UDP-glucuronosyltransferase family 1 member A3 (UGT1A3)

UDP-glucuronosyltransferase family 1 member A3 (UGT1A3) is an enzyme responsible for catalyzing phase II glucuronidation reactions, transforming lipophilic endogenous and exogenous molecules—including steroids, hormones, bilirubin, bile acids, and many drugs—into water-soluble metabolites suitable for excretion in urine or bile. UGT1A3 is one of several related enzymes arising from alternative splicing at the UGT1 locus, each exhibiting slightly different substrate preferences but sharing a common role in drug detoxification and homeostatic metabolism. Human diseases associated with UGT1A3 include hyperbilirubinemia and drug response variability, largely due to genetic differences in enzyme expression and activity. UGT1A3 interacts with several clinically relevant drugs including ezetimibe and angiotensin II receptor antagonists, and its activity is subject to regulation by nuclear receptors and genetic polymorphisms, thereby influencing individual drug responses and safety profiles[1][2][3][4].

Other names

UDP-glucuronosyltransferase 1A3GNT1UGT1UDPGT 1-3UGT1*3UGT1-03UGT1.3UGT-1CUGT1CUDP-glucuronosyltransferase 1-3UDP-glucuronosyltransferase 1-CUDP-glucuronosyltransferase 1A isoform 3UDPGTUGT1A3SUDP-glucuronosyltransferase 1 family polypeptide A3UDP glycosyltransferase 1 family polypeptide A3

Drugs targeting this enzyme may be substrates for glucuronidation, leading to their inactivation or facilitation of excretion. Conversely, drugs can act as inhibitors or inducers of UGT1A3, thereby altering the metabolism rates of other substrates. The primary mechanism involves glucuronidation, which increases drug water solubility and promotes excretion.