EC Number ![](./images/down.png) ![](./images/up.png) |
Substrates ![](./images/down.png) ![](./images/up.png) |
Organism ![](./images/down.png) ![](./images/up.png) |
Products ![](./images/down_red.png) ![](./images/up.png) |
Reversibility ![](./images/down.png) ![](./images/up.png) |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
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 |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
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 |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
enzyme transfers galactose to the terminal N-acetylglucosamine of N- and O-linked glycans in a beta-1,4-linkage |
Rattus norvegicus |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
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 |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
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 |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
donor and acceptor substrate binding, structure analysis, overview |
Drosophila melanogaster |
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![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
donor and acceptor substrate binding, strutcure analysis, overview |
Homo sapiens |
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? |
![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
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 |
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? |
![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
the enzyme catalyzes the transfer of galactose from uridine diphosphogalactose to terminal N-acetylglucosamine, forming the Galbeta1-4GlcNAc structure |
Homo sapiens |
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? |
![Show all pathways known for 2.4.1.133 Show all pathways known for 2.4.1.133](./images/citric_acid_cycle_small.png) ![Display the word map Display the word map](./images/word_maps.png) 2.4.1.133 | more |
enzymatic galactosylation reaction using epimerase UDP-glucose 4-epimerase MgUGE (EC 5.1.3.2) and beta-1,4-galactosyltransferase MgGalT7 with 4-nitrophenol xylose and UDP-glucose as substrates, mass spectrometric analyses of the acceptor substrate and the galactosylated reaction product, coupled assay method, evaluation, overview |
Crassostrea gigas |
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