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  • Title: Transglycosylation of intact sialo complex-type oligosaccharides to the N-acetylglucosamine moieties of glycopeptides by Mucor hiemalis endo-beta-N-acetylglucosaminidase.
    Author: Haneda K, Inazu T, Yamamoto K, Kumagai H, Nakahara Y, Kobata A.
    Journal: Carbohydr Res; 1996 Oct 04; 292():61-70. PubMed ID: 8870237.
    Abstract:
    The endo-beta-N-acetylglucosaminidase (endo-beta-GlcNAc-ase) of Mucor hiemalis, endo-M, was found to transfer the sialo complex-type oligosaccharides from transferrin glycopeptide to the N-acetylglucosamine (GlcNAc) moieties of peptidyl-GlcNAc. Disialo complex-type oligosaccharide of transferrin glycopeptide was transferred to 9-fluorenylmethyloxycarbonyl (Fmoc)-asparaginyl-N-acetylglucosaminide (Fmoc-Asn-GlcNAc) by endo-M in a high yield. The structure of the reaction product was confirmed to be Fmoc-Asn-(GlcNAc)2-Man-(Man-GlcNac-Gal-NeuAc)2 by mass spectrometry. Endo-M also transferred disialo complex-type oligosaccharide to the GlcNAc residue of chemically synthesized H-Ile-Asn(GlcNAc)-Ala-Thr-Leu-OH. Asn-linked asialo complex-type oligosaccharide and Asn-linked high-mannose type oligosaccharide were also effective as oligosaccharide donors. Transfer of disialo complex-type oligosaccharide to the GlcNAc-peptide was the most effective among the three types of oligosaccharides, although the disialo complex-type oligosaccharide attached to the peptide was the poorest substrate for the hydrolytic activity of endo-M.
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