The Enzyme Database

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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 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 5.5.1.1     
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]
 
 


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