Glycoenzymes in glycan analysis and synthesis

Abstract

Glycan structural analysis and glycan synthesis are important for the development of glycan-related therapeutics and vaccines. The utility of glycoenzymes, including glycosidases and glycosyltransferases, for glycan analysis and synthesis has been increasing because these enzymes have specificity for their substrates. Glycosidase catalyzes the hydrolysis of a glycosidic linkage and is generally used to determine the presence of specific glycosidic linkages. Glycosyltransferase catalyzes the transfer of monosaccharide from a glycosyl donor substrate onto an acceptor to form a new specific glycosidic linkage. Enzyme-catalyzed glycan synthesis is often superior to chemical synthesis in view of its regio- and stereospecificity and technical simplicity, although there are still some limitations. Moreover, transglycosylation activity of glycosidase and glycosynthase is also useful for the glycan synthesis. The reservoir of glycoenzymes as an array of useful tools for glycan manipulation will be further enriched by an increase in number of sequenced genome, which will be then accelerating their applications and also enhancing the feasibility in development of glycan-related therapeutics.