Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution

Shangshang Sun; Chun You

doi:10.1016/j.synbio.2021.01.004

Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution

Synth Syst Biotechnol. 2021 Feb 13;6(1):23-31. doi: 10.1016/j.synbio.2021.01.004. eCollection 2021 Mar.

Authors

Shangshang Sun¹, Chun You^{1

2

3}

Affiliations

¹ Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West 7th Avenue, Tianjin Airport Economic Area, Tianjin, 300308, People's Republic of China.
² University of Chinese Academy of Sciences, 19A Yuquan Road, Shijingshan District, Beijing, 100049, People's Republic of China.
³ National Technology Innovation Center of Synthetic Biology, Tianjin, 300308, People's Republic of China.

Abstract

Disaccharide phosphorylases (DSPs) are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They are modular enzymes that form active homo-oligomers. From a mechanistic as well as a structural point of view, they are similar to glycoside hydrolases or glycosyltransferases. As the majority of DSPs show strict stereo- and regiospecificities, these enzymes were used to synthesize specific disaccharides. Currently, protein engineering of DSPs is pursued in different laboratories to broaden the donor and acceptor substrate specificities or improve the industrial particularity of naturally existing enzymes, to eventually generate a toolbox of new catalysts for glycoside synthesis. Herein we review the characteristics and classifications of reported DSPs and the glycoside products that they have been used to synthesize.

Keywords: Classification; Disaccharide phosphorylase; Enzyme engineering; Structure and domains; Substrate specificity.