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Mechanistic Insight into Enzymatic Glycosyl Transfer with Retention of Configuration through Analysis of Glycomimetic Inhibitors
Author(s) -
Errey James C.,
Lee Seung Seo,
Gibson Robert P.,
Martinez Fleites Carlos,
Barry Conor S.,
Jung Pierre M. J.,
O'Sullivan Anthony C.,
Davis Benjamin G.,
Davies Gideon J.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200905096
Subject(s) - glycosyl , ternary complex , anomer , ternary operation , chemistry , enzyme , stereochemistry , walden inversion , mechanism (biology) , biochemistry , computer science , physics , quantum mechanics , programming language
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.