Mechanistic Insight into Enzymatic Glycosyl Transfer with Retention of Configuration through Analysis of Glycomimetic Inhibitors


  • 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.


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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.