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Literature summary for 2.4.1.133 extracted from
- Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human beta1,4-galactosyltransferase 7 (GalT-I) and beta1,3-glucuronosyltransferase I (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans (2005), J. Biol. Chem., 280, 1417-1425.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| placenta | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-galactose + O-beta-D-xylosylprotein | the enzyme is unable to catalyze the transfer of galactose from UDP-galactose onto xylose when this residue is phosphorylated at the C-2 position | Homo sapiens | UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta1,4-galactosyltransferase 7 | - |
Homo sapiens |
| GalT-I | - |
Homo sapiens |
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