Glycosylation in vitro of an asparagine sequon catalysed by preparations of yeast cell membranes.
Preparations of yeast cell membranes can catalyse in vitro the N-acetyl-beta-D-glucosaminylation of the asparagine sequon at residues 34--36 of bovine pancreatic ribonuclease A. The relevant glycopeptides were isolated from tryptic hydrolysates of the glycosylated ribonuclease and analysed. The donor used was UDP-N-acetyl-D-glucosamine, although the mechanism of the transfer is unknown. Mn2+ ions at concentrations of 25 mM double the activity of the enzymic transfer.
D000117:Acetylglucosamine / Q000378:metabolism; D000818:Animals; D001216:Asparagine / Q000378:metabolism*; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology*; D005944:Glucosamine / Q000378:metabolism; D008345:Manganese / Q000494:pharmacology; D010179:Pancreas / Q000201:enzymology; D012260:Ribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000648:ultrastructure
D008345:Manganese; D001216:Asparagine; D012260:Ribonucleases; D005944:Glucosamine; D000117:Acetylglucosamine