The Enzyme Database

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EC 1.3.1.53     
Accepted name: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase
Reaction: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD+ = 3,4-dihydroxybenzoate + CO2 + NADH
Glossary: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate = cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate
Other name(s): (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase; terephthalate 1,2-cis-dihydrodiol dehydrogenase; cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate:NAD+ oxidoreductase (decarboxylating)
Systematic name: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NAD+ oxidoreductase
Comments: Requires FeII. Involved in the terephthalate degradation pathway in bacteria [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 162032-77-1
References:
1.  Saller, E., Laue, H.R., Schläfli Oppenberg, H.R. and Cook, A.M. Purification and some properties of (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2. FEMS Microbiol. Lett. 130 (1996) 97–102.
2.  Wang, Y.Z., Zhou, Y. and Zylstra, G.J. Molecular analysis of isophthalate and terephthalate degradation by Comamonas testosteroni YZW-D. Environ. Health Perspect. 103, Suppl. 5 (1995) 9–12. [PMID: 8565920]
[EC 1.3.1.53 created 1999 (EC 1.3.1.61 created 2000, incorporated 2007)]
 
 
EC 1.3.1.61      
Deleted entry: terephthalate 1,2-cis-dihydrodiol dehydrogenase. Enzyme is identical to EC 1.3.1.53, (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase
[EC 1.3.1.61 created 2000, deleted 2007]
 
 
EC 1.13.11.3     
Accepted name: protocatechuate 3,4-dioxygenase
Reaction: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
For diagram of benzoate metabolism, click here
Glossary: 3,4-dihydroxybenzoate = protocatechuate
Other name(s): protocatechuate oxygenase; protocatechuic acid oxidase; protocatechuic 3,4-dioxygenase; protocatechuic 3,4-oxygenase; protocatechuate:oxygen 3,4-oxidoreductase (decyclizing)
Systematic name: protocatechuate:oxygen 3,4-oxidoreductase (ring-opening)
Comments: Requires Fe3+. The enzyme, which participates in the degradation of aromatic compounds, catalyses 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-47-4
References:
1.  Fujisawa, H. and Hayaishi, O. Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization. J. Biol. Chem. 243 (1968) 2673–2681. [PMID: 4967959]
2.  Gross, S.R., Gafford, R.D. and Tatum, E.L. The metabolism of protocatechuic acid by Neurospora. J. Biol. Chem. 219 (1956) 781–796. [PMID: 13319299]
3.  Stanier, R.Y. and Ingraham, J.L. Protocatechuic acid oxidase. J. Biol. Chem. 210 (1954) 799–820. [PMID: 13211618]
[EC 1.13.11.3 created 1961 as EC 1.99.2.3, transferred 1965 to EC 1.13.1.3, transferred 1972 to EC 1.13.11.3]
 
 
EC 1.13.11.8     
Accepted name: protocatechuate 4,5-dioxygenase
Reaction: 3,4-dihydroxybenzoate + O2 = 4-carboxy-2-hydroxymuconate semialdehyde
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Glossary: 3,4-dihydroxybenzoate = protocatechuate
Other name(s): protocatechuate 4,5-oxygenase; protocatechuic 4,5-dioxygenase; protocatechuic 4,5-oxygenase; protocatechuate:oxygen 4,5-oxidoreductase (decyclizing); protocatechuate:oxygen 4,5-oxidoreductase (ring-opening)
Systematic name: 3,4-dihydroxybenzoate:oxygen 4,5-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-56-5
References:
1.  Trippett, S., Dagley, S. and Stopher, D.A. The bacterial oxidation of nicotinic acid. Biochem. J. 76 (1960) 9.
[EC 1.13.11.8 created 1965 as EC 1.13.1.8, transferred 1972 to EC 1.13.11.8]
 
 
EC 1.14.12.8     
Accepted name: 4-sulfobenzoate 3,4-dioxygenase
Reaction: 4-sulfobenzoate + NADH + H+ + O2 = 3,4-dihydroxybenzoate + sulfite + NAD+
For diagram of reaction, click here
Other name(s): 4-sulfobenzoate dioxygenase; 4-sulfobenzoate 3,4-dioxygenase system
Systematic name: 4-sulfobenzoate,NADH:oxygen oxidoreductase (3,4-hydroxylating, sulfite-forming)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 122933-81-7
References:
1.  Locher, H.H., Leisinger, T. and Cook, A.M. 4-Sulphobenzoate 3,4-dioxygenase. Purification and properties of a desulphonative two-component enzyme system from Comamonas testosteroni T-2. Biochem. J. 274 (1991) 833–842. [PMID: 2012609]
[EC 1.14.12.8 created 1992]
 
 
EC 1.14.13.2     
Accepted name: 4-hydroxybenzoate 3-monooxygenase
Reaction: 4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
For diagram of benzoate metabolism, click here
Glossary: 3,4-dihydroxybenzoate = protocatechuate
Other name(s): p-hydroxybenzoate hydrolyase; p-hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-hydroxylase; 4-hydroxybenzoate monooxygenase; 4-hydroxybenzoic hydroxylase; p-hydroxybenzoate-3-hydroxylase; p-hydroxybenzoic acid hydrolase; p-hydroxybenzoic acid hydroxylase; p-hydroxybenzoic hydroxylase
Systematic name: 4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9059-23-8
References:
1.  Hosokawa, K. and Stanier, R.Y. Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida. J. Biol. Chem. 241 (1966) 2453–2460. [PMID: 4380381]
2.  Howell, L.G., Spector, T. and Massey, V. Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4340–4350. [PMID: 4402514]
3.  Spector, T. and Massey, V. Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4679–4687. [PMID: 4402938]
4.  Spector, T. and Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate. J. Biol. Chem. 247 (1972) 5632–5636. [PMID: 4403446]
5.  Spector, T. and Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Reactivity with oxygen. J. Biol. Chem. 247 (1972) 7123–7127. [PMID: 4404745]
6.  Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J. and Muller, R. 4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity. Eur. J. Biochem. 239 (1996) 469–478. [DOI] [PMID: 8706756]
[EC 1.14.13.2 created 1972, modified 1999]
 
 
EC 1.14.13.23     
Accepted name: 3-hydroxybenzoate 4-monooxygenase
Reaction: 3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O
Other name(s): 3-hydroxybenzoate 4-hydroxylase
Systematic name: 3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating)
Comments: A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37256-76-1
References:
1.  Michalover, J.L. and Ribbons, D.W. 3-Hydroxybenzoate 4-hydroxylase from Pseudomonas testosteroni. Biochem. Biophys. Res. Commun. 55 (1973) 888–896. [DOI] [PMID: 4148586]
2.  Premkumar, R., Subba Rao, P.V., Streeleela, N.S. and Vaidyanathan, C.S. m-Hydroxybenzoic acid 4-hydroxylase from Aspergillus niger. Can. J. Biochem. 47 (1969) 825–827. [PMID: 4390252]
[EC 1.14.13.23 created 1972 as EC 1.14.99.13, transferred 1984 to EC 1.14.13.23]
 
 
EC 1.14.13.33     
Accepted name: 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
Reaction: 4-hydroxybenzoate + NAD(P)H + H+ + O2 = 3,4-dihydroxybenzoate + NAD(P)+ + H2O
Other name(s): 4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine dinucleotide (phosphate)); 4-hydroxybenzoate-3-hydroxylase; 4-hydroxybenzoate 3-hydroxylase
Systematic name: 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein (FAD). 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 4-hydroxybenzoate 3-monooxygenase). It is less specific for NADPH than EC 1.14.13.2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 95471-33-3
References:
1.  Fujii, T. and Kaneda, T. Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 147 (1985) 97–104. [DOI] [PMID: 3971979]
2.  Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J. and Muller, R. 4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity. Eur. J. Biochem. 239 (1996) 469–478. [DOI] [PMID: 8706756]
[EC 1.14.13.33 created 1989, modified 1999]
 
 
EC 1.14.13.82     
Accepted name: vanillate monooxygenase
Reaction: vanillate + O2 + NADH + H+ = 3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
Glossary: vanillate = 4-hydroxy-3-methoxybenzoate
Other name(s): 4-hydroxy-3-methoxybenzoate demethylase; vanillate demethylase
Systematic name: vanillate:oxygen oxidoreductase (demethylating)
Comments: Forms part of the vanillin degradation pathway in Arthrobacter sp.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 39307-11-4
References:
1.  Brunel, F. and Davison, J. Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. J. Bacteriol. 170 (1988) 4924–4930. [DOI] [PMID: 3170489]
2.  Priefert, H., Rabenhorst, J. and Steinbuchel, A. Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J. Bacteriol. 179 (1997) 2595–2607. [DOI] [PMID: 9098058]
[EC 1.14.13.82 created 2000 as EC 1.2.3.12, transferred 2003 to EC 1.14.13.82]
 
 
EC 1.14.19.55     
Accepted name: 4-hydroxybenzoate brominase (decarboxylating)
Reaction: (1) 4-hydroxybenzoate + 2 NADPH + 2 bromide + 2 O2 + 2 H+ = 2,4-dibromophenol + 2 NADP+ + CO2 + 4 H2O (overall reaction)
(1a) 4-hydroxybenzoate + NADPH + bromide + O2 + H+ = 3-bromo-4-hydroxybenzoate + NADP+ + 2 H2O
(1b) 3-bromo-4-hydroxybenzoate + NADPH + bromide + O2 + H+ = 2,4-dibromophenol + NADP+ + CO2 + 2 H2O
(2) 3,4-dihydroxybenzoate + 2 NADPH + 2 bromide + 2 O2 + 2 H+ = 3,5-dibromobenzene-1,2-diol + 2 NADP+ + CO2 + 4 H2O (overall reaction)
(2a) 3,4-dihydroxybenzoate + NADPH + bromide + O2 + H+ = 3-bromo-4,5-dihydroxybenzoate + NADP+ + 2 H2O
(2b) 3-bromo-4,5-dihydroxybenzoate + NADPH + bromide + O2 + H+ = 3,5-dibromobenzene-1,2-diol + NADP+ + CO2 + 2 H2O
Other name(s): bmp5 (gene name)
Systematic name: 4-hydroxybenzoate:NADPH oxidoreductase (brominating, decarboxylating)
Comments: Contains FAD. 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 catalyses a bromination of its substrate, followed by a second bromination concurrent with decarboxylation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Agarwal, V., El Gamal, A.A., Yamanaka, K., Poth, D., Kersten, R.D., Schorn, M., Allen, E.E. and Moore, B.S. Biosynthesis of polybrominated aromatic organic compounds by marine bacteria. Nat. Chem. Biol. 10 (2014) 640–647. [DOI] [PMID: 24974229]
2.  Agarwal, V. and Moore, B.S. Enzymatic synthesis of polybrominated dioxins from the marine environment. ACS Chem. Biol. 9 (2014) 1980–1984. [DOI] [PMID: 25061970]
[EC 1.14.19.55 created 2018]
 
 
EC 2.1.1.341     
Accepted name: vanillate/3-O-methylgallate O-demethylase
Reaction: (1) vanillate + tetrahydrofolate = protocatechuate + 5-methyltetrahydrofolate
(2) 3-O-methylgallate + tetrahydrofolate = gallate + 5-methyltetrahydrofolate
Glossary: protocatechuate = 3,4-dihydroxybenzoate
vanillate = 4-hydroxy-3-methoxybenzoate
gallate = 3,4,5-trihydroxybenzoate
Other name(s): ligM (gene name)
Systematic name: vanillate:tetrahydrofolate O-methyltransferase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nishikawa, S., Sonoki, T., Kasahara, T., Obi, T., Kubota, S., Kawai, S., Morohoshi, N. and Katayama, Y. Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene essential for the O demethylation of vanillate and syringate. Appl. Environ. Microbiol. 64 (1998) 836–842. [PMID: 9501423]
2.  Masai, E., Sasaki, M., Minakawa, Y., Abe, T., Sonoki, T., Miyauchi, K., Katayama, Y. and Fukuda, M. A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J. Bacteriol. 186 (2004) 2757–2765. [DOI] [PMID: 15090517]
3.  Abe, T., Masai, E., Miyauchi, K., Katayama, Y. and Fukuda, M. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187 (2005) 2030–2037. [DOI] [PMID: 15743951]
[EC 2.1.1.341 created 2017]
 
 
EC 4.1.1.55     
Accepted name: 4,5-dihydroxyphthalate decarboxylase
Reaction: 4,5-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO2
Other name(s): 4,5-dihydroxyphthalate carboxy-lyase
Systematic name: 4,5-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37290-48-5
References:
1.  Ribbons, D.W. and Evans, W.C. Oxidative metabolism of phthalic acid by soil pseudomonads. Biochem. J. 76 (1966) 310–318. [PMID: 16748829]
[EC 4.1.1.55 created 1972]
 
 
EC 4.1.1.63     
Accepted name: protocatechuate decarboxylase
Reaction: 3,4-dihydroxybenzoate = catechol + CO2
Glossary: protocatechuate = 3,4-dihydroxybenzoate
Other name(s): 3,4-dihydrobenzoate decarboxylase; protocatechuate carboxy-lyase
Systematic name: 3,4-dihydroxybenzoate carboxy-lyase (catechol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37290-55-4
References:
1.  Grant, D.J.W. and Patel, J.C. Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). J. Microbiol. Serol. 35 (1969) 325–343. [PMID: 5309907]
[EC 4.1.1.63 created 1972]
 
 
EC 4.1.1.69     
Accepted name: 3,4-dihydroxyphthalate decarboxylase
Reaction: 3,4-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO2
Other name(s): 3,4-dihydroxyphthalate carboxy-lyase
Systematic name: 3,4-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83137-76-2
References:
1.  Eaton, R.W. and Ribbons, D.W. Metabolism of dibutylphthalate and phthalate by Micrococcus sp. strain 12B. J. Gen. Microbiol. 151 (1982) 48–57. [PMID: 7085570]
[EC 4.1.1.69 created 1986]
 
 
EC 4.1.3.17     
Accepted name: 4-hydroxy-4-methyl-2-oxoglutarate aldolase
Reaction: (1) 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
(2) 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Other name(s): pyruvate aldolase; γ-methyl-γ-hydroxy-α-ketoglutaric aldolase; 4-hydroxy-4-methyl-2-ketoglutarate aldolase; 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase; HMG aldolase; CHA aldolase; 4-carboxy-4-hydroxy-2-oxoadipate aldolase
Systematic name: 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase (pyruvate-forming)
Comments: Requires a divalent metal ion [3]. This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), phthalate, syringate and 3,4,5-trihydroxybenzoate [1-3]. The enzyme from Pseudomonas straminea can also catalyse the activity of EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase, and the decarboxylation of oxaloacetate [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-65-6
References:
1.  Tack, B.F., Chapman, P.J. and Dagley, S. Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase. J. Biol. Chem. 247 (1972) 6444–6449. [PMID: 5076765]
2.  Wood, W.A. 2-Keto-3-deoxy-6-phosphogluconic and related aldolases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 7, Academic Press, New York, 1972, pp. 281–302.
3.  Maruyama, K. Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate. J. Biochem. 108 (1990) 327–333. [PMID: 2229032]
4.  Nogales, J., Canales, A., Jiménez-Barbero, J., Serra B., Pingarrón, J. M., García, J. L. and Díaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359–374. [DOI] [PMID: 21219457]
[EC 4.1.3.17 created 1972, modified 2012]
 
 
EC 4.2.1.83     
Accepted name: 4-oxalomesaconate hydratase
Reaction: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate + H2O
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Other name(s): 4-oxalmesaconate hydratase; 4-carboxy-2-oxohexenedioate hydratase; 4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase; oxalmesaconate hydratase; γ-oxalmesaconate hydratase; 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase; LigJ; GalB
Systematic name: (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate 1,2-hydro-lyase (2-hydroxy-4-oxobutane-1,2,4-tricarboxylate-forming)
Comments: This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), syringate and 3,4,5-trihydroxybenzoate, catalysing the reaction in the opposite direction [1-3]. It accepts the enol-form of 4-oxalomesaconate, 2-hydroxy-4-carboxy-hexa-2,4-dienedioate [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85204-95-1
References:
1.  Maruyama, K. Enzymes responsible for degradation of 4-oxalmesaconic acid in Pseudomonas ochraceae. J. Biochem. 93 (1983) 567–574. [PMID: 6841354]
2.  Maruyama, K. Purification and properties of γ-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate. Biochem. Biophys. Res. Commun. 128 (1985) 271–277. [DOI] [PMID: 3985968]
3.  Hara, H., Masai, E., Katayama, Y. and Fukuda, M. The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182 (2000) 6950–6957. [DOI] [PMID: 11092855]
4.  Nogales, J., Canales, A., Jiménez-Barbero, J., Serra B., Pingarrón, J. M., García, J. L. and Díaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359–374. [DOI] [PMID: 21219457]
[EC 4.2.1.83 created 1986, modified 2011]
 
 
EC 4.2.1.118     
Accepted name: 3-dehydroshikimate dehydratase
Reaction: 3-dehydro-shikimate = 3,4-dihydroxybenzoate + H2O
Glossary: 3,4-dihydroxybenzoate = protocatechuate
Systematic name: 3-dehydroshikimate hydro-lyase
Comments: Catalyses an early step in the biosynthesis of petrobactin, a siderophore produced by many bacteria, including the human pathogen Bacillus anthracis. Requires divalent ions, with a preference for Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fox, D.T., Hotta, K., Kim, C.Y. and Koppisch, A.T. The missing link in petrobactin biosynthesis: asbF encodes a (-)-3-dehydroshikimate dehydratase. Biochemistry 47 (2008) 12251–12253. [DOI] [PMID: 18975921]
2.  Pfleger, B.F., Kim, Y., Nusca, T.D., Maltseva, N., Lee, J.Y., Rath, C.M., Scaglione, J.B., Janes, B.K., Anderson, E.C., Bergman, N.H., Hanna, P.C., Joachimiak, A. and Sherman, D.H. Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis. Proc. Natl. Acad. Sci. USA 105 (2008) 17133–17138. [DOI] [PMID: 18955706]
[EC 4.2.1.118 created 2009]
 
 
EC 6.2.1.37     
Accepted name: 3-hydroxybenzoate—CoA ligase
Reaction: ATP + 3-hydroxybenzoate + CoA = AMP + diphosphate + 3-hydroxybenzoyl-CoA
Other name(s): 3-hydroxybenzoyl-CoA synthetase; 3-hydroxybenzoate—coenzyme A ligase (AMP-forming); 3-hydroxybenzoyl coenzyme A synthetase; 3-hydroxybenzoyl-CoA ligase
Systematic name: 3-hydroxybenzoate:CoA ligase (AMP-forming)
Comments: The enzyme works equally well with 4-hydroxybenzoate but shows low activity towards 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Laempe, D., Jahn, M., Breese, K., Schägger, H. and Fuchs, G. Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica. J. Bacteriol. 183 (2001) 968–979. [DOI] [PMID: 11208796]
[EC 6.2.1.37 created 2011]
 
 
EC 6.2.1.62     
Accepted name: 3,4-dihydroxybenzoate—[aryl-carrier protein] ligase
Reaction: ATP + 3,4-dihydroxybenzoate + holo-[aryl-carrier protein] = AMP + diphosphate + 3,4-dihydroxybenzoyl-[aryl-carrier protein] (overall reaction)
(1a) ATP + 3,4-dihydroxybenzoate = diphosphate + (3,4-dihydroxybenzoyl)adenylate
(1b) (3,4-dihydroxybenzoyl)adenylate + holo-[aryl-carrier protein] = AMP + 3,4-dihydroxybenzoyl-[aryl-carrier protein]
Other name(s): asbC (gene name)
Systematic name: 3,4-dihydroxybenzoate:[aryl-carrier protein] ligase (AMP-forming)
Comments: The adenylation domain of the enzyme catalyses 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pfleger, B.F., Lee, J.Y., Somu, R.V., Aldrich, C.C., Hanna, P.C. and Sherman, D.H. Characterization and analysis of early enzymes for petrobactin biosynthesis in Bacillus anthracis. Biochemistry 46 (2007) 4147–4157. [PMID: 17346033]
[EC 6.2.1.62 created 2020]
 
 


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