Artificial N-functionalized UDP-glucosamine analogues as modified substrates for N-acetylglucosaminyl transferases.
Analogues of UDP-GlcNAc modified at the 2-acetamido group of the GlcNAc moiety were prepared in order to study their role in the mechanism of N-acetylglucosaminyl transferase mediated glycosylation reactions. The structural analogues with N-formyl-, N-propionyl-, N-butyryl- and N-isobutyryl-groups were synthesized, utilizing the morpholidate coupling method starting from d-glucosaminyl-1-phosphate after selective N-acylation of its amino group with the appropriate N-acyloxysuccinimide esters as well as a chlorinated formylformiate.
Lazarević
Daniel
D
Institut für Organische Chemie, Universität Hamburg, Martin-Luther-King-Platz 6, D-20146 Hamburg, Germany.
Thiem
Joachim
J
D005944:Glucosamine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D013379:Substrate Specificity
C026712:UDP-glucosamine; D017351:N-Acetylglucosaminyltransferases; D005944:Glucosamine