UDP-glucuronosyltransferase 2A2 (UGT2A2)

UDP-glucuronosyltransferase 2A2 (UGT2A2) is a membrane-bound enzyme expressed predominantly in the human nasal mucosa, where it catalyzes the transfer of glucuronic acid from UDP-glucuronic acid to both endogenous and exogenous lipophilic compounds including steroids, drugs, odorants, and toxicants. This conjugation, known as glucuronidation, increases the water solubility of these molecules, facilitating their excretion in urine or bile and generally inactivating them. UGT2A2 shares close sequence similarity and exon structure with UGT2A1 but exhibits some unique substrate specificities, such as enhanced glucuronidation of ethinylestradiol. UGT2A2 is implicated in local detoxification processes in the olfactory neuroepithelium and has been suggested as a molecular factor underlying smell impairment seen in some viral infections (e.g., COVID-19). Variability in UGT2A2 function (e.g., due to genetic polymorphisms) may influence response to drugs or environmental toxins predominantly affecting the nasal mucosa.

Other names

UDP glucuronosyltransferase family 2 member A2UDP-glucuronosyltransferase 2A2UDPGT 2A2UDP glucuronosyltransferase 2 family, polypeptide A2

Increases water solubility of substrates by conjugating glucuronic acid, thus facilitating excretion and usually inactivation (Phase II metabolism)