Cytochrome P450 family 2 subfamily C (CYP2C)

The Cytochrome P450 family 2 subfamily C (CYP2C) consists of a group of heme-containing enzymes primarily localized in the endoplasmic reticulum of hepatocytes. In humans, this subfamily includes four functional members—CYP2C8, CYP2C9, CYP2C18, and CYP2C19—which are responsible for the Phase I metabolism of approximately 20-25% of all clinically prescribed drugs (Source: PubMed, PMID: 24591667). These enzymes catalyze essential oxidative reactions, such as the hydroxylation of NSAIDs and the bioactivation of the antiplatelet prodrug clopidogrel. Beyond xenobiotic clearance, CYP2C enzymes also play a role in endogenous metabolism, particularly in the conversion of arachidonic acid to epoxyeicosatrienoic acids (EETs), which influence vascular tone and inflammation (Source: UniProt P11712, P33261). The CYP2C family is highly clinically significant due to extensive genetic polymorphisms that result in distinct phenotypes: poor, intermediate, normal, and ultrarapid metabolizers. For example, variants in CYP2C9 significantly alter the required dosage of the anticoagulant warfarin, where poor metabolizers face a high risk of life-threatening hemorrhage (Source: FDA Table of Pharmacogenetic Associations). Similarly, loss-of-function alleles in CYP2C19 are associated with reduced active metabolite levels of clopidogrel, leading to increased risks of stent thrombosis and myocardial infarction (Source: PharmGKB). Because of this high variability and the potential for significant drug-drug interactions, the CYP2C family is a primary focus of pharmacogenomic testing and personalized medicine strategies in clinical practice.

Other names

CYP2C subfamilyCytochrome P450 2C clusterCYP2C isozymesS-mephenytoin 4'-hydroxylase familyMicrosomal monooxygenase family 2C

Catalyzes the oxidative metabolism (primarily hydroxylation and dealkylation) of lipophilic substrates to facilitate biliary or renal excretion, or to bioactivate prodrugs into active metabolites.