Cytochrome P450 family 27 subfamily C member 1 (CYP27C1)

Cytochrome P450 family 27 subfamily C member 1 (CYP27C1) is a member of the cytochrome P450 superfamily of monooxygenase enzymes, primarily functioning as an all-trans-retinol 3,4-desaturase. It catalyzes the conversion of vitamin A1 (all-trans-retinol) to vitamin A2 (all-trans-3,4-dehydroretinal), playing a critical role in retinoid metabolism. CYP27C1 is expressed in human skin epidermis and is notable among mammalian P450 enzymes for mediating a desaturation reaction rather than typical hydroxylation. It also has minor hydroxylation activity. This enzyme contributes to drug metabolism, lipid biosynthesis, and may negatively regulate lung cancer cell proliferation through IGF-1R/Akt/p53 signaling. Clinical relevance includes associations with disorders of vitamin A deficiency and potential roles in cancer biology. CYP27C1 can also metabolize certain chemotherapeutics (e.g., vinorelbine) and is inhibited by drugs such as ketoconazole in laboratory assays[1][3][5].

Other names

all-trans-retinol 3,4-desaturaseP450 27C1

Substrate oxidation/desaturation (conversion of all-trans-retinol to all-trans-3,4-dehydroretinol through desaturation); drug metabolism via retinoid modification