A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids (PubMed:
7574697, PubMed:
9866708, PubMed:
9435160, PubMed:
12865317, PubMed:
15766564, PubMed:
19965576, PubMed:
21576599). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:
7574697, PubMed:
9866708, PubMed:
9435160, PubMed:
12865317, PubMed:
15766564, PubMed:
19965576, PubMed:
21576599). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) (PubMed:
7574697, PubMed:
15766564, PubMed:
19965576, PubMed:
9866708). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:
21576599). Exhibits low catalytic activity for the formation of catechol estrogens from 17beta- estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2 (PubMed:
12865317). Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA) (PubMed:
9866708, PubMed:
9435160). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol (PubMed:
11950794). Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan (PubMed:
25994031).
