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• W1966967035 endingPage "11146" @default.
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• W1966967035 abstract "A novel chemoenzymatic approach to synthesizing high-mannose-type N-glycopeptide and its C-linked glycopeptide analog is described. The synthesis consists of two steps: a chemical synthesis of GlcNAc-containing peptides and an enzymatic glycosyl transfer of Man9GlcNAc to the terminal GlcNAc in the peptides in an aqueous medium containing organic solvents. The essential enzyme used is an endo-β-N-acetyl-glucosaminidase from Arthrobacter protophormiae (Endo-A). This approach should be generally applicable to the synthesis of both natural and designed high-mannose-type glycopeptides. It has been found that, while the natural high-mannose-type N-glycopeptide 2 can be rapidly hydrolyzed by glycoamidases [commonly called N-glycanase or, systematically, peptide-N4-(N-acetyl-β-d-glucosaminylasparagine amidase], the synthetic C-glycopeptide 1 with an insertion of a methylene group at the crucial asparagine−GlcNAc linkage is resistant to the enzyme-catalyzed hydrolysis and shows apparent inhibitory activity toward glycoamidases of plant, bacterial, and animal origin, with the Ki values ranging from 1 to 160 μM for different enzymes. The C-glycopeptide 1 is the first, broad spectrum inhibitor for glycoamidases, which is expected to be a useful tool in the study of the mechanism and biological functions of the enzymes." @default.
• W1966967035 created "2016-06-24" @default.
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• W1966967035 date "1997-11-01" @default.
• W1966967035 modified "2023-10-16" @default.
• W1966967035 title "Combined Chemical and Enzymatic Synthesis of a <i>C</i>-Glycopeptide and Its Inhibitory Activity toward Glycoamidases" @default.
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• W1966967035 doi "https://doi.org/10.1021/ja9712027" @default.
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