Cytochrome P450 family 2 subfamily C (CYP2C) (CYP2C)

The Cytochrome P450 family 2 subfamily C (CYP2C) is a group of heme-thiolate enzymes primarily located in the liver's endoplasmic reticulum, responsible for the Phase I metabolism of approximately 20% of clinically prescribed drugs (Source: NCBI, PMID: 15970797). In humans, this subfamily consists of four members—CYP2C8, CYP2C9, CYP2C18, and CYP2C19—which catalyze the oxidation of a broad range of substrates, including anticoagulants, anticonvulsants, and proton pump inhibitors (Source: UniProt). A hallmark of the CYP2C subfamily is its significant genetic polymorphism, particularly in CYP2C9 and CYP2C19, which results in substantial inter-individual variability in drug clearance and clinical response (Source: PharmGKB). This variability is a major factor in drug-drug interactions and adverse drug reactions, especially for medications with narrow therapeutic windows like warfarin and phenytoin (Source: FDA). Beyond drug metabolism, CYP2C enzymes also play a role in endogenous physiology by converting arachidonic acid into epoxyeicosatrienoic acids (EETs), which are involved in regulating vascular tone and inflammation (Source: PubMed, PMID: 21172311).

Other names

CYP2C subfamilyCytochrome P450 2CMicrosomal monooxygenaseCYP2C cluster

CYP2C enzymes act as monooxygenases that catalyze the Phase I oxidative metabolism of drugs. Drugs can serve as substrates, which are chemically modified for excretion; inhibitors, which decrease enzyme activity and lead to potential toxicity of co-administered drugs; or inducers, which increase enzyme expression and may lead to therapeutic failure of co-administered drugs (Source: StatPearls, UniProt).