Rat Cytochrome P450 1A2, CYP1A2 ELI

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins.

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).

Catalyzes the hydroxylation of carbon-hydrogen bonds.

Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2.

Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis.

May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver.

Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid.

Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer.

Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA.

May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Plays a role in the oxidative metabolism of xenobiotics.

Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin.

Metabolizes caffeine via N3-demethylation.