1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED
Tryptophan synthase beta subunit-like PLP-dependent enzymes
1-aminocyclopropane-1-carboxylate deaminase
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source.
Introduced by genetic manipulation and expressed in improved ripening tomato by Monsanto. ACC is the immediate precursor of the phytohormone ethylene which is involved in the control of ripening. ACC deaminase reduces ethylene biosynthesis and thus extends the shelf life of fruits and vegetables.
Belongs to the ACC deaminase/D-cysteine desulfhydrase family.
2-Ammoniobut-3-Enoate, 2-Amino-3-Butenoate
The nucleotide sequence upstream and downstream of 4-CBA-CoA ORFs in 9.5 kb Pseudomonas sp. strain CBS 3 chromosomal DNA.
MUTAGENESIS OF ASP-17; ARG-88; ARG-89; LYS-90; ARG-126 AND ARG-128
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH INHIBITOR AND MUTANT ASN-17 IN COMPLEX WITH SUBSTRATE
Thioesterase/thiol ester dehydrase-isomerase
Hydrolyzes 4-hydroxybenzoate-CoA, and to a lesser extent benzoyl-CoA and 4-chlorobenzoate-CoA. Not active against aliphatic acyl-CoA thioesters, including palmitoyl-CoA, hexanoyl-CoA and acetyl-CoA.
Unaffected by EDTA, Mg(2+), Mn(2+), Fe(2+), Ca(2+), Co(2+) and Zn(2+).
Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
Reduces catalytic activity. Little effect on substrate binding.
Drastically reduces catalytic activity. No effect on substrate binding.
No significant effect on catalytic activity or substrate binding.
Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.
Belongs to the 4-oxalocrotonate tautomerase family.
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPG AND NAD
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Acetaldehyde dehydrogenase [acetylating]
Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP(+) can replace NAD(+) but the rate of reaction is much slower.
Is not activated by Mn(2+), Mg(2+), Ca(2+), Zn(2+) or Co(2+).
Activity increases gradually over the pH range 6.5-8.5.
Heterotetramer composed of two DmpG (aldolase) and two DmpF (dehydrogenase) subunits, which allows a direct channeling of acetaldehyde between the two active sites.
Belongs to the acetaldehyde dehydrogenase family.
Single-stranded right-handed beta-helix, Pectin lyase-like
Belongs to the polysaccharide lyase 6 family.
Glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthases.
3-phosphoshikimate 1-carboxyvinyltransferase
5-enolpyruvylshikimate-3-phosphate synthase
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-337 IN COMPLEXES WITH 6-DIAZO-5-OXO-L-NORLEUCINE AND 5-DIAZO-4-OXO-L-NORVALINE
MUTAGENESIS OF PHE-84; ASN-328 AND SER-331
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON
Composite domain of metallo-dependent hydrolases
Hydrolytically dechlorinates atrazine to hydroxyatrazine. Dechlorinates also simazine, and desethylatrazine but is not active with terbutylazine or desethyldesisopropylatrazine (PubMed:8759853). Has no deaminase activity with melamine (PubMed:8759853, PubMed:22768133).
Binds 1 Fe(2+) ion per subunit (PubMed:12450410, PubMed:25760618). In vitro can also use Co(2+) or Mn(2+) (PubMed:12450410).
Atrazine dechlorination rates are reduced by aminoatrazine but dechlorination is not inhibited by either melanine or CAAT (2-chloro-4,6-diamino-s-triazine).
kcat is 11 sec(-1) with atrazine as substrate.
AtzA and melamine deaminase (TriA) from Acidovorax citrulli strain NRRL B-12227 are 98% identical but catalyze distinct biochemical reactions. Enzymes differ by only 9 amino acids. These 9 amino acid differences between TriA and AtzA represent a short evolutionary pathway connecting enzymes catalyzing physiologically relevant deamination and dehalogenation reactions, respectively (PubMed:11274097). Potential evolutionary trajectories between AtzA and TriA have been constructed, and catalytic activities of the intermediates along those trajectories have been characterized (PubMed:22768133).
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Major determinant of atrazine specificity
6.1-fold decrease in catalytic efficiency with atrazine. Does not confer melamine deaminase activity. 28.5-fold decrease in catalytic efficiency with atrazine and strong increase in melanine deaminase activity; when associated with D-328 and C-331.
24.3-fold decrease in catalytic efficiency with atrazine. Does not confer melamine deaminase activity. 28.5-fold decrease in catalytic efficiency with atrazine and strong increase in melanine deaminase activity; when associated with L-84 and C-331.
4.6-fold decrease in catalytic efficiency with atrazine. Confers weak melamine deaminase activity. 28.5-fold decrease in catalytic efficiency with atrazine and strong increase in melanine deaminase activity; when associated with L-84 and D-328.
AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN
Hydroxydechloroatrazine ethylaminohydrolase
Catalyzes the deamination reaction of hydroxyatrazine to N-isopropylammelide (dihydroxy-isopropyl-atrazine). The enzyme is also capable of catalyzing some dechlorinating reactions.
40 uM for 6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine
29 uM for 2,4-diisopropylamino-6-hydroxy-1,3,5-triazine
120 uM for 2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
230 uM for 2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine
Crystal structure of N-isopropylammelide isopropylaminohydrolase AtzC from Pseudomonas sp. strain ADP complexed with Zn.
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH ZINC
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH ZINC AND INHIBITOR OF WILD-TYPE AND MUTANTS ALA-219; ALA-249 AND ASP-304
MUTAGENESIS OF LYS-65; GLN-160; ASP-188; HIS-219; HIS-249; ASP-303; ASN-304 AND TRP-309
N-isopropylammelide isopropyl amidohydrolase
Transforms N-isopropylammelide to cyanuric acid and isopropylamine.
Inhibited by N-ethylammeline, N-hydroxyethylammeline, N-isopropylammeline, ammeline and 2-amino-4hydroxy-1,3,5-s-triazine.
kcat is 178 sec(-1) for N-methylammelide. kcat is 209 sec(-1) for N-ethylammelide. kcat is 80.6 sec(-1) for N-hydroxyethylammelide. kcat is 13.3 sec(-1) for N-isopropylammelide. kcat is 98.2 sec(-1) for N-cyclopropylammelide. kcat is 0.07 sec(-1) for N-t-butylammelide. kcat is 10.7 sec(-1) for N-dimethylammelide. kcat is 1.65 sec(-1) for ammelide.
Belongs to the metallo-dependent hydrolases superfamily. N-acyl-D-amino-acid deacylase family.
30-fold increase in kcat with ammelide as substrate.
12-fold increase in kcat with ammelide as substrate.
5-fold increase in kcat with ammelide as substrate.
7-fold increase in kcat with ammelide as substrate.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATZG
Hydrolyzes 1-carboxybiuret to urea-1,3-dicarboxylate and NH(3).
kcat is 15.5 sec(-1) with 1-carboxybiuret as substrate. kcat is 9.4 sec(-1) with 1-nitrobiuret as substrate. kcat is 7 sec(-1) with 1-carboxymalonamide as substrate. kcat is 19 sec(-1) with succinamate as substrate.
Heterotetramer consisting of 2 AtzE and 2 AtzG subunits.
Was originally thought to use biuret as substrate (PubMed:11544232). But new evidence has shown that 1-carboxybiuret is the real substrate. The error occurred since 1-carboxybiuret hydrolyzes spontaneously to biuret (PubMed:29523689).
MUTAGENESIS OF LYS-91; SER-165 AND SER-189
Hydrolyzes allophanate to NH(3) and CO(2). Can also use malonamate, but with much lower efficiency.
Inhibited, in a time-dependent manner, by phenyl phosphorodiamidate, which forms a covalently modified Ser-189.
kcat is 16.4 sec(-1) for allophanate. kcat is 0.1 sec(-1) for malonamate.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATZE
Important for the activity of the AtzE subunit of 1-carboxybiuret hydrolase.
TRIMETHYLLYSINE DIOXYGENASE, MITOCHONDRIAL
Gamma-butyrobetaine,2-oxoglutarate dioxygenase
Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
3-PHENYLPROPIONATE/CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA
Heterohexamer consisting of 3 BphA1 subunits and 3 BphA2 subunits. A ferredoxin (BphA3) and a ferredoxin reductase (BphA4) must be present to obtain activity (By similarity).
Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.
3-PHENYLPROPIONATE/CINNAMIC ACID DIOXYGENASE SUBUNIT BETA
The beta subunit may be responsible for the substrate specificity of the enzyme.
Heterohexamer consisting of 3 BphA1 subunits and 3 BphA2 subunits. A ferredoxin (BphA3) and a ferredoxin reductase (BphA4) must be present to obtain activity.
Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.
3-PHENYLPROPIONATE/CINNAMIC ACID DIOXYGENASE FERREDOXIN SUBUNIT
This protein seems to be a 2Fe-2S ferredoxin.
This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (BphA1 and BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4).
Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin component family.
CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-RELATED
Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase
Biphenyl-2,3-dihydro-2,3-diol dehydrogenase
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF NATIVE ENZYME; SUBSTRATE COMPLEXES AND H145A MUTANT
2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1
Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Belongs to the extradiol ring-cleavage dioxygenase family.
ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase
2,6-dioxo-6-phenylhexa-3-enoate hydrolase
Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD).
Belongs to the AB hydrolase superfamily. BphD family.
Draft genome of the atrazine degrading bacteria Pseudomonas sp. ADP.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH METAL ION; SUBSTRATE AND INHIBITOR
Cyanuric acid hydrolase/Barbituras, RU C
Cyanuric acid hydrolase/Barbiturase, RU A
Cyanuric acid hydrolase/Barbiturase, RU B
Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.
kcat is 73 sec(-1) with cyanuric acid as substrate (PubMed:22730121). kcat is 6.8 sec(-1) with cyanuric acid as substrate and 3.1 sec(-1) with N-methylisocyanuric acid as substrate (PubMed:12788776).
The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).
Belongs to the cyclic amide hydrolase (CyAH) family.
MUTAGENESIS OF GLY-163; GLY-166; PRO-168; LYS-169 AND GLU-306
Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as substrates. Inactive towards 4-aminobenzoate, 4-hydroxybenzoate, 2-aminobenzoate, 2,3-dihydroxybenzoate, 4-coumarate and the aliphatic carboxylic acids palmate, caproate, laurate and butyrate. Negligible activity is detected when ATP is replaced by UTP, CTP or GTP as cosubstrate.
Unaffected by 5,5'-dithiobis-(2-nitrobenzoic acid), 4-chloromercuribenzoate and sodium azide. Inhibited by Cu(2+), Fe(2+) and Zn(2+). Unaffected by Na(+), K(+) and Li(+).
104 uM for ATP (with magnesium as cofactor)
43 uM for ATP (with manganese as cofactor)
Optimum pH is 8.4. 85% of activity remains at pH 9.0, 54% of activity remains at pH 7.0.
Optimum temperature is 35 degrees Celsius.
Belongs to the ATP-dependent AMP-binding enzyme family.
Significantly inhibits the adenylation part of the reaction.
MUTAGENESIS OF PHE-64; HIS-81; PHE-82; TRP-89; HIS-90; GLY-114; TRP-137 AND ASP-145
MUTAGENESIS OF ARG-24; PHE-64; ARG-67; GLY-113; GLY-114 AND ARG-257
MUTAGENESIS OF GLY-63; PHE-64; TYR-65; ALA-112; GLY-113 AND GLY-115
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT GLN-90 IN COMPLEX WITH 4-HYDROXYBENZOYL COENZYME A
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT GLN-90 IN COMPLEX WITH 4-HYDROXYBENZOYL COENZYME A
Lyase 2-enoyl-coa Hydratase, Chain A, domain 2
ENOYL-COA HYDRATASE/ISOMERASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G01890)
Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA.
Inactivated by 1 mM Ag(+) and by 5 mM Cu(2+). Partially inhibited by 5 mM Zn(2+), Mn(2+), Co(2+), Fe(2+) and Ni(2+). Unaffected by 10 mM Na(+), K(+) and Li(+) and by 0.5 mM Mg(2+), Mn(2+), Fe(2+), Ca(2+), Co(2+) and Zn(2+). Inhibited by the sulfhydryl blocking agent 5,5'-dithio-bis-(2-nitrobenzoate), SDS and N-bromosuccinimide. Unaffected by sodium azide and EDTA. Inactivated following treatment with diethyl pyrocarbonate; this inactivation is reversible by treatment with hydroxylamine.
2.2 umol/min/mg enzyme with 4-chlorobenzoyl-CoA as substrate
Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and 11.5. Stable from pH 6.5 to 11.0, activity is lost following 10 minutes incubation at pH 4.5 or 12.0.
Optimum temperature is 60 degrees Celsius. Retains 60% of maximum activity at 30 degrees Celsius and 65 degrees Celsius. After 15 minutes preincubation at 60 degrees Celsius 70% of the initial activity remains, 15 minutes preincubation at 65 degrees Celsius results in a total loss of activity.
Homotetramer (PubMed:1610806). Homotetramer, homooctamer and larger multimers (PubMed:7579994). Homotrimer (PubMed:8679561).
By 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA or 4-bromobenzoyl-CoA.
Belongs to the enoyl-CoA hydratase/isomerase family.
Does not strongly affect catalytic activity, but reduces substrate CoA binding.
30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.
Retains catalytic activity, but substrate benzoyl group binding is decreased.
Severely reduces catalytic activity. Arylated intermediate does not accumulate.
Catalytic activity is almost as efficient as wild type.
Loss of catalytic activity, substrate benzoyl group binding is not affected.
Reduced activity and substrate benzoyl group binding.
Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.
Strongly reduced catalytic activity. Arylated intermediate does not accumulate.
Strongly reduced catalytic activity and substrate benzoyl group binding.
Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
Complete loss of catalytic activity, but not substrate binding.
Reduced catalytic activity, increased substrate binding.
Retains catalytic activity and substrate CoA binding.
Significantly reduces catalytic activity and substrate CoA binding.
ligand shared between two oligomeric partners
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-415 IN COMPLEX WITH ZINC
Bacterial exopeptidase dimerisation domain
Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.
Used clinically as a folate-depleting, antitumor agent.
Belongs to the flavin oxidoreductase frp family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-307
2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE
2-hydroxymuconic semialdehyde dehydrogenase
2-hydroxymuconic acid semialdehyde can be converted to 2-hydroxypent-2,4-dienoate either directly by the action of 2-hydroxymuconic semialdehyde hydrolase (HMSH) or by the action of three sequential enzymes, the first of which is HMSD.
Belongs to the aldehyde dehydrogenase family.
2-hydroxymuconate semialdehyde hydrolase
Catalyzes the conversion of 2-hydroxymuconate semialdehyde to 2-hydroxypent-2,4-dienoate.
Belongs to the DmpD/TodF/XylF esterase family.
Fumarylacetoacetase-like, C-terminal domain
Belongs to the hydratase/decarboxylase family.
Phenol 2-monooxygenase, auxiliary component DmpK
DmpK is an auxiliary protein associated with the multicomponent phenol hydroxylase DmpLMNOP and it may be involved in the post-translational incorporation of iron into the oxygenase component of the phenol hydroxylase (PubMed:8995386). Required for growth on phenol but not for in vitro phenol hydroxylase activity (PubMed:2254258, PubMed:2254259).
Homotrimer or homotetramer (PubMed:8995386). Interacts with the phenol hydroxylase components DmpL (P1 component) and DmpN (P3 component) (PubMed:8995386).
Cells lacking this gene cannot grow on phenol.
Phenol 2-monooxygenase, oxygenase component DmpL
Part of a multicomponent enzyme which catalyzes the degradation of phenol and some of its methylated derivatives (PubMed:2254259). DmpL, DmpN and DmpO form the oxygenase component of the complex (PubMed:12186554). Required for growth on phenol and for in vitro phenol hydroxylase activity (PubMed:2254258, PubMed:2254259).
Requires DmpM for efficient turnover. The activity of DmpLNO oxygenase is inhibited by dithiothreitol (DTT) by a mechanism apparently involving H(2)O(2) generation.
The multicomponent enzyme phenol hydroxylase is formed by DmpL (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4 component) and DmpP (P5 component) (PubMed:2254259). The oxygenase component is a dimer composed of three subunits, DmpL, DmpN and DmpO (DmpLNO) (PubMed:12186554). DmpL interacts with the auxiliary protein DmpK (P0 component) (PubMed:8995386).
Monooxygenase (hydroxylase) regulatory protein
Phenol 2-monooxygenase, stimulatory component DmpM
Part of a multicomponent enzyme which catalyzes the degradation of phenol and some of its methylated derivatives (PubMed:2254259). DmpM is a regulatory subunit that stimulates the phenol hydroxylase activity of the complex (PubMed:10451366, PubMed:12186554). The steady-state rate of phenol hydroxylase turnover is dependent on the DmpM concentration, with a maximum observed rate at about 1.5 DmpM per oxygenase monomer. Higher concentrations of DmpM inhibit phenol hydroxylase activity (PubMed:12186554). May act by altering the redox potential of the oxygenase (PubMed:12186554). Required for growth on phenol and for in vitro phenol hydroxylase activity (PubMed:2254258, PubMed:2254259).
Active as a monomer (PubMed:10451366). Formation of dimers inactivates the protein (PubMed:10451366). The multicomponent enzyme phenol hydroxylase is formed by DmpL (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4 component) and DmpP (P5 component) (PubMed:2254259).
Phenol 2-monooxygenase, oxygenase component DmpN
The multicomponent enzyme phenol hydroxylase is formed by DmpL (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4 component) and DmpP (P5 component) (PubMed:2254259). The oxygenase component is a dimer composed of three subunits, DmpL, DmpN and DmpO (DmpLNO) (PubMed:12186554). DmpN interacts with the auxiliary protein DmpK (P0 component) (PubMed:8995386).
Phenol 2-monooxygenase, oxygenase component DmpO
The multicomponent enzyme phenol hydroxylase is formed by DmpL (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4 component) and DmpP (P5 component) (PubMed:2254259). The oxygenase component is a dimer composed of three subunits, DmpL, DmpN and DmpO (DmpLNO) (PubMed:12186554).
Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
Ferredoxin reductase-like, C-terminal NADP-linked domain
Phenol 2-monooxygenase, reductase component DmpP
Part of a multicomponent enzyme which catalyzes the degradation of phenol and some of its methylated derivatives (PubMed:2254259). DmpP probably transfers electrons from NADH, via FAD and the iron-sulfur center, to the oxygenase component of the complex (PubMed:2254259). Required for growth on phenol and for in vitro phenol hydroxylase activity (PubMed:2254258, PubMed:2254259).
The multicomponent enzyme phenol hydroxylase is formed by DmpL (P1 component), DmpM (P2 component), DmpN (P3 component), DmpO (P4 component) and DmpP (P5 component).
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-394 IN COMPLEX WITH NAD
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH NAD AND FORMATE
Formate/glycerate dehydrogenase catalytic domain-like
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
kcat is 10 sec(-1) with formate as substrate.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
High resistance to inactivation by Hg(2+), Increased stability at 25 degree Celsius and decreased thermostability at 45 degree Celsius.
N-terminal nucleophile aminohydrolases (Ntn hydrolases)
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
Cleaved by autocatalysis into a large and a small subunit.
Belongs to the gamma-glutamyltransferase family.
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
HALOACID DEHALOGENASE, TYPE II (AFU_ORTHOLOGUE AFUA_2G07750)-RELATED
HYDROLASE, HALOACID DELAHOGENASE-RELATED
Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids. Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2. Active with 2-halogenated carboxylic acids and converts only the S-isomer (or L-isomer) of 2-chloropropionic acid with inversion of configuration to produce R-lactate (or D-isomer).
(S)-2-haloacid dehalogenases may be used for the biodegradation of halogenated substances and their derivatives which are widely used as pesticides, herbicides and other industrial products.
Belongs to the HAD-like hydrolase superfamily. S-2-haloalkanoic acid dehalogenase family.
2-haloacid dehalogenase, configuration-inverting
Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. Acts on 2-haloalkanoic acids whose carbon chain lengths are five or less.
MUTAGENESIS OF ASP-10; THR-14; ARG-41; SER-118; LYS-151; TYR-157; SER-175; ASN-177 AND ASP-180
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF MUTANT ALA-175 IN COMPLEX WITH MONOCHLOROACETATE AND 2-CHLORO-N-BUTYRATE
The Structure of L-2-Haloacid Dehalogenase Complexed with a Reaction Product Reveals the Mechanism of Intermediate Hydrolysis in Dehalogenase.
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH LACTATE
Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids (PubMed:7490277, PubMed:9614112). Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 (PubMed:7490277, PubMed:9614112). Active with 2-halogenated carboxylic acids and converts only the S-isomer (or L-isomer) of 2-chloropropionic acid with inversion of configuration to produce R-lactate (or D-isomer) (PubMed:7490277, PubMed:9614112).
kcat is 47 sec(-1) for (2S)-2-chloropropanoic acid as substrate.
Severe reduction in catalytic activity. No effect on susbtrate affinity.
Severe reduction in catalytic activity. 4-fold decrease in substrate affinity.
Severe reduction in catalytic activity. 25-fold decrease in substrate affinity.
Severe reduction in catalytic activity. 1.5-fold decrease in substrate affinity.
Severe reduction in catalytic activity. 2-fold decrease in substrate affinity.
Moderate reduction in catalytic activity.
The 3-hexulose-6-phosphate synthase-encoding gene of the obligate methylotroph Aminomonas aminovorus C2A1 is not present on a gene cluster encoding other enzymes of the ribulose monophosphate pathway.
IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7
Belongs to the imidazoleglycerol-phosphate dehydratase family.
2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED
4-hydroxy-2-keto-pentanoic acid aldolase
Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPF; NAD; MANGANESE AND OXALATE
Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols.
Six- to eight-fold activated by Mn(2+). Retains residual activity after EDTA treatment in vitro. Also activated by NADH and, to a lesser extent, by NAD(+). Strongly inhibited by Zn(2+). Mg(2+) and Ca(2+) have no effect on enzymatic activity.
Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes the racemization via enolization of D- and L-5-monosubstituted hydantoins. Is able to racemize 5-substituted hydantoins having either aromatic or aliphatic substituents such as D- and L-5-(2-methylthioethyl)hydantoin.
Strongly inhibited by Cu(2+) and Zn(2+). Slightly stimulated by of Mn(2+) or Co(2+), but also by metal-chelating agents such as EDTA or EGTA.
79 umol/min/mg enzyme with L-5-(2-methylthioethyl)hydantoin as substrate
35.2 umol/min/mg enzyme with D-5-(2-methylthioethyl)hydantoin as substrate
Optimum temperature is 45 degrees Celsius.
Seems to be responsible for recognition and proton retrieval of D-isomers
Seems to be responsible for L-isomers recognition and racemization
This enzyme acts on aliphatic epoxides. Its substrates include epichlorohydrin, epibromohydrin, epoxyoctane and styrene epoxide.
HYPOTHETICAL 5-OXOPROLINASE (EUROFUNG)-RELATED
Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. HyuA and HyuB are both required for the conversion of D- and L-5-substituted hydantoins to corresponding N-carbamoyl-D- and N-carbamoyl-L-amino acids, respectively.
Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes the conversion of N-carbamoyl-L-methionine to L-methionine in an irreversible reaction. Unable to convert N-carbamoyl-D-methionine.
Binds 2 divalent metal cations per subunit.
Confers an increase in glyphosate resistance when expressed in E.coli.
PG2982 is able to utilize glyphosate and other phosphonate compounds as a sole phosphorus source; it can grow in over 100 mM glyphosate.
Belongs to the glycosyl hydrolase 13 family.
May be involved in the folding of the extracellular lipase during its passage through the periplasm.
Catalyzes the hydrolysis of triacylglycerol.
Belongs to the AB hydrolase superfamily. Pseudomonas lipase family.
Catalyzes the hydrolysis of triacylglycerol. Also able to catalyze, in anhydrous organic solvents, intramolecular transesterification of omega-hydroxyfatty acid esters to form macrocyclic lactones. This biosynthesis is dependent on the chain length of the substrates, and the formation of monomer lactone is maximum with methyl 18-hydroxyoctadecanoate. With shorter substrates, monomer lactone decreases and the formation of diolide (dimer lactone) increases.
Alkylsulfatase that cleaves the widely used detergent sodium dodecyl sulfate (SDS), which allows the bacterium to use SDS as a sole carbon or sulfur source.
Belongs to the metallo-beta-lactamase superfamily. Type III sulfatase family.
The N-terminus is shorter than orthologs.
1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase
Cis-naphthalene dihydrodiol dehydrogenase
Dibenzothiophene dihydrodiol dehydrogenase
Catalyzes the oxidation of naphthalene dihydrodiol into 1,2-dihydroxynaphthalene.
Structural explanation for success and failure in the enzymatic ring-cleavage of 3,4 dihydroxybiphenyl and related PCB metabolites.
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-302 IN COMPLEX WITH SUBSTRATE ANALOGS AND IRON ION
Involved in the naphthalene catabolic pathway. Catalyzes the meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic acid (By similarity).
2-hydroxychromene-2-carboxylate isomerase
Involved in the naphthalene catabolic pathway. Catalyzes the reversible glutathione-dependent isomerization of 2-hydroxychromene-2-carboxylate (HCCA) to trans-O-hydroxybenzylidenepyruvate (THBPA) (Probable).
DoxH and doxJ encode different enzymes that may have interchangeable functions.
Belongs to the GST superfamily. NadH family.
4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL
Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase
Involved in the naphthalene upper catabolic pathway. Catalyzes the transformation of trans-O-hydroxybenzylidenepyruvate (THBPA) to salicylaldehyde and pyruvate. The reaction is reversible (Probable).
Dibenzothiophene metabolism operon protein DoxH
May be involved in the conversion of 2-hydroxy-4-(2'-oxo-3,5-cyclohexadienyl)-buta-2,4-dienoate to cis-O-hydroxybenzylidenepyruvate. DoxH and doxJ encode different enzymes that may have interchangeable functions.
Naphthalene 1,2-dioxygenase system, ferredoxin component
Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. Functions as an intermediate electron transfer protein via a specific interaction with iron sulfur protein components (ISP) (DoxB and DoxD).
The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and a dioxygenase component (iron sulfur protein (ISP)). The electron transfer component is composed of a ferredoxin reductase and a ferredoxin (DoxA), and the dioxygenase component is formed of a heterohexamer (trimer of heterodimers) of three large alpha subunits (DoxB) and three small beta subunits (DoxD).
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF WILD-TYPE AND MUTANT VAL-352 IN COMPLEX WITH SUBSTRATE ANALOG; IRON ION AND IRON-SULFUR (2FE-2S)
Naphthalene 1,2-Dioxygenase bound to thioanisole.
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON; IRON-SULFUR (2FE-2S) AND SUBSTRATE ANALOGS
Naphthalene 1,2-dioxygenase system, large oxygenase component
Naphthalene 1,2-dioxygenase subunit alpha
Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme.
Cells lacking this gene are unable to degrade naphthalene.
Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
Naphthalene 1,2-dioxygenase system, small oxygenase component
Naphthalene 1,2-dioxygenase subunit beta
Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The beta subunit seems to have a structural role in the holoenzyme.
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A, MITOCHONDRIAL
Catalyzes the hydrolysis of 6-aminohexanoic acid cyclic dimer (1,8-diazacyclotetradecane-2,9-dione) to form the linear dimer 6-aminohexanoyl-6-aminohexanoic acid.
Besides the cephalosporin acylase I activity which converts GL-7ACA into 7-ACA; this enzyme displays some gamma glutamyltranspeptidase activity.
Dimer of two non-identical chains processed from the same precursor.
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Heterodimer of a small subunit and a large subunit processed from the same precursor.
TonB-dependent receptor, beta-barrel domain
Specific receptor for the siderophore ferric pyoverdine (pseudobactin) M114.
Belongs to the TonB-dependent receptor family.
D-Amino Acid Oxidase, subunit A, domain 2
FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN-RELATED
Belongs to the PheA/TfdB FAD monooxygenase family.
DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14270)-RELATED
DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED
Belongs to the intradiol ring-cleavage dioxygenase family.
MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 217-585
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 216-587
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 216-585 IN COMPLEX WITH INHIBITOR
PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2
Pepstatin-insensitive carboxyl proteinase
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
SDS degradation transcriptional activation protein
Activates the transcription of the sdsA gene for sodium dodecyl sulfate (SDS) degradation.
Belongs to the LysR transcriptional regulatory family.
Vanillate O-demethylase oxygenase subunit
This demethylase system consists of two proteins: an oxygenase and an oxygenase reductase.
CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT
Vanillate degradation ferredoxin-like protein
P-loop containing nucleotide triphosphate hydrolases
SIGMA L-DEPENDENT TRANSCRIPTIONAL REGULATOR YPLP-RELATED
P-loop containing nucleoside triphosphate hydrolases
Uncharacterized protein in HyuA 5'region
NCS1 FAMILY PURINE/PYRIMIDINE TRANSPORTER
Uncharacterized protein in hyuC 3'region
Belongs to the purine-cytosine permease (2.A.39) family.