Cloned (Comment) | Organism |
---|---|
expression of mutant cDNA from a patient with the congenital disorder of glycosylation type IId leads to the synthesis of a truncated, inactive polypeptide, which is localized to the endoplasmic reticulum | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides | Homo sapiens | main enzyme responsible for the transfer of galactose residues from UDPgalactose into terminal N-acetylglucosamine residues of complex-type oligosaccharides in newly synthesized glycoproteins in the Golgi apparatus. Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId, a severe neurologic disease characterized by a hydrocephalus, myopathy and blood-clotting defects | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides | main enzyme responsible for the transfer of galactose residues from UDPgalactose into terminal N-acetylglucosamine residues of complex-type oligosaccharides in newly synthesized glycoproteins in the Golgi apparatus. Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId, a severe neurologic disease characterized by a hydrocephalus, myopathy and blood-clotting defects | Homo sapiens | ? | - |
? |