Uridine diphosphate glucuronosyltransferase (UGT)

Uridine diphosphate glucuronosyltransferase (UGT) refers to a superfamily of membrane-bound enzymes localized primarily in the endoplasmic reticulum that catalyze the covalent addition of glucuronic acid from UDP-glucuronic acid to a broad range of endogenous and exogenous lipophilic substrates, such as drugs, hormones, bilirubin, and environmental toxins[1][3][7]. This conjugation, known as glucuronidation, is a principal Phase II metabolic pathway which increases the solubility of substrates, facilitating their excretion in bile or urine and thereby contributing critically to detoxification and drug clearance in the body[2][3][6]. There are multiple UGT isoforms (notably in the UGT1 and UGT2 families), each with somewhat distinct substrate selectivity, and deficiencies in specific isoforms (e.g., UGT1A1) can cause severe metabolic disorders such as unconjugated hyperbilirubinemia[1][7]. UGT enzymes are known targets for drug interactions, with their activity modifiable by genetic polymorphisms or concurrent medication, making them important biomarkers and determinants of drug safety and efficacy[5][7].

Other names

UDP-glucuronosyltransferaseUDPGTglucuronosyltransferaseUDP-glucuronyl transferaseUGT enzymeUDP-GT[3]

Drug inactivation via glucuronidation, Increased drug solubility and excretion, Regulation of plasma concentrations of drugs and endogenous compounds, Prevention of drug toxicity[2][5][7]