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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) is a type II transmembrane glycosyltransferase enzyme encoded by the B3GNT2 gene in humans. It catalyzes the transfer of N-acetylglucosamine (GlcNAc) from the donor UDP-GlcNAc to beta-galactoside acceptors, forming beta-1,3 glycosidic linkages and thereby participates in the biosynthesis of poly-N-acetyllactosamine chains. These structures are important in cell-cell and cell-matrix interactions, particularly in the biosynthesis of complex glycans in glycoproteins and glycolipids. Mutations in B3GNT2 are associated with glycosylation disorders, including muscular dystrophy-dystroglycanopathy and neurological syndromes such as lissencephaly. The enzyme’s catalytic mechanism involves coordinated substrate binding and inverting glycosyltransferase chemistry dependent on conserved active site residues and magnesium. Its activity and specificity make it a potential, but as yet largely unexploited, therapeutic target for modulating glycan structures in health and disease[1][3][5].
Glycosylation modulation via transfer of N-acetylglucosamine from UDP-GlcNAc to beta-galactoside, forming beta-1,3 glycosidic bonds [1][3][5]
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