beta-1,4-galactosyltransferase I is a key inflammatory mediator that plays a critical role in the initiation and maintenance of inflammatory reaction in diseases, beta-1,4-GalT-I is associated with E-selectin during the pathological process of secondary response after Spinal cord injury
beta-1,4-GalT I might play important roles in Schwann cells during the regeneration and degeneration of the injured sciatic nerve, enzyme plays in important role in Schwann cells in vivo and vitro during pathology, beta-1,4-GalT can catalyze the galactose from UDP-galactose to the terminal N-acetylglucosamine residues on elongating oligosaccharide chains, which are suggested to be involved in various cellular functions including cell-cell and cell-matrix interactions during embryogenesis
beta-1,4-GalT-I may play an important role in adhesion and migration of Schwann cells during inflammation, enzyme is a key inflammatory mediator that participates in the initiation and maintenance of inflammatory reaction in diseases, the long beta-1,4-GalT-I isoform, due to the extra 13 amino acids at the amino-termini, is implicated in targeting the protein to cell surface, and acts as a recognition molecule associated with a variety of biological functions, including sperm-egg interactions, morula compaction, embryonic maturation, embryonal carcinoma cell spreading, neurite extension, and mesenchymal cell migration
enzyme is involved in the biosynthesis of the tetrasaccharide linker protein region (glucuronic acid beta1,3galactose beta1,3galactose beta1,4xylose beta1) of proteoglycans, by catalysing the transfer of galactose from the uridine 5-diphosphogalactose to a xylose residue, this reaction is rate-limiting in glycosaminoglycan biosynthesis
beta1,4-Galactosyltransferase I is a key enzyme in glycobiology mediating several biological mechanisms. The enzyme possibly regulate mutual uterus-embryo adhesion and embryo implantation by regulating cell surface Lewis-Y glycan expression
human xylosylprotein beta1,4-galactosyltransferase catalyzes the transfer of the first Gal residue of the tetrasaccharide linkage from the activated sugar UDP-galactose onto Xyl residues attached to the proteoglycan core protein. Because all glycosaminoglycans share the same stem core tetrasaccharide, the enzyme is a central enzyme in glycosaminoglycan biosynthesis
the galactosyltransferase beta4GalT7 is involved in the biosynthesis of glycosaminoglycan chains, initiated by xylosylation of the core protein followed by galactosylation by the enzyme
mapping of the organization of the acceptor binding pockex in complex with 4-methylumbelliferone-xylopyranoside as prototype substrate by combining molecular modeling, in vitro mutagenesis, and kinetic measurements, and in cellulo analysis of glycosaminoglycan anabolism and decorin glycosylation. The organization is governed, on one side, by three tyrosine residues, Tyr194, Tyr196, and Tyr199, which create a hydrophobic environment and provide stacking interactions with both xylopyranoside and aglycone rings. On the opposite side, a hydrogen-bond network is established between the charged amino acids Asp228, Asp229, and Arg226, and the hydroxyl groups of xylose
molecular docking complex of the beta4GalT7 mutant D211N from Drosophila melanogaster with substrates naphthalen-2-yl beta-D-xylopyranoside, naphthalen-2-yl 1-thio-beta-D-xylopyranoside, 2-naphthyl 5-thio-beta-D-xylopyranoside, and 2-naphthyl 1,5-dithio-beta-D-xylopyranoside