A unified theory of enzyme kinetics based upon the systematic analysis of the variations of kcat, KM, and kcat/KM and the relevant ΔG0≠ values—possible implications in chemotherapy and biotechnology
- 1 May 2001
- journal article
- review article
- Published by Elsevier in Biochemical Pharmacology
- Vol. 61 (9) , 1049-1055
- https://doi.org/10.1016/s0006-2952(01)00579-2
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Metal−Substrate Interactions Facilitate the Catalytic Activity of the Bacterial PhosphotriesteraseBiochemistry, 1996
- Identification of Functional Cysteine Residues in Human GalactosyltransferaseBiochemical and Biophysical Research Communications, 1994
- Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetaseNature, 1991
- Engineering a novel β-Iactamase by a single point mutationProtein Engineering, Design and Selection, 1990
- Redesign of the coenzyme specificity of a dehydrogenase by protein engineeringNature, 1990
- Evolutionary optimization of the catalytic effectiveness of an enzymeBiochemistry, 1989
- Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinaseBiochemistry, 1989
- Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residueNature, 1989
- Enhanced Activity and Altered Specificity of Phospholipase A 2 by Deletion of a Surface LoopScience, 1989
- Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated, and oversaturated regimesBiochemistry, 1986