Uridine diphosphate-glucuronosyltransferase (UGT) (UGT)

Uridine diphosphate-glucuronosyltransferases (UGTs) are a superfamily of membrane-bound enzymes primarily located in the endoplasmic reticulum of the liver, but also present in the kidneys, gastrointestinal tract, and other tissues (Meech et al., 2019). They play a critical role in Phase II metabolism by catalyzing the glucuronidation process, which involves the transfer of glucuronic acid from UDP-glucuronic acid to various endogenous and exogenous lipophilic compounds (Rowland et al., 2013). This conjugation increases the water solubility of substrates, such as bilirubin, steroid hormones, and numerous drugs, facilitating their elimination via bile or urine (Guillemette, 2003). Genetic variations in UGT genes, particularly UGT1A1, are clinically significant as they can lead to impaired metabolism of drugs like irinotecan, resulting in severe toxicity (StatPearls, 2023). Furthermore, UGTs are involved in the detoxification of environmental carcinogens, and their activity is a major determinant of drug pharmacokinetics and potential drug-drug interactions (PubMed, 2021). Understanding the specific isoforms, such as UGT1A1 and UGT2B7, is essential for predicting drug safety and efficacy in clinical settings (UniProt, 2023).

Other names

UDP-glucuronosyltransferaseGlucuronosyltransferaseUDPGTUDP-GTGlucuronyltransferase

UGTs catalyze the transfer of the glucuronic acid moiety from uridine diphosphate glucuronic acid (UDPGA) to nucleophilic functional groups of various lipophilic substrates, converting them into water-soluble glucuronides for biliary or renal excretion (Meech et al., 2019; Rowland et al., 2013).