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Literature summary for 3.3.2.12 extracted from
- Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli (2003), J. Bacteriol., 185, 5391-5397.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme additionally shows enoyl-CoA hydratase activity involved in supplying (R)-3-hydroxyacyl-CoA from the beta-oxidation pathway to polyhydroxyalkanoate biosynthetic pathway in the fadB mutant Escherichia coli strain | Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MaoC | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | a fadB maoC double-mutant strain, lacking fatty acid oxidation complex protein FadB and the enzyme, accumulates 43% less amount of medium-chain-length polyhydroxyalkanoates from fatty acid compared with the fadB mutant | Escherichia coli |
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