ENZYME entry: EC 1.14.15.15
Accepted Name |
cholestanetriol 26-monooxygenase.
|
Alternative Name(s) |
5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase. |
5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase. |
cholestanetriol 26-hydroxylase. |
cholesterol 27-hydroxylase. |
cytochrome P450 27A1'. |
sterol 26-hydroxylase. |
sterol 27-hydroxylase. |
vitamin D3 25-hydroxylase. |
Reaction catalysed |
5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 + 6 reduced [adrenodoxin] <=> (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin] |
Comment(s) |
- Catalyzes the first three sterol side chain oxidations in bile acid
biosynthesis via the neutral (classic) pathway.
- Can also act on cholesterol, cholest-5-en-3beta,7alpha-diol, 7alpha-
hydroxycholest-4-en-3-one, and 5beta-cholestane-3alpha,7alpha-diol.
- The enzyme can also hydroxylate cholesterol at positions 24 and 25.
- The initial source of the electrons is NADPH, which transfers the
electrons to the adrenodoxin via EC 1.18.1.6.
- Formerly EC 1.14.13.15.
|
Cross-references |
BRENDA | 1.14.15.15 |
EC2PDB | 1.14.15.15 |
ExplorEnz | 1.14.15.15 |
PRIAM enzyme-specific profiles | 1.14.15.15 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.15.15 |
IUBMB Enzyme Nomenclature | 1.14.15.15 |
IntEnz | 1.14.15.15 |
MEDLINE | Find literature relating to 1.14.15.15 |
MetaCyc | 1.14.15.15 |
Rhea expert-curated reactions | 1.14.15.15 |
UniProtKB/Swiss-Prot |
|
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