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Start Over Author "Thompson, Andrew J." Journal angewandte chemie
8 results on '"Thompson, Andrew J."'

3. Berichtigung: Evidence for a Boat Conformation at the Transition State of GH76 α-1,6-Mannanases-Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism

Author

Thompson, Andrew J., primary, Speciale, Gaetano, additional, Iglesias-Fernández, Javier, additional, Hakki, Zalihe, additional, Belz, Tyson, additional, Cartmell, Alan, additional, Spears, Richard J., additional, Chandler, Emily, additional, Temple, Max J., additional, Stepper, Judith, additional, Gilbert, Harry J., additional, Rovira, Carme, additional, Williams, Spencer J., additional, and Davies, Gideon J., additional

Published
2016
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4. Evidence for a Boat Conformation at the Transition State of GH76 α‐1,6‐Mannanases—Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism

Author

Thompson, Andrew J., primary, Speciale, Gaetano, additional, Iglesias‐Fernández, Javier, additional, Hakki, Zalihe, additional, Belz, Tyson, additional, Cartmell, Alan, additional, Spears, Richard J., additional, Chandler, Emily, additional, Temple, Max J., additional, Stepper, Judith, additional, Gilbert, Harry J., additional, Rovira, Carme, additional, Williams, Spencer J., additional, and Davies, Gideon J., additional

Published
2015
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5. Combined Inhibitor Free-Energy Landscape and Structural Analysis Reports on the Mannosidase Conformational Coordinate

Author

Williams, Rohan J., primary, Iglesias-Fernández, Javier, additional, Stepper, Judith, additional, Jackson, Adam, additional, Thompson, Andrew J., additional, Lowe, Elisabeth C., additional, White, Jonathan M., additional, Gilbert, Harry J., additional, Rovira, Carme, additional, Davies, Gideon J., additional, and Williams, Spencer J., additional

Published
2013
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6. Innenrücktitelbild: The Reaction Coordinate of a Bacterial GH47 α-Mannosidase: A Combined Quantum Mechanical and Structural Approach (Angew. Chem. 44/2012)

Author

Thompson, Andrew J., primary, Dabin, Jerome, additional, Iglesias-Fernández, Javier, additional, Ardèvol, Albert, additional, Dinev, Zoran, additional, Williams, Spencer J., additional, Bande, Omprakash, additional, Siriwardena, Aloysius, additional, Moreland, Carl, additional, Hu, Ting-Chou, additional, Smith, David K., additional, Gilbert, Harry J., additional, Rovira, Carme, additional, and Davies, Gideon J., additional

Published
2012
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7. The Reaction Coordinate of a Bacterial GH47 α-Mannosidase: A Combined Quantum Mechanical and Structural Approach

Author

Thompson, Andrew J., primary, Dabin, Jerome, additional, Iglesias-Fernández, Javier, additional, Ardèvol, Albert, additional, Dinev, Zoran, additional, Williams, Spencer J., additional, Bande, Omprakash, additional, Siriwardena, Aloysius, additional, Moreland, Carl, additional, Hu, Ting-Chou, additional, Smith, David K., additional, Gilbert, Harry J., additional, Rovira, Carme, additional, and Davies, Gideon J., additional

Published
2012
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8. Combined Inhibitor Free-Energy Landscape and Structural Analysis Reports on the Mannosidase Conformational Coordinate.

Author

Williams, Rohan J., Iglesias ‐ Fernández, Javier, Stepper, Judith, Jackson, Adam, Thompson, Andrew J., Lowe, Elisabeth C., White, Jonathan M., Gilbert, Harry J., Rovira, Carme, Davies, Gideon J., and Williams, Spencer J.

Subjects
MANNOSIDASES, ENZYME inhibitors, MOLECULAR conformation, HYDROLYSIS, POLYSACCHARIDES, GLYCOCONJUGATES
Abstract

Mannosidases catalyze the hydrolysis of a diverse range of polysaccharides and glycoconjugates, and the various sequence-based mannosidase families have evolved ingenious strategies to overcome the stereoelectronic challenges of mannoside chemistry. Using a combination of computational chemistry, inhibitor design and synthesis, and X-ray crystallography of inhibitor/enzyme complexes, it is demonstrated that mannoimidazole-type inhibitors are energetically poised to report faithfully on mannosidase transition-state conformation, and provide direct evidence for the conformational itinerary used by diverse mannosidases, including β-mannanases from families GH26 and GH113. Isofagomine-type inhibitors are poor mimics of transition-state conformation, owing to the high energy barriers that must be crossed to attain mechanistically relevant conformations, however, these sugar-shaped heterocycles allow the acquisition of ternary complexes that span the active site, thus providing valuable insight into active-site residues involved in substrate recognition. [ABSTRACT FROM AUTHOR]

Published
2014
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