Cytochrome P450 family 4 subfamily F member 2 (CYP4F2)

Cytochrome P450 family 4 subfamily F member 2 (CYP4F2) is a microsomal enzyme primarily expressed in the liver, kidney, and intestine, where it catalyzes the omega-hydroxylation of long-chain fatty acids, eicosanoids, and vitamins including vitamin K and vitamin E. Functionally, CYP4F2 initiates the inactivation and breakdown of leukotriene B4, a key inflammatory mediator, and produces 20-hydroxyeicosatetraenoic acid (20-HETE), an important regulator of vascular tone and sodium excretion. Genetic variants in CYP4F2 significantly affect the pharmacokinetics of vitamin K and the dosing of warfarin and related anticoagulants; the most prominent variant, CYP4F2*3 (V433M), exhibits reduced enzymatic activity, resulting in higher hepatic vitamin K levels and increased anticoagulant dose requirements. CYP4F2 activity also modulates vitamin E status, response to drugs such as imatinib and fingolimod, and may influence susceptibility to cardiovascular disease, cancer, and inflammation through its impact on lipid mediator profiles.

Other names

Cytochrome P450 4F220-HETE synthase20-hydroxyeicosatetraenoic acid synthaseArachidonic acid omega-hydroxylaseDocosahexaenoic acid omega-hydroxylaseLeukotriene-B4 20-monooxygenase 1Leukotriene-B4 omega-hydroxylase 1Phylloquinone omega-hydroxylase CYP4F2CYPIVF2Cytochrome P450-LTB-omegaCPF2

CYP4F2 oxidizes vitamin K1 and other lipid substrates, influencing their bioavailability and catabolic rate. Pharmacologic inhibition/modulation alters drug clearance and endogenous mediator levels.