| EC |
4.2.1.149 |
| Accepted name: |
crotonobetainyl-CoA hydratase |
| Reaction: |
L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O |
| Glossary: |
L-carnitinyl-CoA = (3R)-3-hydroxy-4-(trimethylammonio)butanoyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA = crotonobetainyl-CoA |
| Other name(s): |
CaiD; L-carnityl-CoA dehydratase |
| Systematic name: |
L-carnitinyl-CoA hydro-lyase [(E)-4-(trimethylammonio)but-2-enoyl-CoA-forming] |
| Comments: |
The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency [2]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545] |
| 2. |
Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212] |
| 3. |
Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894] |
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| [EC 4.2.1.149 created 2014] |
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