2.4.1.133	4-nitrophenyl beta-D-xylopyranoside + UDP-alpha-D-galactose	-	Homo sapiens	UDP + 4-nitrophenyl 4-O-beta-D-galactopyranosyl-beta-D-xylopyranoside	-	?	420090	
2.4.1.133	additional information	beta-1,4-galactosyltransferase is responsible for the biosynthesis of Gal-beta - 4GlcNAc units in N-glycans and core 2 O-glycans of glycoproteins, including IgG, gp120 and serum alpha-fetoprotein	Homo sapiens	?	-	?	89	
2.4.1.133	additional information	enzyme catalyzes the transfer of galactose from the sugar nucleotide donor uridine diphosphate galactose to glycoside residues with a terminal N-acetylglucosamine moiety	Rattus norvegicus	?	-	?	89	
2.4.1.133	additional information	enzyme transfers galactose to the terminal N-acetylglucosamine of N- and O-linked glycans in a beta-1,4-linkage	Rattus norvegicus	?	-	?	89	
2.4.1.133	additional information	enzyme is able to transfer glucose, xylose and, to a lesser extent glucuronic acid and N-acetylglucosamine, to acceptor sugars, whereas UDP-mannose and UDP-N-acetyl galactosamine are not substrates	Homo sapiens	?	-	?	89	
2.4.1.133	additional information	some beta-D-xylosides, such as 2-naphthyl beta-D-xylopyranoside, can induce glycosaminoglycan synthesis by serving as acceptor substrates for beta4GalT7 and by that also compete with the glycosaminoglycan synthesis on core proteins	Homo sapiens	?	-	?	89	
2.4.1.133	additional information	donor and acceptor substrate binding, structure analysis, overview	Drosophila melanogaster	?	-	?	89	
2.4.1.133	additional information	donor and acceptor substrate binding, strutcure analysis, overview	Homo sapiens	?	-	?	89	
2.4.1.133	additional information	structure-activity relationships for beta4GalT7 and xylosides with modifications of the aromatic aglycon, using enzymatic assays, cell studies, and molecular docking simulations, show that the aglycons reside on the outside of the active site of the enzyme and that quite bulky aglycons are accepted. Increased galactosylation with increased linker length is observed, substrate specificity with glycosides, detailed overview. The galactosylation is influenced by the identity and position of substituents in the aromatic framework, and generally, only xylosides with beta-glycosidic linkages function as good substrates for the enzyme. The galactosylation ability of a xyloside is increased by replacing the anomeric oxygen with sulfur, but decreased by replacing it with carbon. Enzyme reaction kinetics of galactosylation are dependent on subtle differences in orientation of the xylose moiety	Homo sapiens	?	-	?	89	
2.4.1.133	additional information	the enzyme catalyzes the transfer of galactose from uridine diphosphogalactose to terminal N-acetylglucosamine, forming the Galbeta1-4GlcNAc structure	Homo sapiens	?	-	?	89