Cytochrome P450 family 2 subfamily C member 18 (CYP2C18)

Cytochrome P450 family 2 subfamily C member 18 (CYP2C18) is an enzyme belonging to the cytochrome P450 superfamily of heme-containing monooxygenases. It catalyzes the oxidation of diverse substrates, including drugs such as tolbutamide, warfarin, and mephenytoin, some fatty acids, retinoids, and environmental chemicals. CYP2C18 is expressed at low levels in human liver but higher in extrahepatic tissues like skin and lung. Its primary role includes drug metabolism and endogenous lipid modification, such as the formation of epoxides with signaling functions. Genetic variants of CYP2C18 exist, but functional impact is less characterized than for other CYP2C family enzymes. The enzyme contributes to individual variability in drug response and is investigationally relevant in cancer gene therapy as a prodrug-activating enzyme[1][2][5].

Other names

Cytochrome P450 2C18P450IIC17CPCICYP2CCYPIIC18Cytochrome P450-6b/29cCYP2C17 (obsolete/artefact)Mephenytoin 4-hydroxylase associated cytochrome P450EC 1.14.14.1

Monooxygenation: insertion of one atom of molecular oxygen into substrate (with electrons provided by NADPH via cytochrome P450 reductase); Drug hydroxylation (drug activation, deactivation, or detoxification); Fatty acid epoxygenation (modulating lipid signaling pathways); Prodrug activation (in cancer therapy, e.g., cyclophosphamide)