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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প্রধান লেখক: Errey, J, Lee, S, Gibson, R, Martinez Fleites, C, Barry, C, Jung, P, O'Sullivan, A, Davis, B, Davies, G
বিন্যাস: Journal article
ভাষা:English
প্রকাশিত: 2010
বিবরন
সংক্ষিপ্ত:(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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