Small-molecule glucosylation by sucrose phosphorylase: structure-activity relationships for acceptor substrates revisited.
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.
Luley-Goedl
Christiane
C
Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/1, 8010 Graz, Austria.
Nidetzky
Bernd
B
D001644:Bifidobacterium / Q000201:enzymology; D005947:Glucose / Q000378:metabolism*; D005964:Glucosyltransferases / Q000737:chemistry* / Q000378:metabolism*; D006031:Glycosylation; D007934:Leuconostoc / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D005964:Glucosyltransferases; C025901:sucrose phosphorylase; D005947:Glucose