Synthesis of a high-mannose-type glycopeptide analog containing a glucose-asparagine linkage

• Published in: Bioorganic & medicinal chemistry letters Vol. 8; no. 13; pp. 1763 - 1766
• Main Authors: Deras, Ina L., Takegawa, Kaoru, Kondo, Akihiro, Kato, Ikunoshin, Lee, Yuan C.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 07.07.1998; Elsevier
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Asparagine - chemistry; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Carbohydrate Sequence; Chemistry; Enzymes and enzyme inhibitors; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Glucose - chemistry; Glycopeptides - chemical synthesis; Glycopeptides - chemistry; Hydrolases; Magnetic Resonance Spectroscopy; Mannose - chemistry; Methods. Procedures. Technologies; Molecular Sequence Data; Organic chemistry; Peptides; Preparations and properties; Protein Conformation; Enzyme; Oligoholoside; Enzyme inhibitor; In vitro; Biological activity; Peptide-N; Transglycosylation; Branched chain; α-N-Acetylglucosaminidase; Glycopeptide; (N-acetyl-β-glucosaminyl) asparagine amidase; Glycosidases; Bacteria; Hydrolases; Actinomycetes; Chemical synthesis; O-Glycosidases; Arthrobacter; Pentapeptide; Enzymatic reaction
• ISSN: 0960-894X; 1464-3405
• DOI: 10.1016/S0960-894X(98)00306-0

The title compound was prepared by enzymatic transfer of oligosaccharide to a synthetic pentapeptide containing the Glc-Asn linkage. The compound was not hydrolyzed by glycoamidases from plant and bacterial sources, but it inhibited both enzymes in the micromolar range. Its activity is compared to other potential inhibitors. Graphic