Possible Interaction: Acetylglucosamine and Oligosaccharides

“Although the biological meaning of the bisecting GlcNAc structure remains unclear, it is known that the attachment of a bisecting GlcNAc inhibits further processing of oligosaccharides by other glycosyltransferases.”

“Removal of GlcNAc or addition of Gal to either the oligosaccharide or glycopeptide destroyed the ability to serve as substrates.”

“The major phosphorylated oligosaccharides contain one and two and possibly three phosphate groups blocked by N-acetylglucosamine.”

“When GT was overexpressed, oligosaccharides terminating with GlcNAc were significantly reduced compared with controls, whereas overexpression of ST resulted in sialylation of ≥90% of available branches.”

“Among the oligosaccharides tested, GlcNAc beta 1-->4(GlcNAc beta 1-->2)Man alpha 1-O(CH2)2 CH3 was the most potent inhibitor, and the inhibitory potency of the oligosaccharide was 2(4) times greater than those of GlcNAc and GalNAc.”

“… oligosaccharidic ligand toward the upstream end (in an oligo- (or poly-)saccharide, such as A-->B-->C-->D-->E-->m, where A, B, C, … as methyl, we define A as the glycosyl- or upstream terminus, and E as the glycoside- or downstream terminus) by rhamnosyl and N-acetylglucosaminyl moieties ….”

“In the higher oligosaccharides (m = 2-5) the gross extent of C-6 O-sulphation of GlcNAc residues falls systematically with increasing oligosaccharide size , whereas that in the aManOH residues remains below 10%.”

“Addition of the bisecting N-acetylglucosamine residue reduces the affinity of oligosaccharides to the column, but addition of an alpha-fucosyl residue at the C-6 position of the proximal N-acetylglucosamine residue does not affect the behavior of oligosaccharides in the column.”

“However, adding a so-called bisecting N-acetyl-D-glucosamine residue to the trimannosyl oligosaccharide greatly reduces its binding affinity and produces a decrease in the NMRD profile of the protein similar to that observed for monosaccharide binding.”