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Beta-1,3-glucuronyltransferase 2 (B3GAT2) is a type II transmembrane enzyme belonging to the glucuronyltransferase family. It catalyzes the transfer of a beta-1,3-linked glucuronic acid residue from UDP-glucuronic acid to the terminal galactose of glycoproteins or glycolipids that contain Gal-beta-1,4GlcNAc or Gal-beta-1,3GlcNAc residues. This enzyme is critically involved in the biosynthesis of the human natural killer-1 (HNK-1) carbohydrate epitope, a sulfated trisaccharide essential for cell migration and adhesion processes, particularly in the nervous system[1][2][3][6]. Diseases associated with B3GAT2 mutations include rare hereditary hyperbilirubinemia syndromes (Gilbert syndrome and Crigler-Najjar Syndrome, Type I)[1]. While the protein and its encoded activity play key roles in glycosylation, there are currently no known direct drug interactions or targeted therapies, and it is not an established therapeutic target in the sense of being the mechanism of action for approved medicines.
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