5beta-cholestan-3alpha,7alpha,24(S),27-tetrol is oxidized to 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-al
5bCHOL3a,7a,24(s),27-tetrol + O2 + NADPH + H+ → 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-al + H2O + NADP+
- Reactome
- R-HSA-193719
- Compartment
- mitochondrial matrix
- Rhea
- None recorded
Inputs
- 5bCHOL3a,7a,24(s),27-tetrolCHEBI:63833, C27H48O4, mitochondrial matrix
- O2CHEBI:15379, O2, mitochondrial matrix
- NADPHCHEBI:57783, C21H26N7O17P3, mitochondrial matrix
- H+CHEBI:15378, H, mitochondrial matrix
Outputs
- 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-alCHEBI:63848, C27H46O4, 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
- Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways J Biol Chem, 1998