| EC |
4.2.1.74 |
| Accepted name: |
medium-chain-enoyl-CoA hydratase |
| Reaction: |
a medium-chain (3S)-3-hydroxyacyl-CoA = a medium-chain trans-2-enoyl-CoA + H2O |
| Glossary: |
a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms. |
| Other name(s): |
long-chain enoyl coenzyme A hydratase (incorrect); long-chain-enoyl-CoA hydratase (incorrect); long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase (incorrect) |
| Systematic name: |
medium-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase |
| Comments: |
Acts in the reverse direction. The best substrate for the porcine enzyme is oct-2-enoyl-CoA. Unlike EC 4.2.1.17 enoyl-CoA hydratase, it does not act on crotonoyl-CoA. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 62009-81-8 |
| References: |
| 1. |
Fong, J.C. and Schulz, H. Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues. J. Biol. Chem. 252 (1977) 542–547. [PMID: 833142] |
| 2. |
Schulz, H. Long chain enoyl coenzyme A hydratase from pig heart. J. Biol. Chem. 249 (1974) 2704–2709. [PMID: 4828315] |
| 3. |
Arent, S., Christensen, C.E., Pye, V.E., Norgaard, A. and Henriksen, A. The multifunctional protein in peroxisomal β-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2. J. Biol. Chem. 285 (2010) 24066–24077. [DOI] [PMID: 20463021] |
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| [EC 4.2.1.74 created 1981, modified 2022] |
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