Title : A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2.

Pub. Date : 2014 May 7

PMID : 24643241






4 Functional Relationships(s)
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1 Here we present the first QM/MM calculations of human GalNAc-T2, a retaining glycosyltransferase, which initiates the biosynthesis of mucin-type O-glycans. o-glycans polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens
2 Additionally, our calculations for different donor substrates suggest that human GalNAc-T2 would be inactive if 2"-deoxy-Gal or 2"-oxymethyl-Gal were used, while UDP-Gal is confirmed as a valid sugar donor. 2"-deoxy-gal polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens
3 Additionally, our calculations for different donor substrates suggest that human GalNAc-T2 would be inactive if 2"-deoxy-Gal or 2"-oxymethyl-Gal were used, while UDP-Gal is confirmed as a valid sugar donor. 2"-oxymethyl-gal polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens
4 Additionally, our calculations for different donor substrates suggest that human GalNAc-T2 would be inactive if 2"-deoxy-Gal or 2"-oxymethyl-Gal were used, while UDP-Gal is confirmed as a valid sugar donor. Sugars polypeptide N-acetylgalactosaminyltransferase 2 Homo sapiens