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

Journal article

(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.

Authors: Errey, J; Lee, S; Gibson, R; Martinez Fleites, C; Barry, C

• Publication status: Published
• Journal: Angewandte Chemie (International ed. in English)
• Volume: 49
• Issue: 7
• Pages: 1234-1237
• Publication date: 2010-02-01
• DOI: 10.1002/anie.200905096
• EISSN: 1521-3773
• ISSN: 1433-7851
• Language: English
• Keywords: Glucosyltransferases; Uridine Diphosphate; Kinetics; Protein Structure, Tertiary; Trehalose; Enzyme Inhibitors; Catalytic Domain