This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 5beta-cholestane-3alpha,7alpha,12alpha-triol,NADPH:oxygen oxidoreductase (26-hydroxylating). Other names in common use include 5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase, cholestanetriol 26-hydroxylase, sterol 27-hydroxylase, sterol 26-hydroxylase, cholesterol 27-hydroxylase, CYP27A, CYP27A1, and cytochrome P450 27A1'. This enzyme participates in bile acid biosynthesis and ppar signaling pathway.
Wikvall K (1984). "Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids". J. Biol. Chem. 259 (6): 3800–4. PMID6423637.
Andersson S, Davis DL, Dahlback H, Jornvall H, Russell DW (1989). "Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme". J. Biol. Chem. 264 (14): 8222–9. PMID2722778.
Furster C, Bergman T, Wikvall K (1999). "Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria". Biochem. Biophys. Res. Commun. 263 (3): 663–6. doi:10.1006/bbrc.1999.1426. PMID10512735.
Holmberg-Betsholtz I, Lund E, Bjorkhem I, Wikvall K (1993). "Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of oxidation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid". J. Biol. Chem. 268 (15): 11079–85. PMID8496170.
Pikuleva IA, Puchkaev A, Bjorkhem I (2001). "Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A1". Biochemistry. 40 (25): 7621–9. doi:10.1021/bi010193i. PMID11412116.