Evolution of Enzyme Function and the Development of Catalytic Efficiency: Triosephosphate Isomerase, Jeremy R. Knowles, and W. John Albery
Author:
Affiliation:
1. Departments of Biochemistry and Chemistry and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00211
Reference56 articles.
1. Deuterium and tritium exchange in enzyme kinetics
2. Energetics of triosephosphate isomerase: the fate of the 1(R)-3H label of tritiated dihydroxyacetone phosphate in the isomerase reaction
3. Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product
4. Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in product
5. Energetics of triosephosphate isomerase: the nature of the proton transfer between the catalytic base and solvent water
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