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] |
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|
|
|
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] |
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|
|
|
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] |
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|
|
|
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] |
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|
|
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] |
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|
|
|
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] |
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|
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] |
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[EC 1.14.13.82 created 2000 as EC 1.2.3.12, transferred 2003 to EC 1.14.13.82] |
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|
|
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] |
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|
|
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] |
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[EC 2.1.1.341 created 2017] |
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|
|
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] |
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[EC 2.8.3.6 created 1961] |
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|
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] |
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|
|
|
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] |
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|
|
|
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] |
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|
|
|
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] |
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|
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] |
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[EC 4.2.1.83 created 1986, modified 2011] |
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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] |
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[EC 4.2.1.118 created 2009] |
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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] |
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[EC 4.2.1.163 created 2016] |
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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 keto—enol 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] |
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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 keto—enol-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] |
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[EC 5.3.2.8 created 2011 as EC 5.3.3.16, modified 2011, transferred 2012 to EC 5.3.2.8] |
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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 Δ3-Δ2-isomerase |
Systematic name: |
(+)-muconolactone Δ3-Δ2-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. |
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[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] |
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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 Δ2,Δ4-2-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. |
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[EC 5.3.3.10 created 1984] |
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EC
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5.3.3.16
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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] |
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|
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] |
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[EC 5.5.1.1 created 1961] |
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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. |
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[EC 5.5.1.2 created 1972] |
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