| EC |
4.2.1.157 |
| Accepted name: |
(R)-2-hydroxyisocaproyl-CoA dehydratase |
| Reaction: |
(R)-2-hydroxy-4-methylpentanoyl-CoA = 4-methylpent-2-enoyl-CoA + H2O |
| Other name(s): |
2-hydroxyisocaproyl-CoA dehydratase; HadBC |
| Systematic name: |
(R)-2-hydroxy-4-methylpentanoyl-CoA hydro-lyase |
| Comments: |
The enzyme, isolated from the bacterium Peptoclostridium difficile, is involved in the reductive branch of L-leucine fermentation. It catalyses an α/β-dehydration, which depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Kim, J., Darley, D. and Buckel, W. 2-Hydroxyisocaproyl-CoA dehydratase and its activator from Clostridium difficile. FEBS J. 272 (2005) 550–561. [DOI] [PMID: 15654892] |
| 2. |
Knauer, S.H., Buckel, W. and Dobbek, H. Structural basis for reductive radical formation and electron recycling in (R)-2-hydroxyisocaproyl-CoA dehydratase. J. Am. Chem. Soc. 133 (2011) 4342–4347. [DOI] [PMID: 21366233] |
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| [EC 4.2.1.157 created 2015] |
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