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The Reaction Coordinate of a Bacterial GH47 α-Mannosidase: A Combined Quantum Mechanical and Structural Approach

DOI: 10.1002/anie.201207917 DOI Help

Authors: Andrew Thompson (University of York) , Jerome Dabin (University of York) , Javier Iglesias-fernández (Parc Científic de Barcelona) , Albert Ardèvol (Parc Científic de Barcelona) , Zoran Dinev (University of Melbourne) , Spencer J. Williams (University of Melbourne) , Omprakash Bande (CNRS-FRE) , Aloysius Siriwardena (CNRS-FRE) , Carl Moreland (Newcastle University) , Ting-chou Hu (University of York) , David K. Smith (University of York) , Harry J. Gilbert (Newcastle University) , Carme Rovira (Parc Científic de Barcelona) , Gideon J. Davies (University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie International Edition , VOL 51 (44) , PAGES 10997 - 11001

State: Published (Approved)
Published: October 2012

Abstract: Mannosidases are glycoside hydrolases that face special stereoelectronic challenges in effecting the hydrolysis of the glycosidic bond. In their Communication on page?10997?ff., C. Rovira, G.?J. Davies, and co-workers use QM/MM calculations, supported by X-ray structures of the enzyme with ligands mimicking the substrate, transition state, and product, to show that the free-energy landscape of an isolated alpha-mannoside is shaped on-enzyme into a single conformational itinerary along the reaction coordinate.

Subject Areas: Chemistry


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography