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 1.2.1.45      
Transferred entry: 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase. Now EC 1.1.1.312, 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase.
[EC 1.2.1.45 created 1978, deleted 2011]
 
 
EC 1.13.11.1     
Accepted name: catechol 1,2-dioxygenase
Reaction: catechol + O2 = cis,cis-muconate
For diagram of benzoate metabolism, click here
Other name(s): catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II
Systematic name: catechol:oxygen 1,2-oxidoreductase
Comments: Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9027-16-1
References:
1.  Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 353–371.
2.  Hayaishi, O., Katagiri, M. and Rothberg, S. Studies on oxygenases: pyrocatechase. J. Biol. Chem. 229 (1957) 905–920. [PMID: 13502352]
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]
4.  Zeyer, J., Kocher, H.P. and Timmis, N. Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334–339. [PMID: 3752997]
[EC 1.13.11.1 created 1961 as EC 1.99.2.2, transferred 1965 to EC 1.13.1.1, transferred 1972 to EC 1.13.11.1]
 
 
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 1.13.11.22     
Accepted name: caffeate 3,4-dioxygenase
Reaction: 3,4-dihydroxy-trans-cinnamate + O2 = 3-(2-carboxyethenyl)-cis,cis-muconate
Other name(s): 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-61-4
References:
1.  Seidman, M.M., Toms, A. and Wood, J.M. Influence of side-chain substituents on the position of cleavage of the benzene ring by Pseudomonas fluorescens. J. Bacteriol. 97 (1969) 1192–1197. [PMID: 5776526]
[EC 1.13.11.22 created 1972]
 
 
EC 1.13.11.28     
Accepted name: 2,3-dihydroxybenzoate 2,3-dioxygenase
Reaction: 2,3-dihydroxybenzoate + O2 = 2-carboxy-cis,cis-muconate
Other name(s): 2,3-dihydroxybenzoate 2,3-oxygenase; 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Also acts, more slowly, with 2,3-dihydroxy-4-methylbenzoate and 2,3-dihydroxy-4-isopropylbenzoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56802-97-2
References:
1.  La Du, B.N. and Zannoni, V.G. The tyrosine oxidation system of liver. III. Further studies on the oxidation of p-hydroxyphenylpyruvic acid. J. Biol. Chem. 219 (1956) 273–281. [PMID: 13295279]
2.  Sharma, H.K. and Vaidyanathan, C.S. A new mode of ring cleavage of 2,3-dihydroxybenzoic acid in Tecoma stans (L.). Partial purification and properties of 2,3-dihydroxybenzoate 2,3-oxygenase. Eur. J. Biochem. 56 (1975) 163–171. [DOI] [PMID: 1175620]
[EC 1.13.11.28 created 1978]
 
 
EC 1.13.11.29     
Accepted name: stizolobate synthase
Reaction: L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase (recyclizing)
Comments: The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobic acid. The enzyme requires Zn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65979-39-7
References:
1.  Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237–243. [DOI] [PMID: 9285]
2.  Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385–392. [DOI] [PMID: 624278]
[EC 1.13.11.29 created 1978]
 
 
EC 1.13.11.30     
Accepted name: stizolobinate synthase
Reaction: L-dopa + O2 = 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen 2,3-oxidoreductase (recyclizing)
Comments: The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobinic acid. The enzyme requires Zn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65979-38-6
References:
1.  Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237–243. [DOI] [PMID: 9285]
2.  Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385–392. [DOI] [PMID: 624278]
[EC 1.13.11.30 created 1978]
 
 
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, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, 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]
 
 
EC 5.5.1.5     
Accepted name: carboxy-cis,cis-muconate cyclase
Reaction: 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate
For diagram of reaction, click here
Other name(s): 3-carboxymuconate cyclase; 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
Systematic name: 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-55-1
References:
1.  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]
[EC 5.5.1.5 created 1972]
 
 
EC 5.5.1.7     
Accepted name: chloromuconate cycloisomerase
Reaction: (2R)-2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate
For diagram of reaction, click here
Glossary: (2R)-2-chloro-2,5-dihydro-5-oxofuran-2-acetate = (+)-4-chloromuconolactone
3-chloro-cis,cis-muconate = (2E,4Z)-3-chlorohexa-2,4-dienedioate
Other name(s): muconate cycloisomerase II; 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing); 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Systematic name: (2R)-2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Comments: Requires Mn2+. The product of cycloisomerization of 3-chloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylenebut-2-en-4-olide. Also acts on 2-chloro-cis,cis-muconate. Not identical with EC 5.5.1.1 (muconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 95990-33-3
References:
1.  Schmidt, E. and Knackmuss, H.-J. Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid. Biochem. J. 192 (1980) 339–347. [PMID: 7305906]
2.  Kaulmann, U., Kaschabek, S.R. and Schlomann, M. Mechanism of chloride elimination from 3-chloro- and 2,4-dichloro-cis,cis-muconate: new insight obtained from analysis of muconate cycloisomerase variant CatB-K169A. J. Bacteriol. 183 (2001) 4551–4561. [DOI] [PMID: 11443090]
3.  Kajander, T., Lehtio, L., Schlomann, M. and Goldman, A. The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function. Protein Sci. 12 (2003) 1855–1864. [DOI] [PMID: 12930985]
[EC 5.5.1.7 created 1983]
 
 
EC 5.5.1.11     
Accepted name: dichloromuconate cycloisomerase
Reaction: 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate = 2,4-dichloro-cis,cis-muconate
For diagram of reaction, click here
Other name(s): 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
Systematic name: 2,4-dichloro-2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Comments: Requires Mn2+. The product of cycloisomerization of dichloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylene-3-chlorobut-2-en-4-olide. Also acts, in the reverse direction, on cis,cis-muconate and its monochloro-derivatives, but with lower affinity. Not identical with EC 5.5.1.1 (muconate cycloisomerase) or EC 5.5.1.7 (chloromuconate cycloisomerase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 126904-95-8
References:
1.  Kuhm, A.E., Schlömann, M., Knackmuss, H.-J. and Pieper, D.H. Purification and characterization of dichloromuconate cycloisomerase from Alcaligenes eutrophus JMP 134. Biochem. J. 266 (1990) 877–883. [PMID: 2327971]
[EC 5.5.1.11 created 1992]
 
 


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