Beta-1,3-galactosyltransferase 9 (B3GALT9)

Beta-1,3-galactosyltransferase 9 (B3GALT9) is an enzyme classified as a glycosyltransferase, primarily localizing to the Golgi membrane, where it catalyzes the transfer of galactose from UDP-galactose to glycan acceptors during the biosynthesis of O-linked glycoproteins and glycolipids[2]. Its action is important for the formation of specific glycan structures, including Lewis antigens and globo-series glycosphingolipids such as SSEA-3, SSEA-4, and Globo-H, which are highly expressed in many cancers and contribute to tumor malignancy, metastasis, and immunotherapy targets[1]. B3GALT9 is associated with disease mechanisms in certain congenital muscular dystrophies and glycogen storage disorders[2]. Although no interacting drugs are currently listed, the enzyme’s role in cancer-associated glycan biosynthesis makes it a promising candidate for therapeutic targeting and biomarker development.

Other names

Beta-1,3-galactosyltransferase 9B3GALT9B3GNT10UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 10UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 pseudogeneLOC100288842LOC402377

Inhibition or modulation of glycosyltransferase activity to alter cancer-associated glycan biosynthesis (theoretical, as no approved drugs or chemical probes are specifically cited)