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ENZYME entry: EC 1.14.15.15

Accepted Name
Cholestanetriol 26-monooxygenase.
Alternative Name(s)
5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase.
5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol hydroxylase.
Cholestanetriol 26-hydroxylase.
Cholesterol 27-hydroxylase.
Cytochrome P450 27A1'.
Sterol 26-hydroxylase.
Sterol 27-hydroxylase.
Vitamin D(3) 25-hydroxylase.
Reaction catalysed
5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + 6 reduced adrenodoxin + 6 H(+) + 3 O(2) <=> (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + 6 oxidized adrenodoxin + 4 H(2)O
Cofactor(s)
Heme-thiolate.
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-3-beta,7-alpha-diol, 7-alpha-hydroxycholest-4-en-3-one, and 5-beta-cholestane-3-alpha,7- alpha-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
PROSITEPDOC00081
BRENDA1.14.15.15
EC2PDB1.14.15.15
ExplorEnz1.14.15.15
PRIAM enzyme-specific profiles1.14.15.15
KEGG Ligand Database for Enzyme Nomenclature1.14.15.15
IUBMB Enzyme Nomenclature1.14.15.15
IntEnz1.14.15.15
MEDLINEFind literature relating to 1.14.15.15
MetaCyc1.14.15.15
Rhea expert-curated reactions1.14.15.15
UniProtKB/Swiss-Prot
Q02318, CP27A_HUMAN;  Q9DBG1, CP27A_MOUSE;  P17177, CP27A_RABIT;  
P17178, CP27A_RAT;  C4B644, CPVDH_PSEAH;  

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