Beta-1,3-galactosyltransferase 1 (B3GALT1)

Beta-1,3-galactosyltransferase 1 (B3GALT1) is a glycosyltransferase enzyme that catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues on glycoproteins and glycolipids, forming beta-1,3-galactosylated structures[2][4][7]. In mammals, this activity is critical for the production of type 1 chain oligosaccharides, which play various roles in cell-cell recognition, adhesion, and immune response. In plants, GALT1 homologs are essential for the biosynthesis of Lewis a epitopes on N-glycans, with exclusive Golgi apparatus localization governed by a type II transmembrane topology[1][5][6]. B3GALT1 is widely expressed with particularly high levels in the brain and colon mucosa, and its dysregulation or differential expression is implicated in cancer, allergy, and potential immune-mediated diseases[2][8].

Other names

B3GALT1GALT1Beta-1,3-galactosyltransferase

Glycosylation inhibition or modification (typical for drugs targeting glycosyltransferases, but no specific agents for B3GALT1 found in search results); Epigenetic modulation—e.g., histone deacetylase inhibitors can upregulate B3GALT1, impacting cellular recognition and adhesion structures