EC Number   |
Natural Substrates |
|---|
    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 |
| 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 |
| 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 |
| 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 |
| 2.4.1.133 | UDP-alpha-D-galactose + 2-naphthyl beta-D-xylopyranoside |
- |
| 2.4.1.133 | UDP-alpha-D-galactose + O-beta-D-xylosyl-[protein] |
- |
| 2.4.1.133 | UDP-galactose + O-beta-D-xylosylprotein |
- |
| 2.4.1.133 | UDP-galactose + O-beta-D-xylosylprotein |
in a progeroid patient carrying two point mutations in beta4galactosyltransferase I (ß4GalT-7) only 50% of the decorin core protein molecules are substituted with glycosaminoglycan chains. Tthe ß4GalT-7 mutations directly affect the molecular phenotype of decorin observed in a patient with the progeroid form of Ehlers-Danlos syndrome, which may be a major mechanistic cause for the skin and wound healing defects observed in this patient |
| 2.4.1.133 | UDPgalactose + N-acetyl-beta-D-glucosamine |
- |
| 2.4.1.133 | UDPgalactose + O-beta-D-xylosylprotein |
involved in chondroitin sulfate biosynthesis |
