5beta-cholestan-3alpha,7alpha,12alpha,27-tetrol is oxidized to 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al
5bCHOL3a,7a,12a,27-tetrol + NADP+ → 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al + NADPH + H+
- Reactome
- R-HSA-192042
- Compartment
- mitochondrial matrix
- Rhea
- None recorded
Inputs
- 5bCHOL3a,7a,12a,27-tetrolCHEBI:17278, C27H48O4, mitochondrial matrix
- NADP+CHEBI:58349, C21H25N7O17P3, mitochondrial matrix
Outputs
- 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alCHEBI:16466, C27H46O4, mitochondrial matrix
- NADPHCHEBI:57783, C21H26N7O17P3, mitochondrial matrix
- H+CHEBI:15378, H, 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
- Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways J Biol Chem, 1998