Simple model for the effect of Glu165 → Asp165 mutation on the rate of catalysis in triose phosphate isomerase
- 1 September 1986
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 191 (1), 23-27
- https://doi.org/10.1016/0022-2836(86)90419-5
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
- Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme.Proceedings of the National Academy of Sciences, 1985
- Quantum mechanical and molecular mechanical studies on a model for the dihydroxyacetone phosphate-glyceraldehyde phosphate isomerization catalyzed by triose phosphate isomerase (TIM)Journal of the American Chemical Society, 1984
- Theoretical calculations on proton-transfer energetics: studies of methanol, imidazole, formic acid, and methaneethiol as models for the serine and cysteine proteasesJournal of the American Chemical Society, 1981
- Proton transfers in hydrogen-bonded systems. 2. Electron correlation effects in diamminehydrogen(1+)Journal of the American Chemical Society, 1981
- Evolution of enzyme function and the development of catalytic efficiencyBiochemistry, 1976
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence dataNature, 1975