We thank Dr. M Yang for technical assistance. This work was funded by the BBSRC (BB/E004350/1, BB/D006112/1) and EPSRC (EP/E000614/1). G.J.D. and B.G.D. are Royal Society–Wolfson Research Merit Award recipients.
Mechanistic Insight into Enzymatic Glycosyl Transfer with Retention of Configuration through Analysis of Glycomimetic Inhibitors†
Article first published online: 14 JAN 2010
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 7, pages 1234–1237, February 8, 2010
How to Cite
Errey, James C., Lee, S., Gibson, Robert P., Martinez Fleites, C., Barry, Conor S., Jung, Pierre M. J., O'Sullivan, Anthony C., Davis, Benjamin G. and Davies, Gideon J. (2010), Mechanistic Insight into Enzymatic Glycosyl Transfer with Retention of Configuration through Analysis of Glycomimetic Inhibitors. Angew. Chem. Int. Ed., 49: 1234–1237. doi: 10.1002/anie.200905096
- Issue published online: 1 FEB 2010
- Article first published online: 14 JAN 2010
- Manuscript Received: 11 SEP 2009
- BBSRC. Grant Numbers: BB/E004350/1, BB/D006112/1
- EPSRC. Grant Number: EP/E000614/1
- bisubstrate mimetic;
- internal return;
Structural “valid”-ation: The mechanism of enzyme-catalyzed glycosyl transfer with retention of anomeric configuration continues to baffle, a situation compounded by the lack of insightful 3-D structures of ternary enzyme complexes. Synthesis and multi-dimensional kinetic analysis of validoxylamine derivatives are used to access the 3-D structure of a ternary complex (see picture; U=uridyl) providing insight into the geometry and donor–acceptor interplay at the glycosyltransfer site.