N-acylglucosamine-6-phosphate 2-epimerase
N-acetylglucosmamine 6-phosphate 2-epimerase
N-acetylmannosamine-6-phosphate 2-epimerase
an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate.
N-acetyl-D-glucosamine 6-phosphate = N-acetyl-D-mannosamine 6-phosphate.
cytidine diphosphate paratose-2-epimerase
cytidine diphosphodideoxyglucose epimerase
CDP-paratose (CDP-3,6-dideoxy-D-glucose), is more systematically called CDP-alpha-3,6-dideoxy-D-ribo-hexose.
CDP-tyvelose (CDP-3,6-dideoxy-D-mannose) is systematically called CDP-3,6-dideoxy-D-arabino-hexose.
CDP-alpha-D-paratose = CDP-3,6-dideoxy-alpha-D-mannose.
The enzyme catalyzes the interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety.
D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose.
dTDP-4-keto-6-deoxyglucose 3,5-epimerase
thymidine diphospho-4-ketorhamnose 3,5-epimerase
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose.
UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing)
uridine diphosphate-N-acetylglucosamine-2'-epimerase
uridine diphosphoacetylglucosamine 2'-epimerase
uridine diphospho-N-acetylglucosamine 2'-epimerase
This bacterial enzyme catalyzes the reversible interconversion of UDP-GlcNAc and UDP-ManNAc.
The latter is used in a variety of bacterial polysaccharide biosyntheses.
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine.
alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate.
UDP-alpha-D-glucosamine = UDP-alpha-D-galactosamine.
heparosan-N-sulfate-glucuronate 5-epimerase
The enzyme acts on D-glucosyluronate residues in N-sulfated heparosan polymers, converting them to L-iduronate, thus modifying the polymer to heparan-N-sulfate.
The enzyme requires that at least the N-acetylglucosamine residue linked to C-4 of the substrate has been deacetylated and N-sulfated, and activity is highest with fully N-sulfated substrate.
It does not act on glucuronate residues that are O-sulfated or are adjacent to N-acetylglucosamine residues that are O-sulfated at the 6 position.
Thus the epimerization from D-glucuronate to L-iduronate occurs after N-sulfation of glucosamine residues but before O-sulfation.
Not identical with EC 5.1.3.19 or with EC 5.1.3.36.
[heparosan-N-sulfate](n) = [heparan-N-sulfate](n).
The enzyme catalyze the formation of the stable intermediate GDP-beta-L-gulose as well as GDP-beta-L-galactose.
The reaction proceeds by C4' oxidation of GDP-alpha-D-mannose followed by epimerization of the C5' position to give GDP-beta-L-4-dehydro-gulose.
This intermediate is either reduced to give GDP-beta-L-gulose or the C3' position is epimerized to give GDP-beta-L-4-dehydro-galactose, followed by C4' reduction to yield GDP-beta-L-galactose.
Both products serve as intermediates in two different variants of plant L-ascorbate biosynthesis pathways.
GDP-alpha-D-mannose = GDP-beta-L-gulose.
GDP-beta-L-gulose = GDP-beta-L-galactose.
chondroitin 4'-sulfate = dermatan 4'-sulfate.
ADP-L-glycero-D-manno-heptose 6-epimerase
ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose.
The enzyme catalyzes the interconversion of alpha and beta anomers of maltose more effectively than those of disaccharides such as lactose and cellobiose.
Along with EC 4.1.1.85, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
L-ribulose 5-phosphate = L-xylulose 5-phosphate.
UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase
2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid 2-epimerase
Participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of the B-band lipopolysaccharide of Pseudomonas aeroginosa serotype O5 and of the band-A trisaccharide of Bordetella pertussis, both important respiratory pathogens.
Highly specific as UDP-alpha-D-GlcNAc, UDP-alpha-D-GlcNAcA (UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid) and UDP-alpha-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucose) cannot act as substrates.
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate = UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate.
Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages and are released in alpha form during degradation.
This enzyme accelerates maturotation to the beta form via the open form (which also occurs as a slow spontaneous reaction).
The open form is necessary for further metabolism by the bacteria.
N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate.
The equilibrium is strongly toward dTDP-beta-L-rhamnose.
dTDP-6-deoxy-beta-L-talose = dTDP-beta-L-rhamnose.
N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase
The enzyme is involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen produced by some Gram-negative bacteria.
N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate = N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-undecaprenyl diphosphate.
dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase
dTDP-4-keto-6-deoxy-D-glucose 3-epimerase
The enzyme is involved in the biosynthetic pathway of dTDP-6-deoxy-alpha-D-allose, which is converted to mycinose after attachment og the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II.
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-allose.
Involved in bacterial polysaccharide biosynthesis.
UDP-2-acetamido-2,6-dideoxy-beta-L-talose = UDP-N-acetyl-beta-L-fucosamine.
This enzyme shows no 1-epimerase activity with D-glucose, L-rhamnose and D-fucose (cf. EC 5.1.3.3).
The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose (cf. EC 5.1.3.31).
The enzymes isolated from the bacteria Pseudomonas cichorii, Pseudomonas sp. ST-24, Rhodobacter sphaeroides and Mesorhizobium loti catalyze the epimerization of various ketoses at the C3 position, interconverting D-fructose and D-psicose, D-tagatose and D-sorbose, D-ribulose and D-xylulose, and L-ribulose and L-xylulose.
The enzyme is specific for L-rhamnopyranose.
The enzyme, characterized from the bacterium Actinomyces sp.
Lu 9419, is involved in the biosynthesis of the antitumor agent cetoniacytone A.
2-epi-5-epi-valiolone = 5-epi-valiolone.
The enzyme, characterized from cyanobacteria, is involves in the biosynthesis of galactolipids found in their photosynthetic membranes.
a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol = a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol.
2-epi-5-epi-valiolone 7-phosphate 2-epimerase
The enzyme, isolated from the bacterium Actinoplanes sp. SE 50/110, is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose.
2-epi-5-epi-valiolone 7-phosphate = 5-epi-valiolone 7-phosphate.
The enzyme, characterized from the giant African snail Achatina fulica, participates in the biosynthetic pathway of acharan sulfate.
Unlike EC 5.1.3.17, it shows no activity with D-glucuronate residues in heparosan-N-sulfate.
The enzyme epimerizes the C-5 bond in some beta-D-mannuronate residues in mannuronan, converting them to alpha-L-guluronate residues, and thus modifying the mannuronan into alginate.
It is found in brown algae and alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.
[(1->4)-beta-D-mannuronosyl](n) = [alginate](n).
D-erythrulose 1-phosphate = L-erythrulose 1-phosphate.
The enzyme from Agrobacterium fabrum C58 is part of D-altritol and galactitol degradation pathways.
keto-D-tagatose 6-phosphate = keto-D-fructose 6-phosphate.
The enzyme, characterized from the bacterium Escherichia coli, is involved in the catabolism of fructoseamines, amino acid sugar complexes that are formed non-enzymically.
N(6)-(D-psicosyl)-L-lysine = N(6)-(D-fructosyl)-L-lysine.
The enzyme, characterized from the archaeon Sulfolobus tokodaii, participates in a pathway for the biosynthesis of UDP-N-acetyl-alpha-D-galactosamine.
D-glucosamine 6-phosphate = D-galactosamine 6-phosphate.
The enzyme is found in bacteria that possess sulfoglycolytic pathways.
The enzyme can also act on other aldohexoses such as D-galactose, D-glucose, D-glucose-6-phosphate, and D-glucuronate, but with lower efficiency.
6-sulfo-alpha-D-quinovose = 6-sulfo-beta-D-quinovose.
The enzyme, characterized from multiple bacterial species, catalyzes the interconversion between beta-D-glucopyranose and beta-D-mannopyranose through proton abstraction-addition at the C2 position.
(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA.
a 16alpha-hydroxysteroid = a 16beta-hydroxysteroid.
alpha-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates.
Also active toward some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA.
a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA.
This enzyme, along with EC 3.5.1.77, EC 3.5.1.87 and EC 3.5.2.2, forms part of the reaction cascade known as the 'hydantoinase process', which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids.
The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-[2-(methylsulfanyl)ethyl]hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position.
In the enzyme from Sinorhizobium meliloti, Cys-76 is responsible for recognition and proton retrieval of D-isomers, while Cys-181 is responsible for L-isomer recognition and racemization.
a D-5-monosubstituted hydantoin = a L-5-monosubstituted hydantoin.
The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate.
Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93.
dihydroneopterin triphosphate 2'-epimerase
D-erythro-7,8-dihydroneopterin triphosphate epimerase
The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin.
7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate.
The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25.
The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81).
7,8-dihydroneopterin = 7,8-dihydromonapterin.
4-maleylacetoacetate = 4-fumarylacetoacetate.
(9Z,12Z)-octadecadienoate = (9Z,11E)-octadecadienoate.
(E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide = (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide.
The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0).
2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase
2-chlorocarboxymethylenebutenolide isomerase
cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide = trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide.
The enzyme catalyzes the cis-trans isomerization of the 15-15' carbon-carbon double bond in 9,15,9'-tricis-zeta-carotene, which is required for biosynthesis of all plant carotenoids.
9,9',15-tri-cis-zeta-carotene = 9,9'-di-cis-zeta-carotene.
The enzyme is involved in carotenoid biosynthesis.
7,7',9,9'-tetra-cis-lycopene = all-trans-lycopene.
all-trans-beta-carotene = 9-cis-beta-carotene.
D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate.
The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism.
The enzyme catalyzes the aldose-ketose isomerization of several sugars.
Most enzymes also catalyze the reaction of EC 5.3.1.25.
The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose.
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn(2+)).
The enzyme binds beta-L-arabinopyranose and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism.
The enzyme can also convert alpha-D-galactose to D-tagatose with lower efficiency.
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site.
The enzyme catalyzes the interconversion of aldose and ketose sugars with broad substrate specificity.
The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer) and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites.
Isomerization proceeds via a hydride-shift mechanism.
alpha-D-xylose = alpha-D-xylulofuranose.
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate.
D-mannose 6-phosphate = D-fructose 6-phosphate.
The enzyme from yeast catalyzes the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate.
The enzyme also catalyzes the anomerization of both D-hexose 6-phosphates.
alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate.
Also converts D-galacturonate to D-tagaturonate.
aldehydo-D-galacturonate = keto-D-tagaturonate.
The enzyme is involved in the pathway for synthesis of 3-deoxy-D-manno-octulosonate (Kdo), a component of bacterial lipopolysaccharides and plant call walls.
D-arabinose 5-phosphate = D-ribulose 5-phosphate.
The enzyme binds the closed ring form of the substrate and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites.
While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyzes the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose.
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5''-phosphoribosyl)-4-imidazolecarboxamide isomerase
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide.
5-dehydro-4-deoxy-D-glucuronate isomerase
4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
The enzyme is involved in the degradation of polygalacturonate, a later stage in the degradation of pectin by many microorganisms.
5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate.
An epimerization at C-20 and C-21 is probably catalyzed by the same enzyme.
21-hydroxyprogesterone = 20-hydroxy-3-oxopregn-4-en-21-al.
3-hydroxypyruvate = 2-hydroxy-3-oxopropanoate.
S-methyl-5-thioribose-1-phosphate isomerase
1-phospho-5'-S-methylthioribose isomerase
5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase
5-methylthioribose-1-phosphate isomerase
S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate aldose-ketose-isomerase
S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase
S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate.
N-(5'-phosphoribosyl)anthranilate isomerase
In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 4.2.1.20).
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose.
The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose.
aldehydo-D-galactose 6-phosphate = keto-D-tagatose 6-phosphate.
This enzyme, along with EC 4.1.2.43, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds.
The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyzes the reactions of EC 4.1.2.43 and this enzyme.
D-arabino-hex-3-ulose 6-phosphate = beta-D-fructose 6-phosphate.
In Gram-negative bacteria the enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core.
In Gram-positive bacteria the enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein.
2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate.
This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes.
alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate.
The enzyme, found in the bacterium Bacillus subtilis, is part of a myo-inositol degradation pathway leading to acetyl-CoA.
5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate.
6-sulfo-beta-D-quinovose = 6-deoxy-6-sulfo-D-fructose.
6-sulfo-beta-D-quinovose = 6-sulfo-D-rhamnose.
(4S)-4-hydroxy-5-phosphooxypentane-2,3-dione isomerase
(2S)-2-hydroxy-3,4-dioxopentyl phosphate = 3-hydroxy-2,4-dioxopentyl phosphate.
L-erythrulose 1-phosphate = D-erythrulose 4-phosphate.
D-erythrulose 4-phosphate = D-erythrose 4-phosphate.
2-dehydro-L-erythronate = 3-dehydro-L-erythronate.
2-dehydro-D-erythronate = 3-dehydro-D-erythronate.
TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose-forming)
Four moieties of alpha-D-rhamnose and two moities of 3-acetamido-3,6-dideoxy-alpha-D-galactose form the repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus.
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3-dehydro-6-deoxy-alpha-D-galactose.
TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-alpha-D-glucopyranose-forming)
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3-dehydro-6-deoxy-alpha-D-glucose.
2,3-diketo-5-methylthiopentyl-1-phosphate enolase
In some species a single bifunctional enzyme, EC 3.1.3.77, catalyzes both this reaction and that of EC 3.1.3.87.
5-methylsulfanyl-2,3-dioxopentyl phosphate = 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate.
The enol form (2Z,4E)-2-hydroxyhexa-2,4-dienedioate is produced as part of this pathway and is converted to the keto form (3E)-2-oxohex-3-enedioate by the enzyme.
Another keto form, (4E)-2-oxohex-4-enedioate (4-oxalocrotonate), was originally thought to be produced by the enzyme but later shown to be produced non-enzymatically.
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate.
1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase
ascopyrone intramolecular oxidoreductase
The other enzymes involved in this pathway are EC 4.2.1.110, EC 4.2.1.111 and EC 4.2.2.13.
This enzyme has been characterized from the bacterium Pseudomonas putida KT2440 and is involved in the degradation pathway of syringate and gallate.
It catalyzes the interconversion of two of the tautomers of 4-oxalomesaconate, a reaction that can also occur spontaneously.
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = 4-carboxy-2-hydroxy-cis,cis-muconate.
a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.
cholest-5-en-3-one = cholest-4-en-3-one.
isopentenylpyrophosphate Delta-isomerase
isopentenyl diphosphate = dimethylallyl diphosphate.
(S)-muconolactone = (4,5-dihydro-5-oxofuran-2-yl)-acetate.
lathosterol = 5alpha-cholest-8-en-3beta-ol.
2-methylene-3-methylsuccinate = dimethylmaleate.
This isomerization could take place either in a direct cis-trans interconversion or by an allylic rearrangement; the enzyme has been shown to catalyze the latter change.
Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase
The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position.
Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C3, which cannot be processed further by the regular enzymes of the beta-oxidation system.
This enzyme isomerizes the bond to a trans bond at position C2, which can be processed further.
The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers.
The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.
a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.
(3Z)-dodecenoyl-CoA = (2E)-dodecenoyl-CoA.
Interconverts prostaglandin A1 and prostaglandin C1.
5-carboxymethyl-2-hydroxymuconate Delta-isomerase
5-carboxymethyl-2-hydroxymuconic acid isomerase
Part of the homoprotocatechuate degradation pathway in Escherichia coli C.
(2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate.
Stereospecific for L-dopachrome (5,6-dioxo-2,3-5,6-tetrahydroindole-2-carboxylate).
Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroxyindolyl-5,6-quinone) is not (see also EC 4.1.1.84).
L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.
eicosapentaenoate cis-Delta(5,8,11,14,17)-eicosapentaenoate cis-Delta(5)-trans-Delta(7,9)-cis-Delta(14,17) isomerase
The enzyme from the red alga Ptilota filicina catalyzes the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogs, such as arachidonate and gamma-linolenate, to yield a conjugated triene.
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
trans-2-decenoyl-[acyl-carrier-protein] isomerase
beta-hydroxydecanoyl thioester dehydrase
While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs.
ACP can be replaced by either CoA or N-acetylcysteamine thioesters.
The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.
(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP].
trans-2,3-dihydro-3-hydroxyanthranilate isomerase
The enzyme is involved in phenazine biosynthesis.
The product probably spontaneously dimerises to 1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate.
(5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate = (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate.
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase
The enzyme catalyzes the reversible isomerization of 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA to the unusual unsaturated, oxygen-containing, seven-member heterocyclic enol ether 2-oxepin-2(3H)-ylideneacetyl-CoA, as part of an aerobic phenylacetate degradation pathway.
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-oxepin-2(3H)-ylideneacetyl-CoA.
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase
The enzyme can interconvert the (E) isomer formed in the reaction into the (Z) isomer, although this isomerization is not part of the pathway leading to bacilysin.
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate = 3-[(1E,4R)-4-hydroxycyclohex-2-en-1-ylidene]pyruvate.
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase
The enzyme participates in an alternative degradation route of fatty acids with cis-double bonds on odd-number carbons such as oleate and linoleate.
The main physiological substrate is (3E,5Z)-tetradeca-3,5-dienoyl-CoA, but other (3E,5Z)-dienoyl-CoAs with varying carbon chain lengths are also substrates.
a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA.
The enzyme is found in the retinal pigment epithelium (RPE) of vertebrates.
It also has the activity of EC 3.1.1.64.
S-methyl-5-thioribulose 1-phosphate isomerase
5-methylthioribulose-1-phosphate isomerase
The enzyme, characterized from the bacterium Rhodospirillum rubrum, participates in methionine salvage from S-methyl-5'-thioadenosine.
It is a RuBisCO-like protein (RLP) that is not capable of carbon fixation, and catalyzes an isomerization reaction that converts S-methyl-5-thio-D-ribulose 1-phosphate to a 3:1 mixture of S-methyl-1-thioxylulose 5-phosphate and S-methyl-1-thioribulose 5-phosphate.
The reaction is an overall 1,3-proton transfer, which likely consists of two 1,2-proton transfer events.
S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-xylulose 5-phosphate.
S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thiol-D-ribulose 5-phosphate.
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
Catalyzes the rearrangement of -S-S- bonds in proteins.
prostaglandin endoperoxide Delta-isomerase
Brings about the opening of the epidioxy bridge.
Converts prostaglandin H2 into prostaglandin I2 (prostacyclin).
Converts prostaglandin H2 into thromboxane A2.
Allene oxides formed by the action of EC 4.2.1.92 are converted into cyclopentenone derivatives.
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (10Z,15Z)-12-oxophytodienoate.
Induced during chromoplast differentiation in plants.
Isomerization of the epoxide ring of violaxanthin gives the cyclopentyl-ketone of capsorubin or capsanthin.
all-trans-violaxanthin = all-trans-capsorubin.
all-trans-antheraxanthin = all-trans-capsanthin.
The opening of the epoxide ring of violaxanthin generates a chiral allene.
Neoxanthin is a precursor of the plant hormone abscisic acid and the last product of carotenoid synthesis in green plants.
all-trans-violaxanthin = all-trans-neoxanthin.
The enzyme catalyzes the irreversible aromatization of the thiazole moiety of 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate.
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate = 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate.
The enzyme, found in the bacterium Bacillus subtilis, is part of the myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
a 1-acyl-sn-glycero-3-phosphocholine = a 2-acyl-sn-glycero-3-phosphocholine.
The enzyme, purified from the bacterium Chloroflexus aurantiacus, acts as an intramolecular CoA transferase and does not transfer CoA to free mesaconate.
2-methylfumaryl-CoA = 3-methylfumaryl-CoA.
The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, belongs to the amidohydrolase superfamily.
It participates in the degradation of D-galacturonate.
D-galactaro-1,5-lactone = D-galactaro-1,4-lactone.
phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate.
This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization.
Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate.
alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Activated by N-acetyl-alpha-D-glucosamine 1,6-bisphosphate.
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.
In the direction shown, the enzyme is phosphorylated by 3-phosphoglyceroyl phosphate to give phosphoenzyme and 3-phosphoglycerate.
The latter is rephosphorylated by the enzyme to yield 2,3-diphosphoglycerate, but this reaction is slowed down by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate.
Also catalyzes, slowly, the reaction of EC 5.4.2.12.
(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+).
Activated by D-glucose, which probably acts as an acceptor for a phosphate residue from the substrate, thus being itself converted into the product.
The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate.
Although this is a slow reaction, only a single turnover is required for activation.
Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles.
beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate.
Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate.
alpha-D-ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.
2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-phosphate.
alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favors phosphoenolpyruvate.
H(+) + phosphoenolpyruvate = 3-phosphonopyruvate.
The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis.
The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by alpha-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, alpha-D-glucose 1,6-bisphosphate or ATP.
It can also catalyze the interconversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, although at a much lower rate.
alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.
phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)
2,3-diphosphoglycerate dependent phosphoglycerate mutase
cofactor dependent phosphoglycerate mutase
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor.
The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae).
This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine.
The enzyme has no requirement for metal ions.
This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4.
(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate.
(2R)-2,3-bisphosphoglycerate + H2O = (2R)-3-phosphoglycerate + phosphate.
phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
2,3-diphosphoglycerate-independent phosphoglycerate mutase
cofactor independent phosphoglycerate mutase
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate.
The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position.
Both metal ions are involved in the reaction.
The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward D-glucosamine 6-phosphate (cf. EC 5.4.2.10).
D-galactosamine 6-phosphate = alpha-D-galactosamine 1-phosphate.
It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule.
Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions.
A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron-sulfur cluster.
S-adenosyl-L-methionine is regenerated at the end of the reaction.
adenosylcobalamin-dependent D-lysine 5,6-aminomutase
A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of adenosylcobalamin, which is regenerated at the end of the reaction.
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate.
D-lysine = (2R,5S)-2,5-diaminohexanoate.
D-ornithine = (2R,4S)-2,4-diaminopentanoate.
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate.
glutamate-1-semialdehyde 2,1-aminomutase
glutamate-1-semialdehyde aminotransferase
(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
It contains pyridoxal phosphate and a [4Fe-4S] cluster, which is coordinated by 3 cysteines and binds an exchangeable S-adenosyl-L-methionine molecule.
During the reaction cycle, the AdoMet forms a 5'-deoxyadenosyl radical, which is regenerated at the end of the reaction.
phenylalanine aminomutase (L-beta-phenylalanine forming)
phenylalanine aminomutase (D-beta-phenylalanine forming)
The enzyme from the bacterium Pantoea agglomerans produces D-beta-phenylalanine, an intermediate in the biosynthesis of the polyketide non-ribosomal antibiotic andrimid.
L-phenylalanine = (S)-3-amino-3-phenylpropanoate.
3-hydroxyaminophenol = aminohydroquinone.
In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyze in vitro two reactions, the isomerization of (3S)-linalool to geraniol and the hydration of myrcene to (3S)-linalool, the latter activity being classified as EC 4.2.1.127.
9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming)
Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P450 heme thiolate domain.
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate.
9,12-octadecadienoate 8-hydroperoxide 8S-isomerase
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((7S,8S,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming)
The bifunctional enzyme from Gaeumannomyces graminis catalyzes the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60), which is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate.
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate.
The enzyme from mammals accepts a range of hydroperoxy icosatetraenoates producing one or several different hydroxy epoxy icosatrienoates.
The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate.
The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate.
The enzymes also have the activity of EC 4.2.1.152.
a hydroperoxyeicosatetraenoate = a hydroxy-epoxy-eicosatetraenoate.
(8S)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate = (10R)-hydroxy-(8S,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate.
(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-hydroxy-(11R,12R)-epoxy-(5Z,9E,14Z)-eicosatrienoate.
(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (10R)-hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate.
(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8R)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate.
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (13R)-hydroxy-(14S,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate.
3,1-hydroxyl-Delta(1)-Delta(2)-mutase (linalool isomerase)
Isolated from the bacterium Thauera linaloolentis grown on (RS)-linalool as the sole source of carbon.
Unlike EC 5.4.4.4, which only acts on (S)-linalool, this enzyme acts equally well on both enantiomers.
(2S,3S)-3-methyl-L-aspartate = L-glutamate.
(R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase
Also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate.
2-acetolactate = 3-hydroxy-3-methyl-2-oxobutanoate.
(S)-2-ethyl-2-hydroxy-3-oxobutanoate = (R)-3-hydroxy-3-methyl-2-oxopentanoate.
2-methyleneglutarate = 2-methylene-3-methylsuccinate.
UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose.
Simultaneously produces isomaltulose (6-O-alpha-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose) from sucrose.
sucrose = 6-O-alpha-D-glucopyranosyl-D-fructose.
The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine.
TruA specifically modifies uridines at positions 38, 39, and/or 40 in the anticodon stem loop of tRNAs with highly divergent sequences and structures.
uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA.
4-carboxymethyl-4-methylbutenolide mutase
4-carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide.
(1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase
maltodextrin alpha-D-glucosyltransferase
Acts on (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked D-glucose units.
4-[(1->4)-alpha-D-glucosyl](n-1)-D-glucose = 1-[(1->4)-alpha-D-glucosyl](n-1)-alpha-D-glucose.
The enzyme also produces the cyclization product hopan-22-ol by addition of water (cf. EC 4.2.1.129).
Hopene and hopanol are formed at a constant ratio of 5:1.
5-(carboxyamino)imidazole ribonucleotide mutase
N(5)-carboxyaminoimidazole ribonucleotide mutase
In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates.
In the absence of EC 6.3.2.6, the reaction is reversible.
The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation.
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
The enzyme is specific for uridine(516) in 16S rRNA.
In vitro, the enzyme does not modify free 16S rRNA.
The preferred substrate is a 5'-terminal fragment of 16S rRNA complexed with 30S ribosomal proteins.
uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA.
The enzyme modifies uridine(2457) in a stem of 23S RNA in Escherichia coli.
uridine(2457) in 23S rRNA = pseudouridine(2457) in 23S rRNA.
The enzyme is not completely specific for uridine(2604) and can, to a small extent, also react with uridine(2605).
uridine(2604) in 23S rRNA = pseudouridine(2604) in 23S rRNA.
Pseudouridine synthase RluB converts uridine(2605) of 23S rRNA to pseudouridine.
uridine(2605) in 23S rRNA = pseudouridine(2605) in 23S rRNA.
23S rRNA pseudouridine(1911/1915/1917) synthase
Pseudouridine synthase RluD converts uridines at positions 1911, 1915, and 1917 of 23S rRNA to pseudouridines.
These nucleotides are located in the functionally important helix-loop 69 of 23S rRNA.
23S rRNA pseudouridine(955/2504/2580) synthase
The enzyme converts uridines at position 955, 2504 and 2580 of 23S rRNA to pseudouridines.
Pseudourine synthase TruB from Escherichia coli specifically modifies uridine(55) in tRNA molecules.
The bifunctional archaeal enzyme also catalyzes the pseudouridylation of uridine(54).
It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in E.coli tRNAs by thymine.
uridine(55) in tRNA = pseudouridine(55) in tRNA.
TruC specifically modifies uridines at positions 65 in tRNA.
uridine(65) in tRNA = pseudouridine(65) in tRNA.
Pseudouridine synthase PusS from Escherichia coli specifically acts on uridine(13) in tRNA.
The Pus7 protein from Saccharomyces cerevisiae is a multisite-multisubstrate pseudouridine synthase that is able to modify uridine(13) in several yeast tRNAs, uridine(35) in the pre-tRNA(Tyr), uridine(35) in U2 small nuclear RNA, and uridine(50) in 5S rRNA.
uridine(13) in tRNA = pseudouridine(13) in tRNA.
The dual-specificity enzyme also catalyzes the formation of pseudouridine(746) in 23S rRNA.
uridine(32) in tRNA = pseudouridine(32) in tRNA.
RluA is the sole protein responsible for the in vivo formation of 23S RNA pseudouridine(746).
The dual-specificity enzyme also catalyzes the formation of uridine(32) in tRNA.
uridine(746) in 23S rRNA = pseudouridine(746) in 23S rRNA.
The reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10).
UDP-beta-L-arabinofuranose = UDP-beta-L-arabinopyranose.
(17Z)-protosta-17(20),24-dien-3beta-ol is a precursor of the steroidal antibiotic helvolic acid.
(S)-2,3-epoxysqualene = (17Z)-protosta-17(20),24-dien-3beta-ol.
(S)-2,3-epoxysqualene = cucurbitadienol.
The enzyme produces germanicol, beta-amyrin and lupeol in the ratio 63:33:4.
The enzyme gives taraxerol, beta-amyrin and lupeol in the ratio 70:17:13.
(S)-2,3-epoxysqualene = isomultiflorenol.
The product is 97% camelliol, 2% achilleol A and 0.2% beta-amyrin.
Achilleol is an isomer of camelliol C with a 4-methylenecyclohexanol ring system.
This enzyme probably evolved from EC 5.4.99.39.
Some organism possess a monofunctional beta-amyrin synthase, other have a multifunctional enzyme that also catalyzes the synthesis of alpha-amyrin (EC 5.4.99.40) or lupeol (EC 5.4.99.41).
A multifunctional enzyme which produces both alpha- and beta-amyrin (see EC 5.4.99.39).
The enzyme specifically acts on uridine(31) in tRNA.
uridine(31) in tRNA = pseudouridine(31) in tRNA.
The enzyme specifically acts on uridine(2819) in 21S rRNA.
uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA.
mitochondrial tRNA pseudouridine(27/28) synthase
The mitochondrial enzyme Pus2p is specific for position 27 or 28 in mitochondrial tRNA.
uridine(27/28) in mitochondrial tRNA = pseudouridine(27/28) in mitochondrial tRNA.
The enzyme from Saccharomyces cerevisiae is active only toward uridine(38) and uridine(39), and shows no activity with uridine(40) (cf. EC 5.4.99.12).
In vitro the enzyme from mouse is active on uridine(39) and very slightly on uridine(38) (human tRNA(Leu)).
uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA.
The enzyme gives traces of four other triterpenoids.
The enzyme from rice (Oryza sativa) produces parkeol as a single product.
Achilleol B is probably formed by cleavage of the 8-14 and 9-10 bonds of (3S)-2,3-epoxy-2,3-dihydrosqualene as part of the cyclization reaction, after formation of the oleanane skeleton.
The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids.
The enzyme from Stevia rebaudiana also gives traces of other triterpenoids.
(S)-2,3-epoxysqualene = baccharis oxide.
The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of alpha- and beta-seco-amyrin.
(S)-2,3-epoxysqualene = alpha-seco-amyrin.
Marneral is a triterpenoid formed by Grob fragmentation of the A ring of 2,3-epoxy-2,3-dihydrosqualene during cyclization.
(S)-2,3-epoxysqualene = beta-seco-amyrin.
The enzyme from tomato (Solanum lycopersicum) gives 48% delta-amyrin, 18% alpha-amyrin, 13% beta-amyrin and traces of three or four other triterpenoid alcohols.
The product from Arabidopsis thaliana is 85% tirucalla-7,24-dien-3beta-ol with trace amounts of other triterpenoids.
(S)-2,3-epoxysqualene = tirucalladienol.
The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids.
The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen.
dTDP-alpha-D-fucose = dTDP-alpha-D-fucofuranose.
The enzyme, which participates in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway, catalyzes the conversion of cobalt-precorrin-8 to cobyrinate by methyl rearrangement.
The equivalent enzyme in the aerobic pathway is EC 5.4.99.61.
The enzyme, which participates in the aerobic (late cobalt insertion) adenosylcobalamin biosynthesis pathway, catalyzes the conversion of precorrin-8X to hydrogenobyrinate by methyl rearrangement.
The equivalent enzyme in the anaerobic pathway is EC 5.4.99.60.
3 H(+) + precorrin-8X = hydrogenobyrinate.
The enzyme also catalyzes the conversion between beta-allofuranose and beta-allopyranose.
beta-D-ribopyranose = beta-D-ribofuranose.
beta-D-allofuranose = beta-D-allopyranose.
(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA.
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group.
It consists of two subunits, the smaller one containing a cobalamin cofactor.
It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety.
2-hydroxyisobutanoyl-CoA = (3S)-3-hydroxybutanoyl-CoA.
Isolated from the plant Lycopodium clavatum.
The enzyme does not act on (3S)-2,3-epoxy-2,3-dihydrosqualene and does not form any alpha-onocerin.
(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene = pre-alpha-onocerin.
4-amino-4-deoxychorismate = 4-amino-4-deoxyprephenate.
Also acts, in the reverse reaction, on 3-methyl-cis,cis-muconate and, very slowly, on cis,trans-muconate.
Not identical with EC 5.5.1.7 or EC 5.5.1.11.
(S)-muconolactone = cis,cis-muconate + H(+).
3-carboxy-cis,cis-muconate cycloisomerase
2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-cis,cis-muconate + H(+).
pteridine-2,4,6,7-tetrol = H(+) + xanthine-8-carboxylate.
1L-myo-inositol-1-phosphate lyase (isomerizing)
The NAD(+) dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1; finally, the enzyme-bound NADH reconverts C-5 into the -CHOH- form.
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate.
3-carboxy-cis,cis-muconate lactonizing enzyme
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate.
Spontaneous elimination of HCl produces cis-4-carboxymethylenebut-2-en-4-olide.
Also acts in reverse direction on 2-chloro-cis,cis-muconate.
Not identical with EC 5.5.1.1 or EC 5.5.1.11.
(2R)-2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate + H(+).
The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro.
The reaction proceeds via isomeration of geranyl diphosphate to (3R)-linalyl diphosphate.
The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (+)-bornyl diphosphate.
(2E)-geranyl diphosphate = (2S,4R)-bornyl diphosphate.
Opens the cyclopropane ring of a number of related 4alpha-methyl-9beta-19-cyclosterols, but not those with a 4beta-methyl group, with formation of an 8(9) double bond.
Involved in the synthesis of plant sterols.
Both rings of pinene are cleaved in the reaction.
alpha-pinene oxide = (Z)-2-methyl-5-isopropylhexa-2,5-dienal.
The product of cyclisomerization of dichloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylene-3-chlorobut-2-en-4-olide.
Also acts, in the reverse direction, on cis,cis-muconate and its monochloro-derivatives, but with lower affinity.
Not identical with EC 5.5.1.1 or EC 5.5.1.7.
2,4-dichloro-5-oxo-2,5-dihydro-2-furylacetate = (2E,4E)-2,4-dichloromuconate + H(+).
In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional.
In other plants this activity is often a part of a bifunctional enzyme.
For example, in Selaginella moellendorffii this activity is catalyzed by a bifunctional enzyme that also catalyzes EC 4.2.3.131, while in the tree Abies grandis (grand fir) it is catalyzed by a bifunctional enzyme that also catalyzes EC 4.2.3.18.
(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl diphosphate.
Part of a bifunctional enzyme involved in the biosynthesis of kaurene.
(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl diphosphate.
This class II terpene synthase produces syn-copalyl diphosphate, a precursor of several rice phytoalexins, including oryzalexin S and momilactones A and B.
Constitutively expressed in the roots of plants where one of its products, momilactone B, acts as an allelochemical (a molecule released into the environment to suppress the growth of neighboring plants).
In other tissues the enzyme is up-regulated by conditions that stimulate the biosynthesis of phytoalexins.
(2E,6E,10E)-geranylgeranyl diphosphate = 9alpha-copalyl diphosphate.
Contains a DXDD motif, which is a characteristic of diterpene cylases whose reactions are initiated by protonation at the 14,15-double bond of geranylgeranyl diphosphate (GGDP).
The triggering proton is lost at the end of the cyclization reaction.
The product of the reaction, terpentedienyl diphosphate, is the substrate for EC 4.2.3.36 and is a precursor of the diterpenoid antibiotic terpentecin.
(2E,6E,10E)-geranylgeranyl diphosphate = terpentedienyl diphosphate.
Found in pathogenic prokaryotes such as Mycobacterium tuberculosis but not in non-pathogens such as Mycobacterium smegmatis so may play a role in pathogenicity.
The product of the reaction is subsequently dephosphorylated yielding tuberculosinol (halima-5,13-dien-15-ol).
geranylgeranyl diphosphate = tuberculosinyl diphosphate.
(S)-beta-bisabolene = (S)-beta-macrocarpene.
The carotenoid lycopene has the psi-end group at both ends.
When acting on one end, this enzyme forms delta-carotene.
When acting on both ends, it forms epsilon-carotene.
a carotenoid psi-end group = a carotenoid epsilon-end group.
Lycopene has a psi-end group at both ends.
When acting on one end, this enzyme forms gamma-carotene.
When acting on both ends it forms beta-carotene.
It also acts on neurosporene to give beta-zeacarotene.
a carotenoid psi-end group = a carotenoid beta-end derivative.
gamma-carotene = all-trans-beta-carotene.
all-trans-neurosporene = beta-zeacarotene.
prosolanapyrone II oxidase/prosolanapyrone III cyclosiomerase
The enzyme is involved in the biosynthesis of the phytotoxin solanapyrone in some fungi.
The bifunctional enzyme catalyzes the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to (-)-solanapyrone A (cf. EC 1.1.3.42).
prosolanapyrone III = (-)-solanapyrone A.
The enzyme from Tanacetum vulgare (tansey) can also use (3S)-linalyl diphosphate or more slowly neryl diphosphate in vitro.
The reaction proceeds via isomeration of geranyl diphosphate to (3S)-linalyl diphosphate.
The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (-)-bornyl diphosphate.
(2E)-geranyl diphosphate = (2R,4S)-bornyl diphosphate.
The enzyme is involved in the biosynthesis of aklaviketone, an intermediate in the biosynthetic pathways leading to formation of several anthracycline antibiotics, including aclacinomycin, daunorubicin and doxorubicin.
The enzyme has been described from plants and cyanobacteria.
It has similar activity with all four listed benzoquinol substrates.
Involved in the biosynthesis of vitamin E tocopherols and tocotrienols.
delta-tocopherol = 2-methyl-6-phytyl-1,4-benzene-1,4-diol.
gamma-tocopherol = 2,3-dimethyl-6-phytylbenzene-1,4-diol.
delta-tocotrienol = 6-geranylgeranyl-2-methylbenzene-1,4-diol.
gamma-tocotrienol = 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol.
3,6-anhydro-L-galactonate cycloisomerase
The enzyme, characterized from the marine bacteria Vibrio sp. EJY3 and Postechiella marina M091, is involved in a degradation pathway for 3,6-anhydro-alpha-L-galactopyranose, a major component of the polysaccharides of red macroalgae.
3,6-anhydro-L-galactonate = 2-dehydro-3-deoxy-L-galactonate.
The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate.
Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone.
D-galactaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate + H(+).
D-glucaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate + H(+).
Isolated from the hallucinogenic plant Salvia divinorum (seer's sage) and the medicinal plant Tripterygium wilfordii (thunder god vine).
(2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl diphosphate.
(2E,6E,10E)-geranylgeranyl diphosphate = (+)-kolavenyl diphosphate.
(2E,6E,10E)-geranylgeranyl diphosphate = (13E)-labda-7,13-dien-15-yl diphosphate.
The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, forms the core structure of the hapalindole family of alkaloids.
3-geranyl-3-[(Z)-2-isocyanoethenyl]-1H-indole = hapalindole H.
The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, forms the core structure of the 12-epi-hapalindole family of alkaloids.
3-geranyl-3-[(Z)-2-isocyanoethenyl]-1H-indole = 12-epi-hapalindole U.
The enzyme, characterized from multiple species of the cyanobacterial genus Fischerella, participates in the biosynthesis of the terpenoid indole alkaloids 12-epi-fischerindoles.
3-geranyl-3-[(Z)-2-isocyanoethenyl]-1H-indole = 12-epi-fischerindole U.
The product is a precursor of (+)-cis,trans-nepetalactone, the primary ingredient responsible for the psychoactive effects catnip has on cats.
(S)-8-oxocitronellyl enol = cis-trans-nepetalactol.
The product is a precursor of (+)-cis,cis-nepetalactone, one of the stereoisomers responsible for the psychoactive effects catnip has on cats.
(S)-8-oxocitronellyl enol = cis-cis-nepetalactol.
Isomerases altering macromolecular conformation
Enzymes altering polypeptide conformation or assembly
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
A multisubunit protein complex associated with microtubules.
Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome toward the microtubule's minus end.
It also functions in the movement of eukaryotic flagella and cilia.
It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa).
ATP + H2O + a dynein associated with a microtubule at position (n) = ADP + phosphate + a dynein associated with a microtubule at position (n-1, toward the minus end).
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyze ATP.
The enzymes described here move toward the plus end of the microtubule, in contrast to EC 5.6.1.2 and EC 5.6.1.4.
They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons.
The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
ATP + H2O + a kinesin associated with a microtubule at position (n) = ADP + phosphate a kinesin associated with a microtubule at position (n+1, toward the plus end).
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyze ATP and are involved in organelle movement.
This enzyme is similar to EC 5.6.1.3 but the organization of the different domains differs, resulting in movement in the opposite direction along the microtubules.
ATP + H2O + a kinesin associated with a microtubule at position (n) = ADP + phosphate + a kinesin associated with a microtubule at position (n-1, toward the minus end).
Belongs to the AAA-type superfamily and, like EC 5.6.1.4, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome.
Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
ATP + H2O + polypeptide = ADP + phosphate + unfolded polypeptide.
cystic-fibrosis membrane-conductance-regulating protein
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains.
The enzyme is found in animals, and in humans its absence brings about cystic fibrosis.
Unlike most of the ABC transporters, chloride pumping is not directly coupled to ATP hydrolysis.
Instead, the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains.
The enzyme is also involved in the functioning of other transmembrane channels.
ATP + H2O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts.
Molecular masses of subunits ranges from 10-90 kDa.
They are a subclass of molecular chaperones that are related to EC 5.6.1.5.
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa).
The head region of the heavy chain contains actin- and ATP-binding sites.
ATP hydrolysis provides energy for actomyosin contraction.
ATP + H2O + myosin bound to actin filament at position(n) = ADP + phosphate + myosin bound to actin filament at position(n+1).
(R)-2-hydroxyacyl-CoA dehydratase activating ATPase
(R)-2-hydroxyacyl-CoA dehydratase activase
Members of the (R)-2-hydroxyacyl-CoA dehydratase family (including EC 4.2.1.54, EC 4.2.1.157, EC 4.2.1.167 and EC 4.2.1.175) are two-component systems composed of an activator component and a dehydratase component.
The activator is an extremely oxygen-sensitive homodimer with one [4Fe-4S] cluster bound at the dimer interface.
Before it can catalyze the dehydration reaction, the dehydratase requires one high-energy electron that is used to transiently reduce the electrophilic thiol ester carbonyl to a nucleophilic ketyl radical anion, facilitating the elimination of the hydroxyl group.
The activator, which has been named archerase because its open position resembles an archer shooting arrows, binds two ADP molecules.
Upon the reduction of its [4Fe-4S] cluster by a single electron, delivered by a dedicated flavodoxin or a clostridial ferredoxin, the two ADP molecules exchange for two ATP molecules, resulting in a large conformational change.
The change allows the activator to bind to the dehydratase component and transfer the electron to it, activating it.
During this event the two ATP molecules are hydrolyzed and the activator returns to its resting state.
Since the electron is regenerated at the end of each reaction cycle of the dehydratase, the activation is required only once, before the first reaction takes place.
2 ATP + a reduced flavodoxin + an inactive (R)-2-hydroxyacyl-CoA dehydratase + 2 H2O = 2 ADP + 2 phosphate + a flavodoxin semiquinone + an active (R)-2-hydroxyacyl-CoA dehydratase.
Enzymes altering nucleic acid conformation
These enzymes bring about the conversion of one topological isomer of DNA into another, e.g., the relaxation of superhelical turns in DNA, the interconversion of simple and knotted rings of single-stranded DNA, and the intertwisting of single-stranded rings of complementary sequences, cf. EC 5.6.2.2.
ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
The enzyme can introduce negative superhelical turns into double-stranded circular DNA.
One unit has nicking-closing activity, and another catalyzes super-twisting and hydrolysis of ATP (cf. EC 5.6.2.2).
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
The activity is stimulated by DNA polymerase III.
As the lagging ssDNA is created, it becomes coated with S Single-Stranded DNA Binding protein (SSB).
Once every 500-2000 nucleotides, primase is stimulated by DnaB helicase to synthesize a primer at the replication fork.
This primer is elongated by the lagging strand half of DNA polymerase III holoenzyme.
Couples ATP hydroysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.
Helicases are motor proteins that can transiently catalyze the unwinding of energetically stable duplex DNA or RNA molecules by using ATP hydrolysis as the source of energy (although other nucleoside triphosphates can replace ATP in some cases).
DNA helicases unwind duplex DNA and are involved in replication, repair, recombination, transcription, pre-rRNA processing, and translation initiation.
Mechanistically, DNA helicases are divided into those that can translocate in the 3'-5' direction and those that translocate in the 5'-3' direction with respect to the strand on which they initially bind.
This entry describes a number of DNA helicases that translocate in the 3'-5' direction.
Many of the enzymes require a 3' single-stranded DNA tail.
The Rep protein is a component of the bacterial replisome, providing a replication fork-specific motor. The UvrD enzyme, found in Gram-negative bacteria, is involved in maintenance of chromosomal integrity. The RecQ proteins are a family of eukaryotic helicases that are involved in DNA replication, transcription and repair. The Mer3 helicase, found in fungi and plants, is required for crossover formation during meiosis. cf. EC 5.6.2.3, DNA 5'-3' helicase.
Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
benzyl isothiocyanate = benzyl thiocyanate.
2-hydroxychromene-2-carboxylate isomerase
2-hydroxychromene-2-carboxylate = (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate.
Ligases forming aminoacyl-tRNA and related compounds
L-tyrosine-tRNA(Tyr) ligase (AMP-forming)
tyrosine-transfer ribonucleate synthetase
tyrosyl-transfer ribonucleate synthetase
tyrosyl-transfer ribonucleic acid synthetase
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr).
L-tryptophan-tRNA(Trp) ligase (AMP-forming)
tryptophanyl-transfer ribonucleate synthetase
tryptophanyl-transfer ribonucleic acid synthetase
tryptophanyl-transfer ribonucleic synthetase
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp).
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr).
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).
ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).
ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val).
methionyl-transfer ribonucleate synthetase
methionyl-transfer ribonucleic acid synthetase
In those organisms producing N-formylmethionyl-tRNA(fMet) for translation initiation, this enzyme also recognizes the initiator tRNA(fMet) and catalyzes the formation of L-methionyl-tRNA(fMet), the substrate for EC 2.1.2.9.
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).
seryl-transfer ribonucleic acid synthetase
This enzyme also recognizes tRNA(Sec), the special tRNA for selenocysteine, and catalyzes the formation of L-seryl-tRNA(Sec), the substrate for EC 2.9.1.1.
ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser).
ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec).
ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
D-alanine-D-alanyl carrier protein ligase
D-alanyl-poly(phosphoribitol) synthetase
A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine.
Involved in the synthesis of teichoic acids.
ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate).
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).
ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe).
ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His).
ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn).
nondiscriminating aspartyl-tRNA synthetase
When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12.
It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn).
This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon.
This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon).
The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn).
ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx).
nondiscriminating glutamyl-tRNA synthetase
When this enzyme acts on tRNA(Glu), it catalyzes the same reaction as EC 6.1.1.17.
It has, however, diminished discrimination, so that it can also form glutamate-tRNA(Gln).
This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1(Gln) (UUG anticodon) and tRNA(Glu) (UUC anticodon) but not tRNA2(Gln) (CUG anticodon).
The ability of this enzyme to recognize both tRNA(Glu) and one of the tRNA(Gln) isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine).
The glutamyl-tRNA(Gln) is not used in protein synthesis until it is converted by EC 6.3.5.7 into glutaminyl-tRNA(Gln).
ATP + L-glutamate + tRNA(Glx) = AMP + diphosphate + L-glutamyl-tRNA(Glx).
In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNA(Pyl), with a CUA anticodon, can be charged directly with pyrrolysine by this class II aminoacyl--tRNA ligase.
Specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids.
ATP + L-pyrrolysine + tRNA(Pyl) = AMP + diphosphate + L-pyrrolysyl-tRNA(Pyl).
ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys).
The product of this enzyme, the depsipeptide D-alanyl-(R)-lactate, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4.
The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria.
(R)-lactate + ATP + D-alanine = ADP + D-alanyl-(R)-lactate + phosphate.
The enzyme from the bacterium Streptoalloteichus tenebrarius catalyzes the activation of carbamoyl phosphate to O-carbamoyladenylate and the subsequent carbamoylation of kanamycin and tobramycin.
ATP + carbamoyl phosphate + H2O + tobramycin = AMP + diphosphate + H(+) + nebramycin 5' + phosphate.
ATP + carbamoyl phosphate + H2O + kanamycin A = 6''-O-carbamoylkanamycin A + AMP + diphosphate + H(+) + phosphate.
The enzyme, found in certain bacterial species, participates in a pathway for the production of olefins.
The alkyl group at C(2) of the substrate ends up as the 3-alkyl group of the product.
a (2R,3S)-2-alkyl-3-hydroxyalkanoate + ATP = a cis-3-alkyl-4-alkyloxetan-2-one + AMP + diphosphate.
acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate.
Acts on fatty acids from C4 to C11 and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids.
The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives.
a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate.
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity.
The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate.
Itaconate can act instead of succinate, and ITP instead of GTP.
CoA + GTP + succinate = GDP + phosphate + succinyl-CoA.
ATP + CoA + succinate = ADP + phosphate + succinyl-CoA.
ATP + CoA + glutarate = ADP + glutaryl-CoA + phosphate.
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase (AMP-forming)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate--CoA ligase
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase
This membrane-bound enzyme catalyzes the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters.
The second step involves EC 2.3.1.65 and converts the acyl-CoA thioester into the corresponding N-acyl amidate by conjugation with glycine or taurine.
Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates.
ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate.
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + ATP + CoA = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + AMP + diphosphate.
ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA + diphosphate.
ATP + CoA + lithocholate = AMP + diphosphate + lithocholoyl-CoA.
ATP + CoA + deoxycholate = AMP + deoxycholoyl-CoA + diphosphate.
ATP + CoA + oxalate = AMP + diphosphate + oxalyl-CoA.
(S)-malate + ATP + CoA = (S)-malyl-CoA + ADP + phosphate.
a carboxylate + CoA + GTP = an acyl-CoA + GDP + phosphate.
ATP + biotin + CoA = AMP + biotinyl-CoA + diphosphate.
(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate.
Also acts on propanoate and, very slowly, on butanoate.
acetate + ATP + CoA = acetyl-CoA + ADP + phosphate.
ATP + CoA + propanoate = ADP + phosphate + propanoyl-CoA.
ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP + diphosphate.
8,11,14-icosatrienoate, but not the other long-chain fatty acids, can act in place of arachidonate.
(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate.
Also acts, more slowly, on L-3-hydroxybutanoate.
acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP + diphosphate.
Propenoate can act instead of propanoate.
Not identical with EC 6.2.1.1 or EC 6.2.1.2.
ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA.
ATP + citrate + CoA = (3S)-citryl-CoA + ADP + phosphate.
Together with a hydrolase component (EC 3.1.2.2/3.1.2.14) and a reductase component (EC 1.2.1.50), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3).
The enzyme activates free long-chain fatty acids, generated by the action of the transferase component, forming a fatty acyl-AMP intermediate, followed by the transfer of the acyl group to an internal L-cysteine residue.
It then transfers the acyl group to EC 1.2.1.50.
a long-chain fatty acid + ATP + L-cysteinyl-[protein] = AMP + diphosphate + S-(long-chain fatty acyl)-L-cysteinyl-[protein].
long-chain-fatty-acid--[acyl-carrier-protein] ligase
The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein.
a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate.
Both this enzyme and EC 2.3.1.49 acetylate and activate EC 4.1.3.6.
acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate.
Acts on dicarboxylic acids of chain length C5 to C16; the best substrate is dodecanedioic acid.
a dicarboxylate + ATP + CoA = AMP + diphosphate + omega-dicarboxyl-CoA.
3,7,11,15-tetramethylhexadecanoate + ATP + CoA = AMP + diphosphate + phytanoyl-CoA.
Also acts on 2-, 3- and 4-fluorobenzoate, but only very slowly on the corresponding chlorobenzoates.
ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate.
2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP + diphosphate.
4-hydroxybenzoate + ATP + CoA = 4-hydroxybenzoyl-CoA + AMP + diphosphate.
3alpha,7alpha-dihydroxy-5beta-cholestanate--CoA ligase
(25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate + ATP + CoA = (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oyl-CoA + AMP + diphosphate.
Also acts, more slowly, on acetate, propanoate and butanoate, but not on hydroxy derivatives of phenylacetate and related compounds.
2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA.
2-furoate + ATP + CoA = 2-furoyl-CoA + AMP + diphosphate.
anthranilate + ATP + CoA = AMP + anthraniloyl-CoA + diphosphate.
Part of the bacterial 2,4-dichlorobenzoate degradation pathway.
4-chlorobenzoate + ATP + CoA = 4-chlorobenzoyl-CoA + AMP + diphosphate.
It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction.
(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + ADP + phosphate.
(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphate.
This enzyme, from the anaerobic bacterium Malonomonas rubra, is a component of the multienzyme complex EC 7.2.4.4.
The enzyme uses the energy from hydrolysis of ATP to convert the thiol group of the acyl-carrier-protein-bound 2'-(5-phosphoribosyl)-3'-dephospho-CoA prosthetic group into its acetyl thioester.
acetate + ATP + holo-[ACP] = acetyl-[ACP] + AMP + diphosphate.
3-hydroxypropionyl-CoA synthetase (AMP-forming)
The enzymes from Metallosphaera sedula and Sulfolobus tokodaii can also use propanoate, acrylate, acetate, and butanoate as substrates, and are thus different from EC 6.2.1.17, which does not accept acetate or butanoate.
3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP + diphosphate.
3-hydroxybenzoate--coenzyme A ligase (AMP-forming)
The enzyme works equally well with 4-hydroxybenzoate but shows low activity toward benzoate, 4-aminobenzoate, 3-aminobenzoate, 3-fluorobenzoate, 4-fluorobenzoate, 3-chlorobenzoate, and 4-chlorobenzoate.
There is no activity with 3,4-dihydroxybenzoate, 2,3-dihydroxybenzoate, and 2-hydroxybenzoate as substrates.
3-hydroxybenzoate + ATP + CoA = 3-hydroxybenzoyl-CoA + AMP + diphosphate.
(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase
2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA synthetase
Forms part of the pathway of camphor catabolism.
[(1R)-2,2,3-trimethyl-5-oxocyclopent-3-en-1-yl]acetate + ATP + CoA = [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + AMP + diphosphate.
[butirosin acyl-carrier protein]--L-glutamate ligase
[BtrI acyl-carrier protein]--L-glutamate ligase
Catalyzes two steps in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family.
The enzyme adds one molecule of L-glutamate to a dedicated acyl-carrier protein, and following decarboxylation of the product by EC 4.1.1.95, adds a second L-glutamate molecule.
ATP + holo-[BtrI ACP] + L-glutamate = ADP + gamma-L-glutamyl-[BtrI ACP] + phosphate.
4-aminobutanoyl-[BtrI ACP] + ATP + L-glutamate = 4-(gamma-L-glutamylamino)butanoy-[BtrI ACP] + ADP + H(+) + phosphate.
4-hydroxybutyrate--CoA ligase (AMP-forming)
Isolated from the archaeon Metallosphaera sedula.
Involved in the 3-hydroxypropanoate/4-hydroxybutanoate cycle.
4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate.
3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate--CoA ligase
The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyzes a step in the degradation of cholesterol and cholate.
The enzyme is very specific for its substrate, and requires that the side chain at C17 is completely removed.
3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate + ATP + CoA = 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoyl-CoA + AMP + diphosphate.
The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyzes a step in the degradation of cholesterol.
It is responsible for the activation of the C8 side chain.
3beta-hydroxycholest-5-en-26-oate can also be used as substrate.
(25S)-3-oxocholest-4-en-26-oate + ATP + CoA = (25S)-3-oxocholest-4-en-26-oyl-CoA + AMP + diphosphate.
2-hydroxy-7-methoxy-5-methyl-1-naphthoate--CoA ligase
The enzyme from the bacterium Streptomyces carzinostaticus is involved in the attachment of the 2-hydroxy-7-methoxy-5-methyl-1-naphthoate moiety of the antibiotic neocarzinostatin.
In vitro the enzyme also catalyzes the activation of other 1-naphthoic acid analogs, e.g. 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate.
2-hydroxy-7-methoxy-5-methyl-1-naphthoate + ATP + CoA = 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA + AMP + diphosphate.
methylmercaptopropionate-coenzyme A ligase
The enzyme is part of a dimethylsulfoniopropanoate demethylation pathway in the marine bacteria Ruegeria pomeroyi and Pelagibacter ubique.
It also occurs in some nonmarine bacteria capable of metabolizing dimethylsulfoniopropionate (e.g. Burkholderia thailandensis, Pseudomonas aeruginosa, and Silicibacter lacuscaerulensis).
3-(methylsulfanyl)propanoate + ATP + CoA = 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate.
Catalyzes the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein.
The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step.
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.
L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase
L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase
This two-domain protein from the bacterium Pseudomonas syringae contains an adenylation domain (A domain) and a thiolation domain (T domain).
It catalyzes the adenylation of L-allo-isoleucine and its attachment to the T domain.
The enzyme is involved in the biosynthesis of the toxin coronatine, which mimics the plant hormone jasmonic acid isoleucine.
Coronatine promotes opening of the plant stomata allowing bacterial invasion, which is followed by bacterial growth in the apoplast, systemic susceptibility, and disease.
ATP + holo-[CmaA peptidyl-carrier protein] + L-alloisoleucine = AMP + diphosphate + L-alloisoleucyl-[CmaA peptidyl-carrier protein].
medium-chain-fatty-acid--[acyl-carrier-protein] ligase
The enzyme ligates medium chain fatty acids (with aliphatic chain of 6-12 carbons) to an acyl-carrier protein.
a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain fatty acyl-[ACP] + AMP + diphosphate.
The enzyme, originally characterized from the bacterium Escherichia coli, can catalyze the transfer of CoA to L-carnitine, crotonobetaine and gamma-butyrobetaine.
In vitro the enzyme also exhibits the activity of EC 2.8.3.21.
(R)-carnitine + ATP + CoA = (R)-carnitinyl-CoA + AMP + diphosphate.
ATP + CoA + crotonobetaine = AMP + crotonobetainyl-CoA + diphosphate.
4-(trimethylamino)butanoate + ATP + CoA = AMP + diphosphate + gamma-butyrobetainyl-CoA.
long-chain fatty acid adenylyltransferase FadD28
The enzyme, found in certain mycobacteria, activates long-chain fatty acids by adenylation and transfers them to EC 2.3.1.111.
The enzyme participates in the biosynthesis of the virulent lipids dimycocerosates (DIM) and dimycocerosyl triglycosyl phenolphthiocerol (PGL).
a long-chain fatty acid + ATP + holo-[mycocerosate synthase] = AMP + diphosphate + long-chain fatty acyl-[mycocerosate synthase].
4-hydroxybenzoate adenylyltransferase FadD22
This mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols.
Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to EC 2.3.1.261.
4-hydroxybenzoate + ATP + holo-[4-hydroxyphenylalkanoate synthase] = 4-hydroxyphenyl-[4-hydroxyphenylalkanoate synthase] + AMP + diphosphate.
4-hydroxyphenylalkanoate adenylyltransferase FadD29
The mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols.
Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to the phenolphthiocerol/phthiocerol polyketide synthase.
17-(4-hydroxyphenyl)heptadecanoate + ATP + holo-[(phenol)carboxyphthiodiolenone synthase] = 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate.
19-(4-hydroxyphenyl)nonadecanoate + ATP + holo-[(phenol)carboxyphthiodiolenone synthase] = 19-(4-hydroxyphenyl)nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate.
This is an alternative activity of the firefly luciferase (EC 1.13.12.7), which the enzyme exhibits under normal conditions only when acting on the L-enantiomer of its substrate.
The D-isomer can act as a substrate for the CoA--ligase activity in vitro only under low oxygen conditions that are not found in vivo.
The activation of L-firefly luciferin to a CoA ester is a step in a recycling pathway that results in its epimerization to the D enantiomer, which is the only substrate whose oxygenation results in light emission.
ATP + CoA + firefly L-luciferin = AMP + diphosphate + L-firefly luciferyl-CoA.
L-proline--[L-prolyl-carrier protein] ligase
It catalyzes the activation of L-proline to an adenylate form, followed by its transfer to the 4'-phosphopantheine moiety of an L-prolyl-carrier protein.
ATP + holo-[peptidyl-carrier protein] + L-proline = AMP + diphosphate + L-prolyl-[peptidyl-carrier protein].
D-alanine--[D-alanyl-carrier protein] ligase
The enzyme is involved in the modification of wall teichoic acids, as well as type I and IV lipoteichoic acids, with D-alanine residues.
It activates D-alanine using ATP to form a high-energy (D-alanyl)adenylate intermediate and subsequently transfers the alanyl moiety to the phosphopantheinyl prosthetic group of a D-alanyl-carrier protein (DltC).
ATP + D-alanine + holo-[D-alanyl-carrier protein] = AMP + D-alanyl-[D-alanyl-carrier protein] + diphosphate.
The enzyme catalyzes the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea.
SAMPs are involved in protein degradation, and also act as sulfur carriers involved in thiolation of tRNA and other metabolites such as molybdopterin.
The enzyme catalyzes the ATP-dependent formation of a SAMP adenylate intermediate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage.
This intermediate can accept a sulfur atom to form a thiocarboxylate moiety in a mechanism that is not yet understood.
Alternatively, the E1 enzyme can transfer SAMP from its activated form to an internal cysteine residue, releasing AMP.
In this case SAMP is subsequently transferred to a lysine residue in a target protein in a process termed SAMPylation.
Auto-SAMPylation (attachment of SAMP to lysine residues within the E1 enzyme) has been observed.
ATP + [SAMP]-Gly-Gly + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP + diphosphate.
4-hydroxybutyrate--CoA ligase (ADP-forming)
The enzyme, characterized from the marine ammonia-oxidizing archaeon Nitrosopumilus maritimus, participates in a variant of the 3-hydroxypropanoate/4-hydroxybutanate CO2 fixation cycle.
4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + ADP + phosphate.
long-chain fatty acid adenylase/transferase FadD23
long-chain fatty acid adenylyltransferase FadD23
This mycobacterial enzyme activates palmitate and stearate by adenylation, followed by their loading onto the polyketide synthase EC 2.3.1.287.
ATP + holo-[(hydroxy)phthioceranic acid synthase] + octadecanoate = AMP + diphosphate + octadecanoyl-[(hydroxy)phthioceranic acid synthase].
ATP + hexadecanoate + holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + hexadecanoyl-[(hydroxy)phthioceranic acid synthase].
The enzyme, characterized from the bacterium Syntrophorhabdus aromaticivorans, catalyzes the first step in an anaerobic isophthalate degradation pathway.
ATP + CoA + isophthalate = AMP + diphosphate + isophthalyl-CoA.
long-chain fatty acid adenylase/transferase FadD26
The enzyme, present in pathogenic species of mycobacteria, participates in the pathway for biosynthesis of phthiocerols.
It catalyzes the adenylation of the long-chain fatty acids arachidate (C20) or behenate (C22) and potentially the very-long-chain fatty acid lignocerate (C24).
The activated fatty acids are then loaded to EC 2.3.1.292.
a long-chain fatty acid + ATP + holo-[(phenol)carboxyphthiodiolenone synthase] = a long-chain fatty acyl-[(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate.
ATP + eicosanoate + holo-[(phenol)carboxyphthiodiolenone synthase] = AMP + diphosphate + icosanoyl-[(phenol)carboxyphthiodiolenone synthase].
ATP + docosanoate + holo-[(phenol)carboxyphthiodiolenone synthase] = AMP + diphosphate + docosanoyl-[(phenol)carboxyphthiodiolenone synthase].
The enzyme, characterized from the bacterium Pseudoalteromonas sp. SANK 73390, catalyzes the CoA acylation of pseudomonic and marinolic acids, as part of the biosynthesis of thiomarinols and related compounds.
ATP + a marinolic acid + CoA = AMP + diphosphate + a marinoloyl-CoA.
ATP + a pseudomonic acid + CoA = AMP + diphosphate + a pseudomonoyl-CoA.
ATP + CoA + marinolate C = AMP + diphosphate + marinoloyl-CoA C.
ATP + CoA + pseudomonate C = AMP + diphosphate + pseudomonoyl-CoA C.
salicylate--[aryl-carrier protein] ligase
The enzyme catalyzes the activation of salicylate to (salicyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein, which is often a domain of a larger non-ribosimal peptide synthase.
The PmsE enzyme is involved in pseudomonine biosynthesis and transfers the activated salicylate first to itself, and then to a PmsG protein.
The PchD enzyme is involved in pyochelin biosynthesis and transfers the activated salicylate directly to the PchE protein.
ATP + holo-[non-ribosomal peptide synthase] + salicylate = AMP + diphosphate + salicyl-[non-ribosomal peptide synthase].
3,4-dihydroxybenzoate--[aryl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of 3,4-dihydroxybenzoate to (3,4-dihydroxybenzoyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain.
The aryl-carrier protein domain may be part of the same protein, or of a different protein.
This activity is often found as part of a larger non-ribosomal peptide synthase.
3,4-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] = 3,4-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate.
L-arginine--[L-arginyl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-arginine to (L-arginyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
The peptidyl-carrier protein domain may be part of the same protein, or of a different protein.
ATP + holo-[peptidyl-carrier protein] + L-arginine = AMP + diphosphate + L-arginyl-[peptidyl-carrier protein].
The E1 NEDD8-activating enzyme activates NEDD8 in an ATP-dependent reaction by forming a high-energy thioester intermediate between NEDD8 and one of its cysteine residues.
The activated NEDD8 is subsequently transferred to a cysteine residue of EC 2.3.2.34, and is eventually conjugated to a lysine residue of specific substrates in the presence of the appropriate E3 transferase (EC 2.3.2.32).
ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine.
The enzyme, characterized from the bacteria Thauera aromatica and Streptomyces sp. WA46, participates in a salicylate degradation pathway.
It activates salicylate by its adenylation to (2-hydroxybenzoyl)adenylate, followed by the transfer of the activated compound to coenzyme A.
ATP + CoA + salicylate = 2-hydroxybenzoyl-CoA + AMP + diphosphate.
The adenylation domain of the enzyme catalyzes the activation of glycine to (glycyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein.
ATP + glycine + holo-[peptidyl-carrier protein] = AMP + diphosphate + glycyl-[peptidyl-carrier protein].
L-alanine--[L-alanyl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-alanine to (L-alanyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
ATP + holo-[peptidyl-carrier protein] + L-alanine = AMP + diphosphate + L-alanyl-[peptidyl-carrier protein].
L-glutamate--[L-glutamyl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-glutamate to (L-glutamyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
ATP + holo-[peptidyl-carrier protein] + L-glutamate = AMP + diphosphate + L-glutamyl-[peptidyl-carrier protein].
L-cysteine--[L-cysteinyl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-cysteine to (L-cysteinyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
ATP + holo-[peptidyl-carrier protein] + L-cysteine = AMP + diphosphate + L-cysteinyl-[peptidyl-carrier protein].
L-threonine--[L-threonyl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-threonine to (L-threonyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein (as in the case of PmsD in pseudomonine biosynthesis).
ATP + holo-[peptidyl-carrier protein] + L-threonine = AMP + diphosphate + L-threonyl-[peptidyl-carrier protein].
2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of 2,3-dihydroxybenzoate to (2,3-dihydroxybenzoyl)adenylate, followed by the transfer the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain of a specific non-ribosomal peptide synthase.
For example, the EntE enzyme of Escherichia coli is part of the enterobactin synthase complex, the VibE enzyme of Vibrio cholerae is part of the vibriobactin synthase complex, and the DhbE enzyme of Bacillus subtilis is part of the bacillibactin synthase complex.
2,3-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] = 2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate.
L-serine--[L-seryl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-serine to (L-seryl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
ATP + holo-[peptidyl-carrier protein] + L-serine = AMP + diphosphate + L-seryl-[peptidyl-carrier protein].
L-tryptophan--[L-tryptophyl-carrier protein] ligase
The adenylation domain of the enzyme catalyzes the activation of L-tryptophan to (L-tryptophyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain.
ATP + holo-[peptidyl-carrier protein] + L-tryptophan = AMP + diphosphate + L-tryptophyl-[peptidyl-carrier protein].
3-amino-5-hydroxybenzoate--[acyl-carrier protein] ligase
During the biosynthesis of most ansamycin antibiotics such as rifamycins, streptovaricins, naphthomycins, and chaxamycins, the activity is catalyzed by the loading domain of the respective polyketide synthase (PKS), which transfers the substrate to the acyl-carrier protein domain of the first extension module of the PKS.
During the biosynthesis of the mitomycins the reaction is catalyzed by the MitE protein, which transfers the substrate to a dedicated acyl-carrier protein (MmcB).
3-amino-5-hydroxybenzoate + ATP + holo-[aryl-carrier protein] = 3-amino-5-hydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate.
amino acid--[acyl-carrier-protein] ligase
Catalyzes the ATP-dependent activation of L-alanine, and to a lesser extent of L-glycine and L-serine, and their transfer to the phosphopantetheine prosthetic group covalently attached to a vicinal carrier protein.
May participate in nonribosomal peptide synthesis or related processes.
L-proline and L-glutamate are very poor substrates whereas D-amino acids are not substrates for ATP-dependent activation.
Does not display tRNA aminoacylation activity.
an L-alpha-amino acid + ATP + holo-[ACP] = AMP + an L-alpha-aminoacyl-[ACP] + diphosphate.
The enzyme, found in mitochondria, detoxifies malonate, which is a potent inhibitor of mitochondrial respiration, and provides malonyl-CoA to the mitochondrial fatty acid biosynthesis pathway.
ATP + CoA + malonate = AMP + diphosphate + malonyl-CoA.
The enzyme is found in anaerobic methanogenic and methanotrophic archaea, where it modifies a glycine residue in EC 2.8.4.1.
Upon binding to its substrate, an external source of sulfide attacks the target amide bond generating a tetrahedral intermediate.
The amide oxyanion attacks the gamma-phosphate of ATP, releasing ADP and forming a phosphorylated thiolate intermediate that collapses to form thioglycine and phosphate.
In most organisms activity requires a second protein (TfuA) , which may allosterically activate this enzyme or assist in the delivery of sulfide to the substrate.
ATP + glycyl-[methyl-coenzyme M reductase] + hydrogen sulfide = ADP + phosphate + thioglycyl-[methyl-coenzyme M reductase].
The enzyme, which participates in the biosynthesis of ribosomal peptide natural products (RiPPs), converts L-cysteine, L-serine and L-threonine residues to thiazoline, oxazoline, and methyloxazoline rings, respectively.
The enzyme requires two domains - a cyclodehydratase domain, known as a YcaO domain, and a substrate recognition domain (RRE domain) that controls the regiospecificity of the enzyme.
The RRE domain can either be fused to the YcaO domain or occur as a separate protein; however both domains are required for activity.
The enzyme can process multiple residues within the same substrate peptide, and all enzymes characterized so far follow a defined order, starting with the L-cysteine closest to the C-terminus.
The reaction involves phosphorylation of the preceding ribosomal peptide backbone amide bond, forming ADP and a phosphorylated intermediate, followed by release of the phosphate group.
In some cases the enzyme catalyzes a side reaction in which the phosphorylated intermediate reacts with ADP to form AMP and diphosphate.
ATP + L-amino acyl-L-seryl-[protein] = (S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline-[protein] + ADP + H(+) + phosphate.
ATP + L-amino acyl-L-threonyl-[protein] = (S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline-[protein] + ADP + H(+) + phosphate.
ATP + L-amino acyl-L-cysteinyl-[protein] = (1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline-[protein] + ADP + H(+) + phosphate.
The enzyme, which participates in the biosynthesis of some ribosomal peptide natural products (RiPPs) such as the trunkamides, converts L-cysteine residues to thiazoline rings.
The enzyme can process multiple L-cysteine residues within the same substrate peptide, and all enzymes characterized so far follow a defined order, starting with the L-cysteine closest to the C-terminus.
This activity is also catalyzed by the related enzyme EC 6.2.2.2.
That enzyme differs by having an RRE domain that also recognizes L-serine and L-threonine residues, which are converted to oxazoline and methyloxazoline rings, respectively.
Acid--ammonia (or amine) ligases (amide synthases)
ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-asparagine.
Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life.
Several types have been described, differing in their oligomeric structures and cofactor requirements.
ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate.
ATP + L-aspartate + NH4(+) = ADP + H(+) + L-asparagine + phosphate.
L-glutamine also acts, more slowly, as amido-donor (cf. EC 6.3.5.1).
ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+).
ATP + ethylamine + L-glutamate = ADP + H(+) + N(5)-ethyl-L-glutamine + phosphate.
Glutamine can act instead of NH3, more slowly.
4-methylene-L-glutamate + ATP + NH4(+) = 4-methylene-L-glutamine + AMP + diphosphate + H(+).
gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming)
glutathione:spermidine ligase (ADP-forming)
Involved in the synthesis of trypanothione in trypanosomatids.
The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 3.5.1.78 reaction, resulting in a net hydrolysis of ATP.
ATP + glutathione + spermidine = ADP + glutathionylspermidine + H(+) + phosphate.
The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyzes two subsequent reactions, leading to production of trypanothione from glutathione and spermidine.
Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 6.3.1.8).
The enzyme is bifunctional, and also catalyzes the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 3.5.1.78).
ATP + glutathione + glutathionylspermidine = ADP + H(+) + phosphate + trypanothione.
This enzyme forms part of the anaerobic cobalamin biosynthesis pathway.
One of the substrates for this reaction, (R)-1-aminopropan-2-yl phosphate, is produced by CobD (EC 4.1.1.81).
(R)-1-aminopropan-2-yl phosphate + adenosylcob(III)yrate + ATP = adenosylcob(III)inamide phosphate + ADP + H(+) + phosphate.
(R)-1-aminopropan-2-ol + adenosylcob(III)yrate + ATP = adenosylcob(III)inamide + ADP + H(+) + phosphate.
Forms part of a bacterial putrescine utilization pathway.
ATP + L-glutamate + putrescine = ADP + gamma-L-glutamylputrescine + H(+) + phosphate.
Forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp.
Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium.
Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed.
Highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates.
In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13.
[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n) + n ATP + n D-aspartate = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + n ADP + n H(+) + n phosphate.
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
This enzyme is a key enzyme in the biosynthesis of mycothiol, a small molecular weight thiol found in Mycobacteria spp. and other actinomycetes.
Mycothiol plays a fundamental role in these organisms by helping to provide protection from the effects of reactive oxygen species and electrophiles, including many antibiotics.
The enzyme may represent a novel target for new classes of antituberculars.
1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + H(+).
This amidase catalyzes the last step in the conversion of an L-histidine residue in the translation elongation factor translation elongation factor 2 to diphthamide.
This factor is found in all archaebacteria and eukaryotes, but not in eubacteria, and is the target of bacterial toxins such as the diphtheria toxin and the Pseudomonas exotoxin A (see EC 2.4.2.36).
The substrate of the enzyme, diphthine, is produced by EC 2.1.1.98.
ATP + diphthine-[translation elongation factor 2] + NH4(+) = AMP + diphosphate + diphthamide-[translation elongation factor 2] + H(+).
3-amino-4,7-dihydroxycoumarin + 3-dimethylallyl-4-hydroxybenzoate + ATP = 8-desmethylnovobiocic acid + AMP + diphosphate.
The enzyme, found in animals, also has the activity of EC 6.3.2.41.
ATP + citrate + L-glutamate = ADP + beta-citrylglutamate + H(+) + phosphate.
The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyzes the first step in the degradation of aniline.
It can also accept chlorinated and methylated forms of aniline, preferrably in the o- and p-positions.
aniline + ATP + L-glutamate = ADP + N(5)-phenyl-L-glutamine + phosphate.
prokaryotic ubiquitin-like protein ligase
The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum.
It catalyzes the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an epsilon-amino group of a lysine residue of the target protein and the gamma-carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup).
The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation.
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine.
This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid.
The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
Lipoylation is essential for the function of these enzymes.
The enzyme can also use octanoate instead of lipoate.
(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+).
phosphoribosylglycinamide formyltransferase 2
5'-phosphoribosylglycinamide transformylase 2
glycinamide ribonucleotide transformylase 2
This enzyme requires ATP and utilizes formate, which is provided by the hydrolysis of 10-formyltetrahydrofolate by EC 3.5.1.10.
The other enzyme, EC 2.1.2.2, utilizes 10-formyltetrahydrofolate directly.
Formyl phosphate is formed during catalysis as an intermediate.
The enzyme from the bacterium Escherichia coli can also catalyze the activity of EC 2.7.2.1.
ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate.
Acid--amino-acid ligases (peptide synthases)
pantoate--beta-alanine ligase (AMP-forming)
(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+).
Can use L-aminohexanoate in place of glutamate.
ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate.
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate.
Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide.
ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate.
phosphopantothenate--cysteine ligase (CTP)
(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine.
phosphoribosylaminoimidazolesuccinocarboxamide synthase
4-(N-succinocarboxamide)-5-aminoimidazole synthetase
4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide synthetase
5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
phosphoribosylaminoimidazole-succinocarboxamide synthase
phosphoribosylaminoimidazolesuccinocarboxamide synthetase
phosphoribosylaminoimidazole-succinocarboxamide synthetase
Forms part of the purine biosynthesis pathway.
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate.
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase
uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine synthetase
Involved in the synthesis of a cell-wall peptide.
This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC 6.3.2.13 adds 2,6-diaminopimelate instead.
ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine.
UDP-N-acetylmuramoyl-L-alanine synthetase
uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase
uridine diphosphate N-acetylmuramate:L-alanine ligase
uridine-diphosphate-N-acetylmuramate:L-alanine ligase
uridine diphospho-N-acetylmuramoylalanine synthetase
ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine.
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase
UDP-N-acetylmuramoylalanine--D-glutamate ligase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase
Involved in the synthesis of a cell-wall peptide in bacteria.
ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate.
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
UDPacetylmuramoylpentapeptide synthetase
UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase
UDP-N-acetylmuramoylalanine-D-glutamyl-lysine--D-alanyl-D-alanine ligase
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase
UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine synthetase
uridine diphosphoacetylmuramoylpentapeptide synthetase
Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8 and EC 6.3.2.9 in the synthesis of a cell-wall peptide.
Also catalyzes the reaction when the C-terminal residue of the tripeptide is meso-2,6-diaminoheptanedioate (acylated at its L-center), linking the D-Ala--D-Ala to the carboxy group of the L-center.
ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine.
ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine.
This enzyme was thought to form AMP, but studies with highly purified enzyme proved that it forms ADP.
Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates.
It is also found in the skeletal muscle of some invertebrates.
The enzyme can also catalyze the formation of homocarnosine from 4-aminobutyrate and L-histidine, with much lower activity.
ATP + beta-alanine + L-histidine = ADP + carnosine + H(+) + phosphate.
4-aminobutanoate + ATP + L-histidine = ADP + H(+) + L-homocarnosine + phosphate.
ATP + beta-alanine + L-lysine = ADP + beta-alanyl-L-lysine + H(+) + phosphate.
ATP + beta-alanine + L-ornithine = ADP + beta-alanyl-L-ornithine + H(+) + phosphate.
ATP + beta-alanine + L-arginine = ADP + beta-alanyl-L-arginine + H(+) + phosphate.
In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.17, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates.
In contrast, the activities are located on separate proteins in most eukaryotes studied to date.
This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa.
7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate.
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diamino-heptanedioate ligase (ADP-forming)
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 adds lysine instead.
It is the amino group of the L-center of the diaminopimelate that is acylated.
ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate.
N-(2,3-dihydroxybenzoyl)-serine synthetase
This enzyme complex catalyzes the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin.
In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyzes the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyzes the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3-dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule).
3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6 diphosphate + enterobactin + 4 H(+).
D-alanine--alanyl-poly(glycerolphosphate) ligase
D-alanyl-alanyl-poly(glycerolphosphate) synthetase
ATP + D-alanine + alanyl-poly(glycerolphosphate) = ADP + phosphate + D-alanyl-alanyl-poly(glycerolphosphate).
folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase
formyltetrahydropteroyldiglutamate synthetase
N(10)-formyltetrahydropteroyldiglutamate synthetase
tetrahydrofolate:L-glutamate gamma-ligase (ADP-forming)
In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.12, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates (H4folate).
In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast.
Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes.
As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C1 metabolism.
The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.
(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate.
10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate.
(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate.
ATP + histamine + L-glutamate = ADP + H(+) + N(alpha)-gamma-L-glutamylhistamine + phosphate.
(indol-3-yl)acetate + ATP + L-lysine = ADP + H(+) + N(6)-[(indole-3-yl)acetyl]-L-lysine + phosphate.
ATP + beta-alanine + gamma-L-glutamyl-L-cysteine = ADP + gamma-L-glutamyl-L-cysteinyl-beta-alanine + H(+) + phosphate.
ATP + L-arginine + L-tyrosine = AMP + diphosphate + H(+) + L-tyrosyl-L-arginine.
L-Tyrosine is linked via a peptide bond to the C-terminus of de-tyrosinated alpha-tubulin (des-Tyr(omega)-alpha-tubulin).
The enzyme is highly specific for alpha-tubulin and moderately specific for ATP and L-tyrosine.
L-Phenylalanine and 3,4-dihydroxy-L-phenylalanine are transferred but with higher Km values.
ATP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-tyrosine = ADP + C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H(+) + phosphate.
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
L-alpha-aminoadipyl-cysteinyl-valine synthetase
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction.
3 ATP + H2O + L-2-aminoadipate + L-cysteine + L-valine = 3 AMP + 3 diphosphate + 3 H(+) + N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine.
cyanophycin synthase (L-aspartate-adding)
multi-L-arginyl-poly-L-aspartate synthase
Both this enzyme and EC 6.3.2.30 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store.
Both enzymes are found in the same protein but have different active sites.
Both L-Asp and L-Arg must be present before either enzyme will display significant activity.
[L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(+) + phosphate.
cyanophycin synthase (L-arginine-adding)
Both this enzyme and EC 6.3.2.29 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store.
Canavanine and lysine can be incoporated into the polymer instead of arginine.
[L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ATP + L-arginine = [L-4-(L-arginin-2-N-yl)aspartate](n+1) + ADP + H(+) + phosphate.
This protein catalyzes the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions.
In the reaction described here the enzyme attaches a glutamate via its alpha-amine group to F420-0.
In the second reaction (EC 6.3.2.34) it catalyzes the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate.
coenzyme gamma-F420-2:alpha-L-glutamate ligase
The enzyme caps the gamma-glutamyl tail of the hydride carrier coenzyme F420.
ATP + L-glutamate + oxidized coenzyme F420-2 = ADP + H(+) + oxidized coenzyme alpha-F420-3 + phosphate.
This enzyme catalyzes the biosynthesis of 5,6,7,8-tetrahydrosarcinapterin, a modified form of tetrahydromethanopterin found in the Methanosarcinales.
It does not require K(+), and does not discriminate between ATP and GTP.
5,6,7,8-tetrahydromethanopterin + ATP + L-glutamate = 5,6,7,8-tetrahydrosarcinapterin + ADP + H(+) + phosphate.
coenzyme F420-1:gamma-L-glutamate ligase
In the first reaction (EC 6.3.2.31) the enzyme attaches a glutamate via its alpha-amine group to F420-0.
In the second reaction, which is described here, the enzyme catalyzes the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate.
The product of this enzyme, D-alanyl-D-serine, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4, D-alanine--D-alanine ligase.
ATP + D-alanine + D-serine = ADP + D-alanyl-D-serine + H(+) + phosphate.
The two archaeal enzymes that catalyze this conversion are EC 2.7.1.169 and this enzyme.
(R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-phosphopantothenate + AMP + diphosphate + H(+).
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--D-lysine ligase
The D-lysine is attached to the peptide chain at the N(6) position.
The enzyme from Thermotoga maritima also performs the reaction of EC 6.3.2.7.
ATP + D-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + N(6)-(UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl)-D-lysine + phosphate.
N(2)-citryl-N(6)-acetyl-N(6)-hydroxylysine synthase
N(alpha)-citryl-N(epsilon)-acetyl-N(epsilon)-hydroxylysine synthase
The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore.
It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS).
Type A enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate.
The enzyme is believed to form an adenylate intermediate prior to ligation.
ATP + citrate + N(6)-acetyl-N(6)-hydroxy-L-lysine = AMP + diphosphate + H(+) + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine.
It belongs to a class of siderophore synthases known as type C nonribosomal peptide synthase-independent synthases (NIS).
Type C enzymes are responsible for the formation of amide or ester bonds between a variety of substrates and a prochiral carboxyl group of a citrate molecule that is already linked to a different moiety at its other prochiral carboxyl group.
ATP + N(2)-citryl-N(6)-acetyl-N(6)-hydroxy-L-lysine + N(6)-acetyl-N(6)-hydroxy-L-lysine = aerobactin + AMP + diphosphate + H(+).
Cyclopeptine synthase is the key enzyme of benzodiazepine alkaloid biosynthesis in the fungus Penicillium cyclopium.
The enzyme is a non-ribosomal peptide synthase.
anthranilate + 2 ATP + L-phenylalanine + S-adenosyl-L-methionine = 2 AMP + cyclopeptine + 2 diphosphate + 2 H(+) + S-adenosyl-L-homocysteine.
The enzyme, found in animals, produces the neurotransmitter N-acetyl-L-aspartyl-L-glutamate.
One isoform also has the activity of EC 6.3.1.17, while another isoform has the activity of EC 6.3.2.42.
ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-acetyl-L-aspartyl-L-glutamate + phosphate.
N-acetylaspartylglutamylglutamate synthase
N-acetylaspartylglutamylglutamate synthetase
The enzyme, found in mammals, also has the activity of EC 6.3.2.41.
2 ATP + 2 L-glutamate + N-acetyl-L-aspartate = 2 ADP + 2 H(+) + N-acetyl-L-aspartyl-L-glutamyl-L-glutamate + 2 phosphate.
[amino-group carrier protein]--L-2-aminoadipate ligase
The enzymes from the thermophilic bacterium Thermus thermophilus and the thermophilic archaea Sulfolobus acidocaldarius and Sulfolobus tokodaii protect the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW.
This reaction is part of the lysine biosynthesis pathway in these organisms.
[amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-2-aminoadipate = [amino-group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine + ADP + H(+) + phosphate.
pantoate--beta-alanine ligase (ADP-forming)
The enzyme, characterized from the archaeon Methanosarcina mazei, is involved in the biosynthesis of pantothenate.
It is different from EC 6.3.2.1, the AMP-forming pantoate-beta-alanine ligase found in bacteria and eukaryota.
(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + ADP + H(+) + phosphate.
UDP-N-acetylmuramate L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase
The enzyme catalyzes the reincorporation into peptidoglycan of the tripeptide L-alanyl-gamma-D-glutamyl-2,6-meso-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division.
The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine in vivo and in vitro.
ATP + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate.
fumarate--(S)-2,3-diaminopropanoate ligase
The enzyme, characterized from the bacterium Enterobacter agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an L-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold.
(S)-2,3-diaminopropanoate + ATP + fumarate = AMP + diphosphate + N(3)-fumaroyl-(S)-2,3-diaminopropanoate.
The enzyme, characterized from the bacterium Pantoea agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an (S)-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold.
3-[[[(2R,3R)-3-carboxyoxiran-2-yl]carbonyl]amino]-L-alanine + ATP + L-valine = ADP + dapdiamide E + H(+) + phosphate.
ATP + L-valine + N(3)-fumaramoyl-(S)-2,3-diaminopropanoate = ADP + dapdiamide A + H(+) + phosphate.
ATP + L-isoleucine + N(3)-fumaramoyl-(S)-2,3-diaminopropanoate = ADP + dapdiamide B + H(+) + phosphate.
ATP + L-leucine + N(3)-fumaramoyl-(S)-2,3-diaminopropanoate = ADP + dapdiamide C + H(+) + phosphate.
The enzyme shows strict substrate specificity toward L-arginine as the N-terminal amino acid of the product.
The second amino acid could be any standard protein-building amino acid except for L-proline.
an L-alpha-amino acid + ATP + L-arginine = ADP + H(+) + L-arginyl-L-alpha-amino acid + phosphate.
ATP + L-alanine + L-anticapsin = ADP + bacilysin + H(+) + phosphate.
This fungal enzyme, isolated from Magnaporthe oryzae, is an non-ribosomal peptide synthetase (NRPS)-polyketide synthase (PKS) hybrid protein that consists of condensation (C), adenylation (A) and peptidyl-carrier protein (PCP) domains in the NRPS portion and a ketosynthase (KS) domain in the PKS portion.
ATP is required for activation of isoleucine, which is then condensed with acetoacetyl-CoA.
Cyclization and release from the enzyme are catalyzed by the KS domain.
acetoacetyl-CoA + ATP + L-isoleucine = AMP + CoA + diphosphate + 2 H(+) + tenuazonic acid.
phosphopantothenate--cysteine ligase (ATP)
(R)-4'-phosphopantothenate + ATP + L-cysteine = AMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine.
Two jasmonoyl-L-amino acid synthetases have been described from Nicotiana attenuata and one from Arabidopsis thaliana.
The N.attenuata enzymes generate jasmonoyl-L-isoleucine, jasmonoyl-L-leucine, and jasmonoyl-L-valine.
The enzyme from A.thaliana could catalyze the addition of many different amino acids to jasmonate in vitro.
While the abundant form of jasmonate in plants is (-)-jasmonate, the active form of jasmonoyl-L-isoleucine is (+)-7-iso-jasmonoyl-L-isoleucine.
a jasmonate + an L-alpha-amino acid + ATP = a jasmonyl-L-amino acid + AMP + diphosphate + H(+).
UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate synthetase
The enzyme, characterized from the bacterium Xanthomonas oryzae, catalyzes the ligation of a terminal L-glutamate to UDP-N-acetyl-alpha-D-muramoyl-L-alanine.
The combined activity of this enzyme and EC 5.1.1.23 provides an alternative route for incorporating D-glutamate into peptidoglycan, replacing the more common combination of EC 5.1.1.3 and EC 6.3.2.9.
ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate synthtase
Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate.
The enzyme forms a citrate adenylate intermediate prior to ligation.
(S)-2,3-diaminopropanoate + ATP + citrate = 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate + AMP + diphosphate.
2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase
Type B NIS enzymes recognize esterified or amidated derivatives of carboxylic acids.
The enzyme likely forms a 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate adenylate intermediate prior to ligation.
(S)-2,3-diaminopropanoate + 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + ATP = 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + AMP + diphosphate.
The enzyme, characterized from the bacterium Staphylococcus aureus, catalyzes the last step in the biosynthesis of the siderophore staphyloferrin B.
It belongs to a class of siderophore synthases known as type B nonribosomal peptide synthase-independent synthases (NIS).
Type B NIS enzymes recognize the delta-acid group of 2-oxoglutarate.
The enzyme forms a 2-oxoglutarate adenylate intermediate prior to ligation.
2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate + ATP = AMP + diphosphate + H(+) + staphyloferrin B.
The enzyme, characterized from the bacterium Staphylococcus aureus, catalyzes the last step in the biosynthesis of the siderophore staphyloferrin A.
ATP + citrate + N(5)-[(S)-citryl]-D-ornithine = AMP + diphosphate + H(+) + staphyloferrin A.
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin A.
ATP + citrate + D-ornithine = AMP + diphosphate + H(+) + N(5)-[(S)-citryl]-D-ornithine.
N(6)-[(2R,3R)-3-methylornithyl]-L-lysine synthase
The enzyme participates in the biosynthesis of L-pyrrolysine, a naturally occurring, genetically coded amino acid found in some methanogenic archaea and a few bacterial species.
L-pyrrolysine is present in several methyltransferases that are involved in methyl transfer from methylated amine compounds to coenzyme M.
(3R)-3-methyl-D-ornithine + ATP + L-lysine = (3R)-3-methyl-D-ornithyl-N(6)-L-lysine + ADP + H(+) + phosphate.
glutamate--[amino group carrier protein] ligase
The enzyme, originally characterized from the archaeon Sulfolobus acidocaldarius, is involved in L-arginine biosynthesis.
The enzyme from the archaeon Thermococcus kodakarensis is bifunctional and also catalyzes the activity of EC 6.3.2.43.
[amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-glutamate = [amino-group carrier protein]-C-terminal-gamma-(L-glutamyl)-L-glutamate + ADP + H(+) + phosphate.
The enzyme from human also functions as EC 2.3.2.27.
ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine.
phosphoribosylformylglycinamidine cyclo-ligase
phosphoribosyl-aminoimidazole synthetase
2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate.
5,10-methenyltetrahydrofolate synthetase
(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + phosphate.
(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate.
(carboxyethyl)arginine beta-lactam-synthase
It has been proposed that L-N(2)-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the beta-lactam ring is then formed by the intramolecular attack of the beta-nitrogen on the activated carboxy group.
ATP + N(2)-(2-carboxyethyl)-L-arginine = AMP + deoxyamidinoproclavaminate + diphosphate + H(+).
ATP + H(+) + H2O + O-ureido-D-serine = ADP + CO2 + D-cycloserine + NH4(+) + phosphate.
(2S,5S)-5-carboxymethylproline + ATP = (3S,5S)-carbapenam-3-caboxylate + AMP + diphosphate + H(+).
Ni-sirohydrochlorin a,c-diamide reductive cyclase
3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide = 15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate.
The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place.
The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP.
Ammonia then reacts with this intermediate generating CTP and a phosphate.
The enzyme can also use ammonia from the surrounding solution.
ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate.
In eukaryotes occurs as a trifunctional enzyme also having EC 1.5.1.5 and EC 3.5.4.9 activity.
(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate.
GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate.
ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+).
The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 3.5.1.54, thus bringing about the hydrolysis of urea to CO2 and NH3.
The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates.
ATP + hydrogencarbonate + urea = ADP + H(+) + phosphate + urea-1-carboxylate.
ATP + D-ribose 5-phosphate + NH4(+) = 5-phospho-beta-D-ribosylamine + ADP + H(+) + phosphate.
imidazoleacetate--phosphoribosyldiphosphate ligase
5-phosphoribosylimidazoleacetate synthetase
5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + imidazole-4-acetate = 1-(5-phosphoribosyl)imidazole-4-acetate + ADP + diphosphate + H(+) + phosphate.
biotin--[methylmalonyl-CoA-carboxytransferase] ligase
biotin--[methylmalonyl-CoA-carboxyltransferase] ligase
biotin--[methylmalonyl-CoA-carboxyltransferase] synthetase
biotin--[methylmalonyl-CoA-carboxytransferase] synthetase
apo-[methylmalonyl-CoA:pyruvate carboxytransferase] + ATP + biotin = AMP + diphosphate + H(+) + holo-[methylmalonyl-CoA:pyruvate carboxytransferase].
biotin--[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase
biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] synthetase
propionyl-CoA holocarboxylase synthetase
apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)].
biotin--[methylcrotonoyl-CoA-carboxylase] ligase
biotin--[methylcrotonoyl-CoA-carboxylase] synthetase
apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].
ATP + L-glutamate + methylamine = ADP + H(+) + N(5)-methyl-L-glutamine + phosphate.
5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate.
This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15.
In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria).
Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2).
ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate.
biotin--[biotin carboxyl-carrier protein] ligase
acetyl-CoA carboxylase biotin holoenzyme synthetase
biotin--[acetyl-CoA carboxylase] synthetase
The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14.
The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15.
In some organisms the carrier protein is part of EC 6.4.1.2.
ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein].
carbamoyl-phosphate synthetase (ammonia)
The enzyme catalyzes the first committed step in the urea cycle.
The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate.
Two moles of ATP are utilized for the synthesis of one molecule of carbamoyl phosphate, making the reaction essentially irreversible.
The enzyme requires the allosteric activator N-acetyl-L-glutamate.
2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate.
7,8-dihydrofolate + ATP + formate = 10-formyldihydrofolate + ADP + phosphate.
5-(carboxyamino)imidazole ribonucleotide synthase
N(5)-carboxyaminoimidazole ribonucleotide synthetase
In Escherichia coli, this enzyme, along with EC 5.4.99.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates.
Carboxyphosphate is the putative acyl phosphate intermediate.
Involved in the late stages of purine biosynthesis.
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate.
isoleucine-specific transfer ribonucleate lysidine synthetase
The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNA(Ile) at the oxo group in position 2 of cytidine(34).
This modification determines both codon and amino acid specificities of tRNA(Ile).
ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2).
7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate.
nicotinic acid mononucleotide glycohydrolase
nicotinic acid mononucleotide pyrophosphorylase
nicotinic acid phosphoribosyltransferase
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP.
However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate.
The phospho-enzyme is hydrolyzed during the transferase reaction, regenerating the low affinity form.
The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100.
5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate.
tRNA(Ile)-2-agmatinylcytidine synthetase
The enzyme from the archaeon Archaeoglobus fulgidus modifies the wobble base of the CAU anticodon of the archaeal tRNA(Ile)(2) at the oxo group in position 2 of cytidine(34).
This modification is crucial for accurate decoding of the genetic code.
In bacteria EC 6.3.4.19, catalyzes the modification of [tRNA(Ile)(2)]-cytidine(34) to [tRNA(Ile)(2)]-lysidine(34).
agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H(+) + 2 phosphate.
formate--phosphoribosylaminoimidazolecarboxamide ligase
5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase
5-formaminoimidazole-4-carboxamide ribonucleotide synthetase
This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyzes a step in the synthesis of purine nucleotides.
It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP.
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + ATP + formate = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + ADP + phosphate.
The enzyme, which has been characterized from the archaea Methanocaldococcus fervens, participates in the biosynthesis of the cofactor methanofuran.
ATP + L-glutamate + tyramine = ADP + gamma-L-glutamyltyramine + H(+) + phosphate.
2-amino-2'-deoxyadenylo-succinate synthase
The enzyme, characterized from a number of bacteriophages, participates in the biosynthesis of dZTP, which replaces dATP in the genome of these phages.
ATP + dGMP + L-aspartate = (2S)-2-amino-2'-deoxyadenylo-succinate + ADP + 2 H(+) + phosphate.
Carbon--nitrogen ligases with glutamine as amido-N-donor
NAD(+) synthetase (glutamine-hydrolyzing)
nicotinamide adenine dinucleotide synthetase (glutamine)
NH3 can act instead of glutamine (cf. EC 6.3.1.5).
ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+).
Involved in the de novo biosynthesis of guanosine nucleotides.
An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain.
The enzyme can catalyze the second reaction alone in the presence of ammonia.
ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate.
phosphoribosylformylglycinamidine synthase
formylglycinamide ribotide amidotransferase
phosphoribosylformylglycinamidine synthetase
ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate.
asparagine synthase (glutamine-hydrolyzing)
asparagine synthetase (glutamine-hydrolyzing)
glutamine-dependent asparagine synthetase
The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel.
The enzyme catalyzes three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain.
The C-terminal active site mediates both the synthesis of a beta-aspartyl-AMP intermediate and its subsequent reaction with ammonia.
The ammonia released is channeled to the other active site to yield asparagine.
ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate.
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
carbamoyl phosphate synthetase (glutamine)
carbamoyl-phosphate synthetase (glutamine-hydrolyzing)
glutamine-dependent carbamoyl-phosphate synthase
glutamine-dependent carbamoyl phosphate synthetase
The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides.
The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length.
The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate.
The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate.
The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit.
The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate.
2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate.
asparaginyl-tRNA synthase (glutamine-hydrolyzing)
This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis.
In the first step, a non-discriminating ligase (EC 6.1.1.23) mischarges tRNA(Asn) with aspartate, leading to the formation of aspartyl-tRNA(Asn).
The aspartyl-tRNA(Asn) is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNA(Asn) (aspartyl-tRNA(Asp) is not a substrate for this enzyme).
A glutaminase subunit (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation.
Bacterial GatCAB complexes also has the activity of EC 6.3.5.7.
ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate.
glutaminyl-tRNA synthase (glutamine-hydrolyzing)
In systems lacking discernible glutamine--tRNA ligase (EC 6.1.1.18), glutaminyl-tRNA(Gln) is formed by a two-enzyme system.
In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln).
The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl-tRNA(Glu) is not a substrate for this enzyme).
Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6.
ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate.
hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolyzing)
This enzyme, which participates in the aerobic (late cobalt insertion) cobalamin biosynthesis pathway, generates hydrogenobyrinate a,c-diamide, the substrate required by EC 6.6.1.2 which adds cobalt to the macrocycle.
The equivalent reaction in the anaerobic cobalamin biosynthesis pathway is catalyzed by EC 6.3.5.11.
2 ATP + 2 H2O + hydrogenobyrinate + 2 L-glutamine = 2 ADP + 2 H(+) + hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2 phosphate.
adenosylcobyric acid synthase (glutamine-hydrolyzing)
5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase
Ado-cobyric acid synthase [glutamine hydrolyzing]
This enzyme catalyzes the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates.
adenosylcob(III)yrinate a,c-diamide + 4 ATP + 4 H2O + 4 L-glutamine = adenosylcob(III)yrate + 4 ADP + 4 H(+) + 4 L-glutamate + 4 phosphate.
cobyrinate a,c-diamide synthase (glutamine-hydrolyzing)
This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyzes the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source.
It is proposed that the enzyme first catalyzes the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate.
The Km for ammonia is substantially higher than that for L-glutamine.
The equivalent reaction in the aerobic cobalamin biosynthesis pathway is catalyzed by EC 6.3.5.9.
2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate.
Ni-sirohydrochlorin a,c-diamide synthase
2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate.
lipid II isoglutaminyl synthase (glutamine-hydrolyzing)
The enzyme complex, found in Gram-positive bacteria, consists of two subunits.
A glutaminase subunit (cf. EC 3.5.1.2) produces an ammonia molecule that is channeled to a ligase subunit, which adds it to the activated D-glutamate residue of lipid II, converting it to an isoglutamine residue.
ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosphate.
ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate.
This enzyme is a multi-domain polypeptide that catalyzes three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyzes the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA.
In some organisms these activities are catalyzed by separate enzymes (see EC 6.3.4.14 and EC 2.1.3.15).
The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate.
Also carboxylates butanoyl-CoA and catalyzes transcarboxylation.
ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate.
3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate.
Also carboxylates dimethylpropenoyl-CoA and farnesoyl-CoA.
ATP + geranoyl-CoA + hydrogencarbonate = 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + ADP + H(+) + phosphate.
The enzyme from Xanthobacter sp. strain Py2 also carboxylates butan-2-one to 3-oxopentanoate.
2 ATP + butan-2-one + 3 H2O + hydrogencarbonate = 3-oxopentanoate + 2 AMP + 4 H(+) + 4 phosphate.
acetone + 2 ATP + 3 H2O + hydrogencarbonate = acetoacetate + 2 AMP + 4 H(+) + 4 phosphate.
It was originally thought that this enzyme was a promoting factor for the carboxylation of 2-oxoglutarate by EC 1.1.1.41, but this has since been disproved.
The product of the reaction is unstable and is quickly converted into isocitrate by the action of EC 1.1.1.41.
2-oxoglutarate + ATP + hydrogencarbonate = (S)-oxalosuccinate + ADP + H(+) + phosphate.
The enzyme is involved in anaerobic degradation of ethylbenzene.
No activity with acetone, butanone, 4-hydroxy-acetophenone or 4-amino-acetophenone.
acetophenone + 2 ATP + H2O + hydrogencarbonate = 3-oxo-3-phenylpropanoate + 2 ADP + 2 H(+) + 2 phosphate.
The enzyme, studied from the methanogenic archaeon Methanosarcina acetivorans, catalyzes the last step in the biosynthesis of the nickel-containing tetrapyrrole cofactor coenzyme F430, which is required by EC 2.8.4.1.
15,17(3)-seco-F430-17(3)-acid + ATP = ADP + coenzyme F430 + phosphate.
The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue.
The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[DNA].
Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
RNA can also act as substrate, to some extent.
ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
polydeoxyribonucleotide synthase (NAD(+))
The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue.
NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
The enzyme catalyzes the ligation of RNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in RNA.
The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[RNA].
ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.
The enzyme converts the 3'-terminal phosphate of various RNA substrates into the 2',3'-cyclic phosphodiester in an ATP-dependent reaction.
Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a histidine residue.
The adenylate group is then transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [RNA]-3'-(5'-diphosphoadenosine).
Finally, the enzyme catalyzes an attack of the vicinal O-2' on the 3'-phosphorus, which results in formation of cyclic phosphate and release of the adenylate.
The enzyme also has a polynucleotide 5' adenylation activity.
a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate.
The enzyme, which is specific for GTP, was characterized from the archaeon Pyrococcus furiosus.
The enzyme converts the 3'-terminal phosphate of various RNA substrates into the 2',3'-cyclic phosphodiester in a GTP-dependent reaction.
Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by GTP, forming a phosphoramide bond between guanylate and a histidine residue.
The guanylate group is then transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [RNA]-3'-(5'-diphosphoguanosine).
Finally, the enzyme catalyzes an attack of the vicinal O-2' on the 3'-phosphorus, which results in formation of cyclic phosphate and release of the guanylate.
a 3'-end 3'-phospho-ribonucleotide-RNA + GTP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + diphosphate + GMP.
The enzymes from the archaea Thermococcus fumicolans and Thermococcus onnurineus show high activity with either ATP or NAD(+), and significantly lower activity with TTP, GTP, and CTP.
Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP or NAD(+), forming a phosphoramide bond between adenylate and a lysine residue.
The enzymes from the archaea Hyperthermus butylicus and Sulfophobococcus zilligii are active with ATP, ADP or GTP.
Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, ADP, or GTP, forming a phosphoramide bond between adenylate/guanylate and a lysine residue.
The nucleotide is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine/guanosine)-[DNA].
Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the nucleotide.
Different from EC 6.5.1.1 and EC 6.5.1.6, which cannot utilize GTP.
ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.
GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP + diphosphate.
3'-phosphate/5'-hydroxy nucleic acid ligase
The enzyme is a 3'-5' nucleic acid ligase with the ability to join RNA with 3'-phosphate or 2',3'-cyclic-phosphate ends to RNA with 5'-hydroxy ends.
It can also join DNA with 3'-phosphate ends to DNA with 5'-hydroxy ends, provided the DNA termini are unpaired.
The enzyme is found in members of all three kingdoms of life, and is essential in metazoa for the splicing of intron-containing tRNAs.
The reaction follows a three-step mechanism with initial activation of the enzyme by GTP hydrolysis, forming a phosphoramide bond between the guanylate and a histidine residue.
The guanylate group is transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [DNA/RNA]-3'-(5'-diphosphoguanosine).
When a suitable 5'-OH end is available, the enzyme catalyzes an attack of the 5'-OH on the capped end to form a 3'-5' phosphodiester splice junction, releasing the guanylate.
When acting on an RNA 2',3'-cyclic-phosphate, the enzyme catalyzes an additional reaction, hydrolyzing the cyclic phosphate to a 3'-phosphate.
The metazoan enzyme requires activating cofactors in order to achieve multiple turnover catalysis.
a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP.
a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+).
The enzyme is present in a number of methanogenic archaeal genera that accumulate cyclic 2,3-bisphosphoglycerate as a thermoprotectant.
(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate.
This is the first committed step of chlorophyll biosynthesis and is a branchpoint of two major routes in the tetrapyrrole pathway.
ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate.
hydrogenobyrinic acid a,c-diamide cobaltochelatase
This enzyme, which forms part of the aerobic (late cobalt insertion) cobalamin biosynthesis pathway, is a type I chelatase, being heterotrimeric and ATP-dependent.
It comprises two components, one of which corresponds to CobN and the other is composed of two polypeptides, specified by cobS and cobT in Pseudomonas denitrificans, and named CobST.
Hydrogenobyrinate is a very poor substrate.
ATP can be replaced by dATP or CTP but the reaction proceeds more slowly.
CobN exhibits a high affinity for hydrogenobyrinate a,c-diamide.
The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding.
See EC 4.99.1.3 for the cobaltochelatase that participates in the anaerobic cobalamin biosynthesis pathway.
ATP + Co(2+) + H2O + hydrogenobyrinate a,c-diamide = ADP + cob(II)yrinate a,c diamide + 5 H(+) + phosphate.
Hydron translocation or charge separation linked to oxidoreductase reactions
proton-translocating NAD(P)(+) transhydrogenase
The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane.
In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH.
Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+).
NADH:ubiquinone reductase (H(+)-translocating)
complex I (mitochondrial electron transport)
dihydronicotinamide adenine dinucleotide-coenzyme Q reductase
mitochondrial electron transport complex 1
mitochondrial electron transport complex I
reduced nicotinamide adenine dinucleotide-coenzyme Q reductase
The enzyme is a very large complex that participates in electron transfer chains of mitochondria and aerobic bacteria.
The mitochondrial enzyme transfers electrons from NADH to the ubiquinone pool.
The cyanobacterial enzyme prefers NADPH, reduces plastoquinone, and also participates in reversed electron transport that results in the reduction of NAD(P)(+) to NAD(P)H.
a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+).
This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane.
The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo3 oxidase it is 2, while for the bd-II oxidase it is 1.
2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) + 2 H2O.
caldariellaquinol oxidase (H(+)-transporting)
The enzyme from thermophilic archaea is part of the terminal oxidase and catalyzes the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane.
2 caldariellaquinol + n H(+)(in) + O2 = 2 caldariellaquinone + n H(+)(out) + 2 H2O.
Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homolog of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.
The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.
2 a menaquinol + O2 = 2 a menaquinone + 2 H2O.
Contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster.
The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12).
Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly.
In chloroplasts, protons are translocated through the thylakoid membrane from the lumen to the stroma.
The mechanism occurs through the Q cycle as in EC 7.1.1.8 (complex III) and involves electron bifurcation.
a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin].
ubiquinol oxidase (electrogenic, proton-motive force generating)
This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water.
The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1.
The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism.
2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in).
complex III (mitochondrial electron transport)
The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain.
It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria.
The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin.
Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3).
a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out).
complex IV (mitochondrial electron transport)
An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms.
The reduction of O2 to water is accompanied by the extrusion of four protons.
The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist.
All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal center composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB).
Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome.
While most bacterial enzymes consist of only 3-4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits.
4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O.
ferredoxin--quinone oxidoreductase (H(+)-translocating)
The enzyme, present in plants and cyanobacteria, couples electron transport from ferredoxin to plastoquinone and proton pumping from the cytoplasm to the thylakoid lumen.
It participates in cyclic electron flow, retuning electrons generated by photosystem I to the plastoquinone pool, thus bypassing the generation of reducing power.
It may also participate in respiration using electrons originating from NADPH via the action of EC 1.18.1.2 operating in the direction of ferredoxin reduction.
It is a large complex, with some of its subunits resembling those from the bacterial/mitochondrial EC 7.1.1.2.
However, it lacks the NADH-oxidizing module and instead has a module that interacts with ferredoxin.
Several forms of the enzyme exist, differing in their exact combination of subunits used.
Some of the forms participate in carbon dioxide hydration rather than electron transfer.
a plastoquinone + 6 H(+)(in) + 2 reduced [2Fe-2S]-[ferredoxin] = a plastoquinol + 4 H(+)(out) + 2 oxidized [2Fe-2S]-[ferredoxin].
ferredoxin--NAD(+) oxidoreductase (H(+)-transporting)
This iron-sulfur and flavin-containing electron transport complex, isolated from some anaerobic bacteria, couples the energy from reduction of NAD(+) by ferredoxin to pumping protons out of the cell, generating a proton motive force across the cytoplasmic membrane.
Most similar complexes pump sodium ions rather than protons (cf. EC 7.2.1.2).
3 H(+)(in) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = 2 H(+)(out) + NADH + 2 oxidized [2Fe-2S]-[ferredoxin].
Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate.
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1).
The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
This movement is driven by the H(+) electrochemical potential gradient.
The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate.
Hydron translocation linked to the hydrolysis of diphosphate
This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole.
The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
diphosphate + H(+)(in) + H2O = 2 H(+)(out) + 2 phosphate.
Na(+)-translocating membrane pyrophosphatase
This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane.
The enzyme is electrogenic, as the Na(+) transport results in generation of a positive potential in the inner side of the membrane.
diphosphate + H2O + Na(+)(in) = H(+) + Na(+)(out) + 2 phosphate.
Catalysing the translocation of inorganic cations
NADH:ubiquinone reductase (Na(+)-transporting)
Na(+)-translocating NADH-quinone reductase
An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one non-covalently bound FAD, one riboflavin, and one [2Fe-2S] cluster.
a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+).
ferredoxin--NAD(+) oxidoreductase (Na(+)-transporting)
This electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD(+) by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.
H(+) + Na(+)(in) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = Na(+)(out) + NADH + 2 oxidized [2Fe-2S]-[ferredoxin].
ascorbate ferrireductase (transmembrane)
A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole.
Acts on hexacyanoferrate(III) and other ferric chelates.
Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) + monodehydro-L-ascorbate radical(in).
Linked to the hydrolysis of a nucleoside triphosphate
A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis.
The enzyme is similar to EC 7.1.2.2 but pumps Na(+) rather than H(+).
ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) + phosphate.
A Saccharomyces cerevisiae enzyme that exports some heavy metals, especially Cd(2+), from the cytosol into the vacuole.
ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate.
This enzyme from yeast is involved in the efflux of Na(+), with one ion being exported per ATP hydrolyzed.
ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate.
ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins.
This bacterial enzyme, characterized from Bacillus subtilis, exports Na(+) ions out of the cell.
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of Mn(2+), Zn(2+) and iron chelates.
ATP + H2O + Mn(2+)(out) = ADP + H(+) + Mn(2+)(in) + phosphate.
A bacterial enzyme that is involved in K(+) import.
The probable stoichiometry is one ion per ATP hydrolyzed.
ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate.
A bacterial enzyme that interacts with a periplasmic iron-binding protein to imports Fe(3+) ions into the cytoplasm.
ATP + Fe(3+)(out) + H2O = ADP + Fe(3+)(in) + H(+) + phosphate.
This enzyme transports Cu(+) or Ag(+), and cannot transport the divalent ions, contrary to EC 7.2.2.9, which mainly transports the divalent copper ion.
ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate.
The enzyme from the termophilic bacterium Archaeoglobus fulgidus is involved in copper extrusion from the cell.
ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate.
This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria.
The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolyzed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolyzed.
In muscle cells Ca(2+) is transported from the cytosol into the sarcoplasmic reticulum.
ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate.
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of Ni(2+); the identity of the nickel species transported has not been conclusively established.
Does not undergo phosphorylation during the transport process.
ATP + H2O + Ni(2+)(out) = ADP + H(+) + Ni(2+)(in) + phosphate.
The enzyme, present in prokaryotes and photosynthetic eukaryotes, exports Zn(2+) and the related cations Cd(2+) and Pb(2+).
ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out).
P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
An enzyme from the plasma membrane of animal cells that catalyzes the efflux of three Na(+) and influx of two K(+) per ATP hydrolyzed.
It is involved in generating the plasma membrane electrical potential.
ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate.
A bacterial enzyme that imports Mg(2+) with, rather than against, the Mg(2+) electrochemical gradient.
The enzyme is also involved in Ni(2+) import.
ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate.
A P-type ATPase that exports Ag(+) ions from some bacteria, archaea as well as from some animal tissues.
The proteins also transport Cu(+) ions (cf. EC 7.2.2.8).
Ag(+)(in) + ATP + H2O = ADP + Ag(+)(out) + H(+) + phosphate.
iron(III) hydroxamate transporting ATPase
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of Fe(3+)-complexed hydroxamate siderophores such as coprogen, ferrichrome and the ferric hydroxamate antibiotic, albomycin.
ATP + H2O + Fe(3+)-hydroxamate complex-[hydroxamate-binding protein]Side 1 = ADP + phosphate + Fe(3+)-hydroxamate complexSide 2 + [hydroxamate-binding protein]Side 1.
ABC-type ferric enterobactin transporter
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of Fe(3+)-enterobactin complexes.
ATP + Fe(III)-enterobactin(out) + H2O = ADP + Fe(III)-enterobactin(in) + H(+) + phosphate.
The enzyme from Escherichia coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of Fe(3+)-citrate in the form of a mononuclear (containing one iron(III) ion and two citrate molecules) or dinuclear (containing 2 iron(III) ions) complexes.
ATP + H2O + iron(III) dicitrate(out) = ADP + H(+) + iron(III) dicitrate(in) + phosphate.
A gastric mucosal enzyme that catalyzes the efflux of one H(+) and the influx of one K(+) per ATP hydrolyzed.
ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of Zn(2+).
ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in).
This enzyme occurs in protozoa, fungi and plants.
The enzyme, detected in mycobacteria, is a high affinity slow turnover ATPase exporting Mn(2+).
ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate.
The integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89.
The free energy of the decarboxylation reaction is used to pump Na(+) out of the cell.
The enzyme is a member of the Na(+)-translocating decarboxylase family, other members of which include EC 7.2.4.2 and EC 7.2.4.3.
H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + n Na(+)(in) = CO2 + N(6)-biotinyl-L-lysyl-[protein] + n Na(+)(out).
oxaloacetate decarboxylase (Na(+) extruding)
The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA.
The process is accompanied by the extrusion of two sodium ions from cells.
Differs from EC 4.1.1.112 (oxaloacetate decarboxylase) for which there is no evidence for involvement in Na(+) transport.
H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate.
(S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
(S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase
This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na(+) across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis.
It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
(S)-methylmalonyl-CoA + H(+)(out) + Na(+)(in) = CO2 + Na(+)(out) + propanoyl-CoA.
malonate carboxy-lyase (biotin-dependent)
The enzyme described here is a membrane-bound biotin-dependent, Na(+)-translocating enzyme.
The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88).
Both enzymes achieve this by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-bound form of the enzyme.
The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side-chain as 2-(5-triphosphoribosyl)-3-dephospho-CoA rather than as phosphopantetheine 4'-phosphate.
In the anaerobic bacterium Malonomonas rubra, the components of the multienzyme complex/enzymes involved in carrying out the reactions of this enzyme are as follows: MadA (EC 2.3.1.187), MadB (EC 7.2.4.1), MadC/MadD (EC 2.1.3.10) and MadH (EC 6.2.1.35).
Two other components that are involved are MadE, the acyl-carrier protein and MadF, the biotin protein.
H(+) + malonate + Na(+)(in) = acetate + CO2 + Na(+)(out).
The enzyme from the bacterium Acidaminococcus fermentans is a biotinyl-protein, requires Na(+), and acts as a sodium pump.
Prior to the Na(+)-dependent decarboxylation, the carboxylate is transferred to biotin in a Na(+)-independent manner.
The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.
(2E)-glutaconyl-CoA + H(+) + Na(+)(in) = (2E)-butenoyl-CoA + CO2 + Na(+)(out).
Catalysing the translocation of inorganic anions and their chelates
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of phosphate anions.
Unlike P-type ATPases, it does not undergo phosphorylation during the transport process.
ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in).
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of phosphonate and organophosphate anions.
ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in).
The enzyme from Escherichia coli can interact with either of two periplasmic binding proteins and mediates the high affinity uptake of sulfate and thiosulfate.
May also be involved in the uptake of selenite, selenate and possibly molybdate.
Does not undergo phosphorylation during the transport.
ATP + H2O + sulfate(out) = ADP + H(+) + phosphate + sulfate(in).
ATP + H2O + thiosulfate(out) = ADP + H(+) + phosphate + thiosulfate(in).
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of nitrate, nitrite, and cyanate.
ATP + H2O + nitrate(out) = ADP + H(+) + nitrate(in) + phosphate.
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate.
ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate.
The enzyme, characterized from the archaeon Pyrococcus furiosus, the Gram-positive bacterium Eubacterium acidaminophilum and the Gram-negative bacterium Campylobacter jejuni, interacts with an extracytoplasmic substrate binding protein and mediates the import of tungstate into the cell for incorporation into tungsten-dependent enzymes.
ATP + H2O + tungstate(in) = ADP + H(+) + phosphate + tungstate(out).
This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family.
The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site.
It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) + phosphate.
Catalysing the translocation amino acids and peptides
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of polar amino acids.
This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
a polar amino acid(out) + ATP + H2O = a polar amino acid(in) + ADP + H(+) + phosphate.
ATP + H2O + L-arginine(out) = ADP + H(+) + L-arginine(in) + phosphate.
ATP + H2O + L-ornithine(out) = ADP + H(+) + L-ornithine(in) + phosphate.
ATP + H2O + L-lysine(out) = ADP + H(+) + L-lysine(in) + phosphate.
ABC-type nonpolar-amino-acid transporter
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein.
This entry comprises enzymes that import Leu, Ile and Val.
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein]Side 1 = ADP + phosphate + nonpolar amino acidSide 2 + [nonpolar amino acid-binding protein]Side 1.
mitochondrial protein-transporting ATPase
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex.
TIM is the protein transport machinery of the mitochondrial inner membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.
ATP + H2O + mitochondrial-proteinSide 1 = ADP + phosphate + mitochondrial-proteinSide 2.
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport.
Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).
ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate + chloroplast-proteinSide 2.
This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families.
Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
ATP + H2O + proteinSide 1 = ADP + phosphate + proteinSide 2.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of oligopeptides of varying nature.
The binding protein determines the specificity of the system.
a [oligopeptide](in) + ATP + H2O = a [oligopeptide](out) + ADP + H(+) + phosphate.
ABC-type alpha-factor-pheromone transporter
alpha-factor-pheromone transporting ATPase
A yeast enzyme that exports the alpha-factor sex pheromone.
an [alpha-factor](in) + ATP + H2O = ADP + an [alpha-factor](out) + H(+) + phosphate.
There are several families of enzymes included here, e.g. ATP-hydrolyzing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV).
Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.
ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of di- and tripeptides.
The enzyme from Pseudomonas aeruginosa can interact with five different substrate binding proteins.
a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate.
A prokaryotic ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins.
The enzyme from the bacterium Escherichia coli is a heterotrimeric complex that interacts with an extracytoplasmic substrate binding protein to mediate the uptake of glutathione.
ATP + glutathione(out) + H2O = ADP + glutathione(in) + H(+) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and functions to import methionine.
The enzyme from Escherichia coli K-12 mediates the high affinity transport of both L- and D-methionine, as well as methionine-S-oxide and N-acetyl-DL-methionine.
ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate.
ATP + D-methionine(out) + H2O = ADP + D-methionine(in) + H(+) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity import of trace cystine.
The enzyme from Escherichia coli K-12 can import both isomers of cystine and a variety of related molecules including djenkolate, lanthionine, diaminopimelate and homocystine.
ATP + H2O + L-cystine(out) = ADP + H(+) + L-cystine(in) + phosphate.
ATP + D-cystine(out) + H2O = ADP + D-cystine(in) + H(+) + phosphate.
The enzyme, found in Clostridioides, interacts with an extracytoplasmic substrate binding lipoprotein and mediates the import of L-tyrosine.
L-phenylalanine is also tranported however with lower efficiency.
ATP + H2O + L-tyrosine(out) = ADP + H(+) + L-tyrosine(in) + phosphate.
This entry describes vertebrate transporters involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with major histocompatibility complex (MHC) class I molecules.
The substrates are generated mainly from degradation of cytosolic proteins by the proteasome.
a peptide antigen(in) + ATP + H2O = a peptide antigen(out) + ADP + H(+) + phosphate.
Catalysing the translocation carbohydrates and their derivatives
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides.
ATP + D-maltose(out) + H2O = ADP + D-maltose(in) + H(+) + phosphate.
The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of lactose, melibiose and raffinose.
ATP + H2O + oligosaccharide-[oligosaccharide-binding protein]Side 1 = ADP + phosphate + oligosaccharideSide 2 + [oligosaccharide-binding protein]Side 1.
An enzyme found in Gram-negative bacteria that exports beta-glucans.
[(1->2)-beta-D-glucosyl](n)(in) + ATP + H2O = [(1->2)-beta-D-glucosyl](n)(out) + ADP + H(+) + phosphate.
An enzyme found in Gram-positive bacteria that exports teichoic acid.
ATP + H2O + teichoic acidSide 1 = ADP + phosphate + teichoic acidSide 2.
The enzyme, characterized from the bacterium Escherichia coli, functions as part of the lipopolysaccharide (LPS) export system, a seven protein system that translocates LPS from the inner- to the outer membrane.
The ATPase activity in this system is implicated in releasing LPS from the inner membrane.
ATP + H2O + lipopolysaccharideSide 1 = ADP + phosphate + lipopolysaccharideSide 2.
ABC-type lipid A-core oligosaccharide transporter
The enzyme, best characterized from the bacterium Escherichia coli, is located in the inner membrane and mediates the movement of lipid A attached to the core oligosaccharide from the cytoplasm to the periplasmic side of the inner membrane, an important step in the lipopolysaccharide biosynthetic pathway.
Not to be confused with EC 7.5.2.5, which is implicated in the translocation of LPS from the inner membrane to the outer membrane and acts later in the process.
ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-ribose.
ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) + phosphate.
The enzyme from the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-allose, which can be used by the bacterium as a sole carbon source.
ATP + D-allose(out) + H2O = ADP + D-allose(in) + H(+) + phosphate.
The enzyme from Escherichai coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of D-galactofuranose.
The periplasmic binding protein exhibits selective binding of D-galactofuranose over D-galactopyranose.
ATP + D-galactofuranose(out) + H2O = ADP + D-galactofuranose(in) + H(+) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-xylose.
ATP + D-xylose(out) + H2O = ADP + D-xylose(in) + H(+) + phosphate.
A bacterial enzyme, best characterized from Escherichia coli where it interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of D-galactose and methyl-beta-D-galactoside.
ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity uptake of L-arabinose.
ATP + H2O + L-arabinose(out) = ADP + H(+) + L-arabinose(in) + phosphate.
ABC-type D-xylose/L-arabinose transporter
ATP-binding cassette (ABC) type transporter with a 10-transmembrane-spanning (TMD) subunit and a single nucleotide binding domain.
The enzyme from the archaeon Sulfolobus acidocaldarius interacts with an extracytoplasmic sugar-binding protein and mediates the uptake of of D-xylose and L-arabinose (cf. EC 7.5.2.10 and EC 7.5.2.12).
Catalysing the translocation of other compounds
Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
ATP phosphohydrolase (steroid-exporting)
The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally.
Several distinct enzymes may be present in a single eukaryotic cell.
Many of them also transport glutathione--drug conjugates (see EC 7.6.2.3) while others also show some 'flippase' activity (cf. EC 7.6.2.1).
ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+) + phosphate.
ABC-type glutathione-S-conjugate transporter
glutathione-S-conjugate-translocating ATPase
multidrug resistance-associated protein 1
A eukaryotic ATP-binding cassette (ABC) type transporter that mediates the transport of glutathione-S-conjugates.
The mammalian enzyme, which also transports some glucuronides, exports the substrates out of the cell, while plant and fungal transporters export them into the vacuole.
Over-expression confers resistance to anticancer drugs by their efficient exportation in glutathione-S-conjugate form.
an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate.
An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes.
In humans, it is associated with Zellweger's syndrome.
an acyl-CoA(out) + ATP + H2O = ADP + an acyl-CoA(in) + H(+) + phosphate.
The enzyme has been described from Gram-negative bacteria and green plants.
ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate.
An ATP-binding cassette (ABC) type transporter found in insects that transports guanine and other purines into pigment granules in the eye, where they are converted to pteridine pigments.
The transporter is a hererodimer composed of two different peptides, each containing one membrane-spanning and one cytoplasmic ATP-binding domain.
In Drosophila, this transporter is encoded by the white and brown genes.
ATP + guanine(out) + H2O = ADP + guanine(in) + H(+) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of taurine.
In Escherichia coli the enzyme imports a range of sulfonates (including taurine) that can be used as a source of sulfur.
ATP + H2O + taurine(out) = ADP + H(+) + phosphate + taurine(in).
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of cobalamin derivatives.
an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of quaternary amine derivatives.
ATP + H2O + quaternary ammonium(out) = ADP + H(+) + phosphate + quaternary ammonium(in).
ABC-type glycerol 3-phosphate transporter
glycerol-3-phosphate-transporting ATPase
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.
ATP + H2O + sn-glycerol 3-phosphate(out) = ADP + H(+) + phosphate + sn-glycerol 3-phosphate(in).
A bacterial enzyme that imports putrescine and spermidine.
In Escherichia coli the enzyme imports spermidine preferentially.
ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
ATP + H2O + spermidine(out) = ADP + H(+) + phosphate + spermidine(in).
ABC-type capsular-polysaccharide transporter
capsular-polysaccharide-transporting ATPase
An enzyme that exports capsular polysaccharide in Gram-negative bacteria.
ATP + H2O + capsular polysaccharide-[capsular polysaccharide-binding protein]Side 1 = ADP + phosphate + capsular polysaccharideSide 2 + [capsular polysaccharide-binding protein]Side 1.
A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of the signaling molecule (2R,4S)-2-methyl-2,3,3,4-tetrahydoxytetrahydrofuran (also known as autoinducer-2).
ATP + H2O + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran-[AI-2-binding protein]Side 1 = ADP + phosphate + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuranSide 2 + [AI-2-binding protein]Side 1.
ABC-type aliphatic sulfonate transporter
The enzyme from the bacterium Escherichia coli K-12 interacts with an extracytoplasmic substrate binding protein and imports a broad range of aliphatic sulfonates for use as a source of sulfur.
ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
The enzyme, characterized from the bacterium Salmonella typhimurium, is a heterodimeric complex that interacts with an extracytoplasmic substrate binding protein and functions to import thiamine, thiamine monophosphate and thiamine diphosphate.
ATP + H2O + thiamine(out) = ADP + H(+) + phosphate + thiamine(in).
The enzyme from the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of putrescine.
Differs in specificity from EC 7.6.2.11, ABC-type polyamine transporter.
ATP + H2O + putrescine(out) = ADP + H(+) + phosphate + putrescine(in).