UDP-glucuronosyltransferase 1-9 and UDP-glucuronosyltransferase 2B7 (UGT1A9 and UGT2B7)

UDP-glucuronosyltransferase 1-9 (UGT1A9) and UDP-glucuronosyltransferase 2B7 (UGT2B7) are major phase II drug-metabolizing enzymes that play a pivotal role in the detoxification and elimination of a wide range of xenobiotics and endogenous compounds [1, 11]. These enzymes are primarily expressed in the liver and kidneys, where they catalyze the glucuronidation reaction—the transfer of a glucuronic acid moiety from UDP-glucuronic acid to lipophilic substrates to enhance their water solubility for excretion [1, 6]. UGT1A9 and UGT2B7 are often studied together because they exhibit overlapping substrate specificities and have been shown to form functional heterodimers that modulate their individual catalytic activities [8, 9]. They are responsible for the metabolism of several clinically significant drugs, including the anesthetic propofol, the immunosuppressant mycophenolic acid, and the analgesic morphine [1, 4, 13]. Genetic polymorphisms in the genes encoding these enzymes, such as UGT1A9*3 and UGT2B7*2, are critical biomarkers that contribute to inter-individual variability in drug response and the risk of adverse drug reactions [2, 5, 12]. Consequently, these enzymes are essential considerations in pharmacogenomics, drug-drug interaction assessments, and the development of personalized therapeutic strategies [14, 15].

Other names

UGT1A9UGT2B7UDP-glucuronosyltransferase 1A9UDP-glucuronosyltransferase 2B7UDPGTUDP-glycosyltransferase

Drugs typically interact with these enzymes as substrates for glucuronidation, which facilitates their metabolic inactivation and elimination. Some drugs may also act as inhibitors or inducers, altering the metabolism of co-administered medications [1, 16, 17].