کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1390667 | 983117 | 2010 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Small-molecule glucosylation by sucrose phosphorylase: structure–activity relationships for acceptor substrates revisited Small-molecule glucosylation by sucrose phosphorylase: structure–activity relationships for acceptor substrates revisited](/preview/png/1390667.png)
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-α-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.
Figure optionsDownload as PowerPoint slide
Journal: Carbohydrate Research - Volume 345, Issue 10, 2 July 2010, Pages 1492–1496