Effect of Asp122 Mutation on the Hydride Transfer in E. coli DHFR Demonstrates the Goldilocks of Enzyme Flexibility
Author:
Affiliation:
1. Department of Chemistry and the Lise Meitner-Minerva Center of Computational Quantum Chemistry, Bar-Ilan University, Ramat-Gan 52900, Israel
2. Department of Chemistry, University of Iowa, Iowa City, Iowa 52242, United States
Funder
United States-Israel Binational Science Foundation
Israel Science Foundation
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b05556
Reference101 articles.
1. Energetics of enzyme catalysis.
2. Electrostatic Basis for Enzyme Catalysis
3. A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis
4. Evidence that a ‘dynamic knockout’ in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis
5. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
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