Synthesis and biological evaluation of new UDP-GalNAc analogues for the study of polypeptide-alpha-GalNAc-transferases.
A series of three O-methylated UDP-GalNAc analogues have been synthesised using a divergent strategy from a 3,6-di-O-pivaloyl GlcNAc derivative. The biological activity of these probes toward polypeptide-alpha-GalNAc-transferase T1 has been investigated. This study shows that this glycosyltransferase exhibits a very high substrate specificity.
Institut de Chimie Organique et Analytique, Université d'Orléans, BP 6759, 45067 Orléans, France.
Patricia
P
Busca
Véronique
V
Piller
Friedrich
F
Piller
Olivier R
OR
Martin
D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology; D006031:Glycosylation; D007527:Isoenzymes; D008745:Methylation; D017350:N-Acetylgalactosaminyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity; D014536:Uridine Diphosphate N-Acetylgalactosamine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology*; D000097763:Polypeptide N-acetylgalactosaminyltransferase
D004791:Enzyme Inhibitors; D007527:Isoenzymes; D017350:N-Acetylgalactosaminyltransferases; D014536:Uridine Diphosphate N-Acetylgalactosamine; D000097763:Polypeptide N-acetylgalactosaminyltransferase