UGT2B10 is a UDP-glucuronosyltransferase enzyme primarily expressed in human liver that catalyzes the glucuronidation of diverse substrates, playing a critical role in xenobiotic detoxification and drug metabolism 1. The enzyme exhibits high-affinity N-glucuronidation activity toward tertiary amines, including nicotine and cotinine, where UGT2B10 demonstrates superior catalytic efficiency compared to other UGT isoforms 2. UGT2B10 metabolizes multiple clinically important drugs, including tricyclic antidepressants (amitriptyline, imipramine, clomipramine, trimipramine), atypical antipsychotics (asenapine, clozapine), and lamotrigine, often serving as the primary glucuronidation enzyme at therapeutic concentrations 345. Beyond N-glucuronidation, UGT2B10 catalyzes N-glucosidation as an alternative metabolic pathway 6. Expression of UGT2B10 is subject to epigenetic regulation by microRNA-485-5p, which reduces enzyme activity and contributes to inter-individual variability in drug response 1. A functional polymorphism (D67Y) significantly impairs UGT2B10 activity against tobacco-specific nitrosamines and may influence smoking-related cancer susceptibility 7. UGT2B10 polymorphisms represent an important pharmacogenomic factor affecting dexmedetomidine and other medication pharmacokinetics, particularly in pediatric populations 8.