UDP-glucuronosyltransferase 2B10 (UGT2B10)

UDP-glucuronosyltransferase 2B10 (UGT2B10) is a membrane-bound enzyme predominantly expressed in the liver, catalyzing the transfer of glucuronic acid from UDP-glucuronic acid to a range of exogenous and endogenous molecules (especially amine-containing drugs and xenobiotics). This glucuronidation reaction is a major route for the conjugation and excretion of drugs, environmental toxins, and hormones. UGT2B10 has unique substrate specificity relative to other UGT family members, displaying efficient N-glucuronidation activity for compounds such as nicotine, amitriptyline, and imipramine. Deficient or variant UGT2B10 can impact drug metabolism efficiency and increase risk for toxicity, making it clinically relevant as both a therapeutic target and biomarker for pharmacogenomics. Structural insights: Recent high-resolution crystallography of the C-terminal domain reveals the conserved cofactor (UDPGA) binding pocket critical for catalytic function. The enzyme belongs to the glycosyltransferase family, functioning within the endoplasmic reticulum membrane. Clinical and pharmacological relevance: UGT2B10 plays a crucial role in the metabolic clearance of several drugs and toxins, influencing drug efficacy and safety through genetic variability. Drugs targeting or metabolized by UGT2B10 may require patient genotyping for optimal therapeutic outcomes.

Other names

UDP-glucuronosyltransferase family 2 member B10UGT2B10UDPGT 2B10UDPGT2B10UDP-glucuronosyltransferase 2 familypolypeptide B10UDB10EC 2.4.1.17UDP glycosyltransferase 2B10

Substrate N-glucuronidation (addition of glucuronic acid to nitrogen atom on drugs/xenobiotics) leading to increased water-solubility and excretion