A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 1.17.99.3
| Accepted Name |
|---|
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA
24-hydroxylase.
|
| Alternative Name(s) |
|---|
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate
24-hydroxylase. |
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase. |
| THC-CoA oxidase. |
| THCA-CoA oxidase. |
| Trihydroxycoprostanoyl-CoA oxidase. |
| Reaction catalysed |
|---|
| (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oyl-CoA + H(2)O + acceptor <=> (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestan-26-oyl-CoA + reduced acceptor |
| Comment(s) |
|---|
- Requires ATP.
- The reaction in mammals possibly involves dehydrogenation to give a
24(25)-double bond followed by hydration.
- However, in amphibians such as the Oriental fire-bellied toad
(Bombina orientalis), it is probable that the product is formed via
direct hydroxylation of the saturated side chain of (25R)-3-alpha,7-
alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate and not via
hydration of a 24(25) double bond.
- In microsomes, the free acid is preferred to the coenzyme A ester,
whereas in mitochondria, the coenzyme A ester is preferred to the
free-acid form of the substrate.
|
| Cross-references |
|---|
| BRENDA | 1.17.99.3 |
| EC2PDB | 1.17.99.3 |
| ExplorEnz | 1.17.99.3 |
| PRIAM enzyme-specific profiles | 1.17.99.3 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.17.99.3 |
| IUBMB Enzyme Nomenclature | 1.17.99.3 |
| IntEnz | 1.17.99.3 |
| MEDLINE | Find literature relating to 1.17.99.3 |
| MetaCyc | 1.17.99.3 |
| UniProtKB/Swiss-Prot |
|
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