Abstract

The carbohydrate portions of glycoproteins are implicated to play a major role in modulating the structure and biological functions of glycoproteins. However, deciphering the structure and functions of glycoproteins is often hampered by the difficulties in obtaining homogeneous glycoproteins and glycopeptides. This article reviews the transglycosylation with endo-β-N-acetylglucosamindases and their application for glycopeptide synthesis. In contrast to glycosyltransferase that adds monosaccharide units one at a time, the endoglycosidase transfers an oligosaccharide moiety to a suitable acceptor in a single step. Incorporation of endoglycosidases into synthetic strategy has made available an array of homogeneous, complex glycopeptides for structural and biological studies.

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