The Enzyme Database

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EC 1.1.1.312     
Accepted name: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
Reaction: 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Other name(s): 2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase; 4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+ oxidoreductase; α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase; 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase; LigC; ProD
Systematic name: 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase
Comments: 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 [1]. However, later studies showed that the substrate is the hemiacetal form [3], and the product is 2-oxo-2H-pyran-4,6-dicarboxylate [2,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Maruyama, K., Ariga, N., Tsuda, M. and Deguchi, K. Purification and properties of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem. (Tokyo) 83 (1978) 1125–1134. [PMID: 26671]
2.  Maruyama, K. Isolation and identification of the reaction product of α-hydroxy-γ-carboxymuconic ε-semialdehyde dehydrogenase. J. Biochem. 86 (1979) 1671–1677. [PMID: 528534]
3.  Maruyama, K. Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. J. Biochem. (Tokyo) 93 (1983) 557–565. [PMID: 6841353]
4.  Masai, E., Momose, K., Hara, H., Nishikawa, S., Katayama, Y. and Fukuda, M. Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 182 (2000) 6651–6658. [DOI] [PMID: 11073908]
[EC 1.1.1.312 created 1978 as EC 1.2.1.45, transferred 2011 to EC 1.1.1.312]
 
 
EC 1.2.1.85     
Accepted name: 2-hydroxymuconate-6-semialdehyde dehydrogenase
Reaction: 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
For diagram of catechol catabolism (meta ring cleavage), click here
Glossary: 2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): xylG (gene name); praB (gene name)
Systematic name: 2-hydroxymuconate-6-semialdehyde:NAD+ oxidoreductase
Comments: This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2, catechol 2,3-dioxygenase), and is an intermediate in the bacterial degradation of several aromatic compounds. Has lower activity with benzaldehyde [1]. Activity with NAD+ is more than 10-fold higher than with NADP+ [3]. cf. EC 1.2.1.32, aminomuconate-semialdehyde dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Inoue, J., Shaw, J.P., Rekik, M. and Harayama, S. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. J. Bacteriol. 177 (1995) 1196–1201. [DOI] [PMID: 7868591]
2.  Orii, C., Takenaka, S., Murakami, S. and Aoki, K. Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. strain 10d: A different modified meta-cleavage pathway for 2-aminophenols. Biosci. Biotechnol. Biochem. 70 (2006) 2653–2661. [DOI] [PMID: 17090920]
3.  Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758–6768. [DOI] [PMID: 19717587]
[EC 1.2.1.85 created 2012]
 
 
EC 1.13.1.3      
Transferred entry: Now EC 1.13.11.3, protocatechuate 3,4-dioxygenase
[EC 1.13.1.3 created 1961 as EC 1.99.2.3, transferred 1965 to EC 1.13.1.3, deleted 1972]
 
 
EC 1.13.1.8      
Transferred entry: Now EC 1.13.11.8, protocatechuate 4,5-dioxygenase
[EC 1.13.1.8 created 1965, deleted 1972]
 
 
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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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 1.13.11.15     
Accepted name: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
Reaction: 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde
Other name(s): 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase; HPC dioxygenase; homoprotocatechuate 2,3-dioxygenase; 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (ring-opening)
Comments: An iron protein.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-56-7
References:
1.  Adachi, K., Takeda, Y., Senoh, S. and Kita, H. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta 93 (1964) 483–493. [DOI] [PMID: 14263147]
2.  Barbour, M.G. and Bayly, R.C. Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 147 (1981) 844–850. [PMID: 6895079]
3.  Krishnan Kutty, R., Devi, N.A., Veeraswamy, M., Ramesh, S. and Subba Rao, P.V. Degradation of (±)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde. Biochem. J. 167 (1977) 163–170. [PMID: 588248]
[EC 1.13.11.15 created 1972]
 
 
EC 1.13.11.57     
Accepted name: gallate dioxygenase
Reaction: 3,4,5-trihydroxybenzoate + O2 = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Glossary: 3,4,5-trihydroxybenzoate = gallate
Other name(s): GalA; gallate:oxygen oxidoreductase
Systematic name: 3,4,5-trihydroxybenzoate:oxygen oxidoreductase
Comments: Contains non-heme Fe2+. The enzyme is a ring-cleavage dioxygenase that acts specifically on 3,4,5-trihydroxybenzoate to produce the keto-tautomer of 4-oxalomesaconate [1,2].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc
References:
1.  Nogales, J., Canales, A., JimĂ©nez-Barbero, J., García, J.L. and Díaz, E. Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440. The prototype of a new subgroup of extradiol dioxygenases. J. Biol. Chem. 280 (2005) 35382–35390. [DOI] [PMID: 16030014]
2.  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 1.13.11.57 created 2011]
 
 
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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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 1.14.13.82     
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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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 1.99.2.3      
Transferred entry: Now EC 1.13.11.3, protocatechuate 3,4-dioxygenase
[EC 1.99.2.3 created 1961, deleted 1965]
 
 
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, PDB
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 2.8.3.6     
Accepted name: 3-oxoadipate CoA-transferase
Reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
For diagram of benzoate metabolism, click here and for diagram of 4-nitrophenol metabolism, click here
Other name(s): 3-oxoadipate coenzyme A-transferase; 3-oxoadipate succinyl-CoA transferase
Systematic name: succinyl-CoA:3-oxoadipate CoA-transferase
Comments: 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.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-16-8
References:
1.  Katagiri, M. and Hayaishi, O. Enzymatic degradation of β-ketoadipic acid. J. Biol. Chem. 226 (1957) 439–448. [PMID: 13428776]
2.  Kaschabek, S.R., Kuhn, B., Müller, D., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 207–215. [DOI] [PMID: 11741862]
3.  Gobel, M., Kassel-Cati, K., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 216–223. [DOI] [PMID: 11741863]
[EC 2.8.3.6 created 1961]
 
 
EC 3.1.1.24     
Accepted name: 3-oxoadipate enol-lactonase
Reaction: 3-oxoadipate enol-lactone + H2O = 3-oxoadipate
For diagram of benzoate metabolism, click here
Other name(s): carboxymethylbutenolide lactonase; β-ketoadipic enol-lactone hydrolase; 3-ketoadipate enol-lactonase; 3-oxoadipic enol-lactone hydrolase; β-ketoadipate enol-lactone hydrolase
Systematic name: 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase
Comments: The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-04-3
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway. J. Biol. Chem. 241 (1966) 3787–3794. [PMID: 5916392]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
[EC 3.1.1.24 created 1961 as EC 3.1.1.16, part transferred 1972 to EC 3.1.1.24]
 
 
EC 3.1.1.57     
Accepted name: 2-pyrone-4,6-dicarboxylate lactonase
Reaction: 2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Other name(s): 2-pyrone-4,6-dicarboxylate hydrolase; 2-pyrone-4,6-dicarboxylate lactonohydrolase
Systematic name: 2-oxo-2H-pyran-4,6-dicarboxylate lactonohydrolase
Comments: The product is most likely the keto-form of 4-oxalomesaconate (as shown in the reaction) [1,2]. 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, 4-oxalomesaconate tautomerase [3].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 84177-55-9
References:
1.  Kersten, P.J., Dagley, S., Whittaker, J.W., Arciero, D.M. and Lipscomb, J.D. 2-Pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species. J. Bacteriol. 152 (1982) 1154–1162. [PMID: 7142106]
2.  Maruyama, K. Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase. J. Biochem. (Tokyo) 93 (1983) 557–565. [PMID: 6841353]
3.  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 3.1.1.57 created 1986, modified 2010]
 
 
EC 4.1.1.44     
Accepted name: 4-carboxymuconolactone decarboxylase
Reaction: (R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 4,5-dihydro-5-oxofuran-2-acetate + CO2
For diagram of benzoate metabolism, click here
Glossary: 4-carboxymuconolactone = 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate
Other name(s): γ-4-carboxymuconolactone decarboxylase; 4-carboxymuconolactone carboxy-lyase; 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)
Systematic name: (R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-46-6
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J. Biol. Chem. 241 (1966) 3795–3799. [PMID: 5330966]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
[EC 4.1.1.44 created 1972]
 
 
EC 4.1.1.63     
Accepted name: protocatechuate decarboxylase
Reaction: 3,4-dihydroxybenzoate = catechol + CO2
For diagram of catechol biosynthesis, click here
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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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 4.1.1.77     
Accepted name: 2-oxo-3-hexenedioate decarboxylase
Reaction: (3E)-2-oxohex-3-enedioate = 2-oxopent-4-enoate + CO2
For diagram of catechol catabolism (meta ring cleavage), click here
Other name(s): 4-oxalocrotonate carboxy-lyase (misleading); 4-oxalocrotonate decarboxylase (misleading); cnbF (gene name); praD (gene name); amnE (gene name); nbaG (gene name); xylI (gene name)
Systematic name: (3E)-2-oxohex-3-enedioate carboxy-lyase (2-oxopent-4-enoate-forming)
Comments: 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 [1-4]. 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, 2-hydroxymuconate tautomerase, showed that the actual substrate for the enzyme is (3E)-2-oxohex-3-enedioate [4].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37325-55-6
References:
1.  Shingler, V., Marklund, U., Powlowski, J. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174 (1992) 711–724. [DOI] [PMID: 1732207]
2.  Takenaka, S., Murakami, S., Shinke, R. and Aoki, K. Metabolism of 2-aminophenol by Pseudomonas sp. AP-3: modified meta-cleavage pathway. Arch. Microbiol. 170 (1998) 132–137. [PMID: 9683650]
3.  Stanley, T.M., Johnson, W.H., Jr., Burks, E.A., Whitman, C.P., Hwang, C.C. and Cook, P.F. Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase. Biochemistry 39 (2000) 718–726. [DOI] [PMID: 10651637]
4.  Wang, S.C., Johnson, W.H., Jr., Czerwinski, R.M., Stamps, S.L. and Whitman, C.P. Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions. Biochemistry 46 (2007) 11919–11929. [DOI] [PMID: 17902707]
5.  Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758–6768. [DOI] [PMID: 19717587]
[EC 4.1.1.77 created 1999, modified 2011, modified 2012]
 
 
EC 4.1.2.52     
Accepted name: 4-hydroxy-2-oxoheptanedioate aldolase
Reaction: 4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde
Other name(s): 2,4-dihydroxyhept-2-enedioate aldolase; HHED aldolase; 4-hydroxy-2-ketoheptanedioate aldolase; HKHD aldolase; HpcH; HpaI; 4-hydroxy-2-oxoheptanedioate succinate semialdehyde lyase (pyruvate-forming)
Systematic name: 4-hydroxy-2-oxoheptanedioate succinate-semialdehyde-lyase (pyruvate-forming)
Comments: Requires Co2+ or Mn2+ for activity. The enzyme is also able to catalyse 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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Wang, W. and Seah, S.Y. Purification and biochemical characterization of a pyruvate-specific class II aldolase, HpaI. Biochemistry 44 (2005) 9447–9455. [DOI] [PMID: 15996099]
2.  Rea, D., Fulop, V., Bugg, T.D. and Roper, D.I. Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli. J. Mol. Biol. 373 (2007) 866–876. [DOI] [PMID: 17881002]
3.  Wang, W. and Seah, S.Y. The role of a conserved histidine residue in a pyruvate-specific class II aldolase. FEBS Lett. 582 (2008) 3385–3388. [DOI] [PMID: 18775708]
4.  Wang, W., Baker, P. and Seah, S.Y.K. Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling. Biochemistry 49 (2010) 3774–3782. [DOI] [PMID: 20364820]
[EC 4.1.2.52 created 2013]
 
 
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, PDB, 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, PDB, 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, PDB
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 4.2.1.163     
Accepted name: 2-oxo-hept-4-ene-1,7-dioate hydratase
Reaction: (4Z)-2-oxohept-4-enedioate + H2O = (4S)-4-hydroxy-2-oxoheptanedioate
Other name(s): HpcG
Systematic name: (4S)-4-hydroxy-2-oxoheptanedioate hydro-lyase [(4Z)-2-oxohept-4-enedioate-forming]
Comments: Requires Mg2+ [2]. Part of a 4-hydroxyphenylacetate degradation pathway in Escherichia coli C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Burks, E.A., Johnson, W.H., Jr. and Whitman, C.P. Stereochemical and isotopic labeling studies of 2-oxo-hept-4-ene-1,7-dioate hydratase: evidence for an enzyme-catalyzed ketonization step in the hydration reaction. J. Am. Chem. Soc. 120 (1998) 7665–7675.
2.  Izumi, A., Rea, D., Adachi, T., Unzai, S., Park, S.Y., Roper, D.I. and Tame, J.R. Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli. J. Mol. Biol. 370 (2007) 899–911. [DOI] [PMID: 17559873]
[EC 4.2.1.163 created 2016]
 
 
EC 5.3.2.6     
Accepted name: 2-hydroxymuconate tautomerase
Reaction: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate
For diagram of catechol catabolism (meta ring cleavage), click here
Glossary: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
Other name(s): 4-oxalocrotonate tautomerase (misleading); 4-oxalocrotonate isomerase (misleading); cnbG (gene name); praC (gene name); xylH (gene name)
Systematic name: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate ketoenol isomerase
Comments: Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols. 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 [6]. Another keto form, (4E)-2-oxohex-4-enedioate (4-oxalocrotonate), was originally thought to be produced by the enzyme [1,2] but later shown to be produced non-enzymically [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Whitman, C.P., Aird, B.A., Gillespie, W.R. and Stolowich, N.J. Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol. J. Am. Chem. Soc. 113 (1991) 3154–3162.
2.  Whitman, C.P., Hajipour, G., Watson, R.J., Johnson, W.H., Jr., Bembenek, M.E. and Stolowich, N.J. Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase. J. Am. Chem. Soc. 114 (1992) 10104–10110.
3.  Subramanya, H.S., Roper, D.I., Dauter, Z., Dodson, E.J., Davies, G.J., Wilson, K.S. and Wigley, D.B. Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. Biochemistry 35 (1996) 792–802. [DOI] [PMID: 8547259]
4.  Stivers, J.T., Abeygunawardana, C., Mildvan, A.S., Hajipour, G., Whitman, C.P. and Chen, L.H. Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies. Biochemistry 35 (1996) 803–813. [DOI] [PMID: 8547260]
5.  Wang, S.C., Johnson, W.H., Jr., Czerwinski, R.M., Stamps, S.L. and Whitman, C.P. Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions. Biochemistry 46 (2007) 11919–11929. [DOI] [PMID: 17902707]
6.  Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758–6768. [DOI] [PMID: 19717587]
[EC 5.3.2.6 created 2012]
 
 
EC 5.3.2.8     
Accepted name: 4-oxalomesaconate tautomerase
Reaction: (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Glossary: (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = keto tautomer of 4-oxalomesaconate
(1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate = one of the enol tautomers of 4-oxalomesaconate
Other name(s): GalD
Systematic name: 4-oxalomesaconate ketoenol-isomerase
Comments: This enzyme has been characterized from the bacterium Pseudomonas putida KT2440 and is involved in the degradation pathway of syringate and 3,4,5-trihydroxybenzoate. It catalyses the interconversion of two of the tautomers of 4-oxalomesaconate, a reaction that can also occur spontaneously.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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 5.3.2.8 created 2011 as EC 5.3.3.16, modified 2011, transferred 2012 to EC 5.3.2.8]
 
 
EC 5.3.3.4     
Accepted name: muconolactone Δ-isomerase
Reaction: (+)-muconolactone = (4,5-dihydro-5-oxofuran-2-yl)-acetate
For diagram of benzoate metabolism, click here
Glossary: (+)-muconolactone = (S)-(2,5-dihydro-5-oxofuran-2-yl)-acetate
Other name(s): muconolactone isomerase; 5-oxo-4,5-dihydrofuran-2-acetate Δ32-isomerase
Systematic name: (+)-muconolactone Δ32-isomerase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-46-0
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J. Biol. Chem. 241 (1966) 3795–3799. [PMID: 5330966]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
[EC 5.3.3.4 created 1961 as EC 3.1.1.16, part transferred 1972 to EC 5.3.3.4 rest to EC 5.3.3.4]
 
 
EC 5.3.3.10     
Accepted name: 5-carboxymethyl-2-hydroxymuconate Δ-isomerase
Reaction: 5-carboxymethyl-2-hydroxymuconate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate
Glossary: 5-carboxymethyl-2-hydroxymuconate = (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate
Other name(s): CHM isomerase; 5-carboxymethyl-2-hydroxymuconic acid isomerase
Systematic name: 5-carboxymethyl-2-hydroxymuconate Δ24-2-oxo,Δ3-isomerase
Comments: Part of the homoprotocatechuate degradation pathway in Escherichia coli C.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-05-3
References:
1.  Garrido-Pertierra, A. and Cooper, R.A. Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway of Escherichia coli. Eur. J. Biochem. 117 (1981) 581–584. [DOI] [PMID: 7026235]
2.  Johnson, W.H., Jr., Hajipour, G. and Whitman, C.P. Stereochemical studies of 5-(carboxymethyl)-2-hydroxymuconate isomerase and 5-(carboxymethyl)-2-oxo-3-hexene-1,6-dioate decarboxylase from Escherichia coli C: mechanistic and evolutionary implications. J. Am. Chem. Soc. 117 (1995) 8719–8726.
[EC 5.3.3.10 created 1984]
 
 
EC 5.3.3.16      
Transferred entry: 4-oxalomesaconate tautomerase. Now EC 5.3.2.8, 4-oxalomesaconate tautomerase
[EC 5.3.3.16 created 2011, modified 2011, deleted 2013]
 
 
EC 5.5.1.1     
Accepted name: muconate cycloisomerase
Reaction: (+)-muconolactone = cis,cis-muconate
For diagram of benzoate metabolism, click here
Glossary: (+)-muconolactone = (S)-(2,5-dihydro-5-oxofuran-2-yl)-acetate
cis,cis-muconate = cis,cis-hexadienedioate = (2Z,4Z)-hexa-2,4-dienedioate
Other name(s): muconate cycloisomerase I; cis,cis-muconate-lactonizing enzyme; cis,cis-muconate cycloisomerase; muconate lactonizing enzyme; 4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing); CatB; MCI; 2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing); 2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Systematic name: (+)-muconolactone lyase (ring-opening)
Comments: Requires Mn2+. 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 (chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-72-7
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J. Biol. Chem. 241 (1966) 3795–3799. [PMID: 5330966]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
3.  Sistrom, W.R. and Stanier, R.Y. The mechanism of formation of β-ketoadipic acid by bacteria. J. Biol. Chem. 210 (1954) 821–836. [PMID: 13211620]
[EC 5.5.1.1 created 1961]
 
 
EC 5.5.1.2     
Accepted name: 3-carboxy-cis,cis-muconate cycloisomerase
Reaction: 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = cis,cis-butadiene-1,2,4-tricarboxylate
For diagram of benzoate metabolism, click here
Other name(s): β-carboxymuconate lactonizing enzyme; 3-carboxymuconolactone hydrolase; 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
Systematic name: 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-77-8
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway. J. Biol. Chem. 241 (1966) 3787–3794. [PMID: 5916392]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
[EC 5.5.1.2 created 1972]
 
 


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