Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate Isomerase
Author:
Affiliation:
1. Science for Life Laboratory, Department of Chemistry − BMC, Uppsala University, BMC, Box 576, S-751 23 Uppsala, Sweden
2. Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States
Funder
Vetenskapsr?det
Knut och Alice Wallenbergs Stiftelse
Human Frontier Science Program
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
http://pubs.acs.org/doi/pdf/10.1021/jacs.9b08713
Reference107 articles.
1. Quantum mechanical and molecular mechanical studies on a model for the dihydroxyacetone phosphate-glyceraldehyde phosphate isomerization catalyzed by triose phosphate isomerase (TIM)
2. Simple model for the effect of Glu165 → Asp165 mutation on the rate of catalysis in triose phosphate isomerase
3. Molecular dynamics simulations of “loop closing” in the enzyme triose phosphate isomerase
4. Molecular dynamics simulations of active site mutants of triosephosphate isomerase
5. Anatomy of a Conformational Change: Hinged "Lid" Motion of the Triosephosphate Isomerase Loop
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