CYP27A1 27-hydroxylates 5bCHOL3a,7a,12a-triol
5bCHOL3a,7a,12a-triol + NADPH + H+ + O2 → 5bCHOL3a,7a,12a,27-tetrol + H2O + NADP+
- Reactome
- R-HSA-191999
- Compartment
- mitochondrial matrix
- Rhea
- None recorded
Inputs
- 5bCHOL3a,7a,12a-triolCHEBI:16496, C27H48O3, mitochondrial matrix
- NADPHCHEBI:57783, C21H26N7O17P3, mitochondrial matrix
- H+CHEBI:15378, H, mitochondrial matrix
- O2CHEBI:15379, O2, mitochondrial matrix
Outputs
- 5bCHOL3a,7a,12a,27-tetrolCHEBI:17278, C27H48O4, mitochondrial matrix
- H2OCHEBI:15377, H2O, mitochondrial matrix
- NADP+CHEBI:58349, C21H25N7O17P3, mitochondrial matrix
Catalysed by
- oxidoreductase activity, acting on NAD(P)H as acceptor of CYP27A1 [mitochondrial matrix]EC 1.6.1; UniProt Q02318
Literature
- Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. J Biol Chem, 1991
- Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis J Biol Chem, 1991
- Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways J Biol Chem, 1998