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UDP-glucuronosyltransferase 2B7 is a key phase II metabolic enzyme primarily expressed in the liver but also found in other tissues. It belongs to the large family of glycosyltransferases responsible for catalyzing glucuronidation reactions—conjugating glucuronic acid with a broad spectrum of endogenous substances (such as steroid hormones) and xenobiotics including many clinically used drugs. This modification increases water solubility, facilitating elimination from the body through urine or bile. The gene encoding this protein is highly polymorphic, leading to significant inter-individual differences in metabolic capacity that can impact both therapeutic outcomes and toxicity risks for various medications. Additionally, altered function has been implicated in cancer susceptibility related both directly through hormone regulation and indirectly via environmental exposures.[1][3][4]
Drugs interacting with UGT2B7 are typically subject to glucuronidation, where the enzyme catalyzes the conjugation of glucuronic acid to lipophilic substrates. This process generally leads to detoxification and increased excretion but can sometimes result in active or toxic metabolites depending on the substrate.[3]
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