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UDP-glucuronosyltransferase 1A7 (UGT1A7) is an enzyme belonging to the UGT1 subfamily of UDP-glucuronosyltransferases, which are key phase II metabolic enzymes located primarily at the endoplasmic reticulum membrane. UGT1A7 catalyzes the conjugation of glucuronic acid to a range of small lipophilic molecules, including drugs, bilirubin, steroids, phenols, and dietary flavonoids, rendering them more water-soluble for excretion. The UGT1A7 enzyme plays a crucial role in the detoxification of xenobiotics and endogenous toxins and participates in the biotransformation of drugs such as irinotecan and mycophenolate. Genetic polymorphisms affecting UGT1A7 have been associated with interindividual variation in drug metabolism, susceptibility to certain cancers, and predisposition to adverse drug reactions, particularly severe toxicity from irinotecan treatment.
Drugs are typically inactivated/detoxified by glucuronidation catalyzed by UGT1A7. For irinotecan: inactivation of SN-38 metabolite by conjugation with glucuronic acid
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