Uridine 5′-diphospho-glucuronosyltransferase (UGT)

Uridine 5′-diphospho-glucuronosyltransferases (UGTs) are a superfamily of membrane-bound Phase II drug-metabolizing enzymes primarily located in the endoplasmic reticulum of the liver, kidneys, and intestines [6, 15]. They catalyze the glucuronidation reaction, which involves the transfer of a glucuronic acid moiety from UDP-glucuronic acid to a wide range of endogenous and exogenous lipophilic substrates, including bilirubin, steroid hormones, and therapeutic drugs [9, 14]. This process increases the water solubility of these compounds, facilitating their excretion via bile or urine [17, 19]. UGTs play a critical role in detoxification and the maintenance of metabolic homeostasis [12, 16]. Genetic polymorphisms in UGT genes, such as the UGT1A1*28 variant, are clinically significant as they can lead to impaired drug metabolism and increased risk of severe toxicities, notably with the anticancer drug irinotecan [1, 4, 20]. Furthermore, UGTs are involved in numerous drug-drug interactions where inhibitors or inducers alter the clearance of co-administered medications [2, 10].

Other names

UDP-glucuronosyltransferaseUDPGTGlucuronosyltransferaseUDP-glycosyltransferaseUridine diphosphate glucuronosyltransferase

UGTs catalyze the transfer of a glucuronic acid group from uridine diphosphate glucuronic acid (UDPGA) to a substrate, a process known as glucuronidation, which increases the substrate's hydrophilicity and facilitates its excretion [6, 15, 17].