EC |
4.1.2.44 |
Accepted name: |
2,3-epoxybenzoyl-CoA dihydrolase |
Reaction: |
2,3-epoxy-2,3-dihydrobenzoyl-CoA + 2 H2O = (3Z)-6-oxohex-3-enoyl-CoA + formate |
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For diagram of Benzoyl-CoA catabolism, click here |
Glossary: |
(3Z)-6-oxohex-3-enoyl-CoA = 3,4-didehydroadipyl-CoA semialdehyde |
Other name(s): |
2,3-dihydro-2,3-dihydroxybenzoyl-CoA lyase/hydrolase (deformylating); BoxC; dihydrodiol transforming enzyme; benzoyl-CoA oxidation component C; 2,3-dihydro-2,3-dihydroxybenzoyl-CoA 3,4-didehydroadipyl-CoA semialdehyde-lyase (formate-forming); benzoyl-CoA-dihydrodiol lyase (incorrect); 2,3-dihydro-2,3-dihydroxybenzoyl-CoA 3,4-didehydroadipyl-CoA-semialdehyde-lyase (formate-forming) |
Systematic name: |
2,3-epoxy-2,3-dihydrobenzoyl-CoA (3Z)-6-oxohex-3-enoyl-CoA-lyase (formate-forming) |
Comments: |
The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii. The enzyme converts 2,3-epoxy-2,3-dihydrobenzoyl-CoA to its oxepin form prior to the ring-opening and the formation of a dialdehyde intermediate. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc |
References: |
1. |
Gescher, J., Eisenreich, W., Worth, J., Bacher, A. and Fuchs, G. Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme. Mol. Microbiol. 56 (2005) 1586–1600. [DOI] [PMID: 15916608] |
2. |
Rather, L.J., Knapp, B., Haehnel, W. and Fuchs, G. Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation. J. Biol. Chem. 285 (2010) 20615–20624. [DOI] [PMID: 20452977] |
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[EC 4.1.2.44 created 2010, modified 2015] |
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