UDP-glucuronosyltransferase 2B11 (UGT2B11)

UDP-glucuronosyltransferase 2B11 is an enzyme of the glycosyltransferase 1 family, encoded by the UGT2B11 gene on chromosome 4q13.2. Its primary biological role is in the conjugation (glucuronidation) and elimination of potentially toxic xenobiotics and endogenous compounds, such as steroids and drugs, thereby facilitating their excretion. It is a membrane-bound protein, localized predominantly at the endoplasmic reticulum membrane. UGT2B11’s canonical function involves transferring glucuronic acid from UDP-glucuronic acid to molecules with appropriate accepting groups. Recent evidence suggests it plays a more nuanced regulatory role in cancer biology by interacting with lipid signaling pathways and modulating other UGT enzymes, particularly in the context of androgen responses in prostate and breast cancer cells. While a member of the broader UDP-glucuronosyltransferase family important in drug metabolism, its direct substrate specificity, disease associations, and roles are less characterized compared to other UGTs (such as UGT2B7 and UGT2B15).

Other names

UDP glucuronosyltransferase family 2 member B11UDPGT 2B11UDP-glucuronosyltransferase 2B11UDP glucuronosyltransferase 2 family, polypeptide B11UDP glycosyltransferase 2 family proteinUDP glycosyltransferase 2 family, polypeptide B11

Drugs metabolized by UGT2B11 are converted via glucuronidation, resulting in increased solubility and enhanced excretion. In cancer, UGT2B11 may indirectly modulate steroid (androgen) and lipid signaling by influencing SREBP pathway activity and inhibiting other UGT enzymes involved in androgen metabolism.