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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap
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5beta-cholestan-3alpha, 7alpha, 26-triol is oxidized to 3alpha, 7alpha-dihydroxy-5beta-cholestan-26-al

5beta-cholestan-3alpha,7alpha,26-triol + NADP+ → 3alpha,7alpha-dihydroxy-5beta-cholestan-26-al + H+ + NADPH

Reactome
R-HSA-193497
Compartment
mitochondrial matrix
Rhea
None recorded

Inputs

  • 5beta-cholestan-3alpha,7alpha,26-triolCHEBI:28540, C27H48O3, mitochondrial matrix
  • NADP+CHEBI:58349, C21H25N7O17P3, mitochondrial matrix

Outputs

  • 3alpha,7alpha-dihydroxy-5beta-cholestan-26-alCHEBI:27428, C27H46O3, mitochondrial matrix
  • H+CHEBI:15378, H, mitochondrial matrix
  • NADPHCHEBI:57783, C21H26N7O17P3, mitochondrial matrix

Catalysed by

  • oxidoreductase activity, acting on NAD(P)H as acceptor of CYP27A1 [mitochondrial matrix]EC 1.6.1; UniProt Q02318

Literature

  1. Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. J Biol Chem, 1991
  2. Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways J Biol Chem, 1998