Cytochrome P450 family 4 subfamily F (CYP4F) (CYP4F)

Cytochrome P450 family 4 subfamily F (CYP4F) consists of a group of heme-thiolate enzymes that play a pivotal role in the omega-oxidation of endogenous lipids, including long-chain fatty acids and eicosanoids [UniProt: P98187, Q08477]. A primary function of this subfamily, particularly CYP4F2 and CYP4F3, is the metabolic inactivation of leukotriene B4 (LTB4), a potent mediator of inflammation, thereby helping to resolve inflammatory responses [PubMed: 10744681]. CYP4F2 is also recognized as the major enzyme responsible for the omega-hydroxylation of vitamin K1 and vitamin E (tocopherols), which regulates their systemic levels and influences blood coagulation [PubMed: 18305455, 24523444]. In clinical pharmacology, genetic polymorphisms in CYP4F2, such as the V433M variant, are significant determinants of warfarin dose requirements due to their effect on vitamin K metabolism [PharmGKB: PA128]. Furthermore, CYP4F enzymes are involved in the metabolism of certain therapeutic agents, including the immunomodulator fingolimod and the antihistamine ebastine [PubMed: 23934134, 11773031]. Consequently, the CYP4F subfamily is a critical factor in both lipid homeostasis and the personalized management of cardiovascular and inflammatory diseases [NCBI Gene: 8529].

Other names

CYP4F subfamilyLeukotriene B4 omega-hydroxylaseFatty acid omega-hydroxylaseVitamin K1 hydroxylase

Catalyzes the omega-hydroxylation of medium- and long-chain fatty acids, eicosanoids, and fat-soluble vitamins, facilitating their degradation and excretion [UniProt: P98187].