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

Errey James C. | Zendy; Lee Seung Seo | Zendy; Gibson Robert P. | Zendy; Martinez Fleites Carlos | Zendy; Barry Conor S. | Zendy; Jung Pierre M. J. | Zendy; O'Sullivan Anthony C. | Zendy; Davis Benjamin G. | Zendy; Davies Gideon J. | Zendy

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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.

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