Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors.

Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors.

(Figure Presented) 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 kineti...

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Bibliografische gegevens
Hoofdauteurs: Errey, J, Lee, S, Gibson, R, Martinez Fleites, C, Barry, C, Jung, P, O'Sullivan, A, Davis, B, Davies, G
Formaat: Journal article
Taal:English
Gepubliceerd in: 2010
Omschrijving
Samenvatting:(Figure Presented) 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. © 2010 Wiley-VCH Verlag GmbH and. Co. KGaA.

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