Glycoside phosphorylases for carbohydrate synthesis: An insight into the diversity and potentiality

Abstract

Glycoside phosphorylases (GPs) are a major group of enzymes which catalyze the reversible formation and cleavage of glycosidic linkages, thus combining a dual functionality of both glycoside hydrolases (GHs) and glycosyltransferases (GTs). This unique advantage of reversibility, alongside with the strict regioselectivity, and the use of simple sugar phosphate donors, makes phosphorylases valuable catalysts in the synthesis of various carbohydrate structures, such as the synthesis of low-calorie sweeteners and valuable disaccharides, the synthesis of prebiotic compounds linked to health benefits, synthetic drug delivery systems and other physiological related structures, including, core components of N-linked glycans, O-linked mucin glycoproteins. Although these types of enzymes are still under-explored compared to the glycoside hydrolases and the glycosyltransferases, recently more discovered phosphorylases had been reported leading to more possibilities of synthesizing difficult glycosides. Herein we provide an overview of the distribution of GPs within the carbohydrate-active enzymes (CAZy) database, and the recent utilization of these enzymes for synthetic approaches of di- and oligosaccharides. • Glycoside phosphorylases (GPs) catalyze the reversible formation and cleavage of glycosidic linkages. • Glycoside phosphorylases have distinctive strict regioselectivity. • The reverse phosphorylsis functionality of GPs can be exploited to synthesize high value carbohydrate structures.