Small-molecule glucosylation by sucrose phosphorylase: structure-activity relationships for acceptor substrates revisited.

Christiane Luley-Goedl, Bernd Nidetzky

Index: Carbohydr. Res. 345(10) , 1492-6, (2010)

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Abstract

Sucrose phosphorylase catalyzes the O-glucosylation of a wide range of acceptor substrates. Acceptors presenting a suitable 1,2-diol moiety are glucosylated exclusively at the secondary hydroxyl. Production of the naturally occurring compatible solute, 2-O-alpha-d-glucopyranosyl-sn-glycerol, from sucrose and glycerol is a notable industrial realization of the regio- and stereoselective biotransformation promoted by sucrose phosphorylase. The acceptor substrate specificity of sucrose phosphorylase was analyzed on the basis of recent high-resolution crystal structures of the enzyme. Interactions at the acceptor binding site, observed in the crystal (d-fructosyl) and suggested by results of docking experiments (glycerol), are used to rationalize experimentally determined efficiencies and regioselectivities of enzymatic glucosyl transfer.Copyright 2010 Elsevier Ltd. All rights reserved.