A Buried Water Molecule Influences Reactivity in α-Amylase on a Subnanosecond Time Scale
Author:
Affiliation:
1. UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007 Porto, Portugal
Funder
European Commission
Minist?rio da Educa??o e Ci?ncia
Publisher
American Chemical Society (ACS)
Subject
Catalysis,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acscatal.7b04400
Reference57 articles.
1. Comparison of Formation of Reactive Conformers (NACs) for the Claisen Rearrangement of Chorismate to Prephenate in Water and in the E. coli Mutase: The Efficiency of the Enzyme Catalysis
2. The catalytic power of enzymes: Conformational selection or transition state stabilization?
3. Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism
4. The near attack conformation approach to the study of the chorismate to prephenate reaction
5. Computing the Role of Near Attack Conformations in an Enzyme-Catalyzed Nucleophilic Bimolecular Reaction
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