Synopses & Reviews
This book provides a systematic introduction to the field of enzyme-catalyzed reactions. The content develops from monosubstrate to bisubstrate to trisubstrate reactions, concluding with nonhyperbolic rate equations and allosteric and cooperative effects. Because it outlines the subject in such a way that it builds from less complicated to more demanding kinetic models, it can be used as a textbook for students of biochemistry and molecular biology. The author stresses the importance of graphical representation of kinetic models by frequent use of such mathematical models in the form of double-reciprocal plots. In addition, special attention is paid to isotope exchange studies, kinetic isotope effects, and the statistical evaluation of initial rate and ligand binding data.
Table of Contents
1. Introduction.- 2. Chemical kinetics.- 3. Kinetics of monosubstrate reactions.- 4. Derivations of rate equations.- 5. Linear inhibition.- 6. Hyperbolic and parabolic inhibition.- 7. Enzyme activation.- 8. Kinetics of rapid equilibrium bisubstrate reactions.- 9. Steady state kinetics of bisubstrate reactions.- 10. Kinetic analysis of bisubstrate mechanisms.- 11. Substrate inhibition and mixed dead-end and product inhibition.- 12. Kinetics of trisubstrate reactions.- 13. Cooperative and allosteric effects.- 14. The pH dependence of enzyme catalysis.- 15. Effects of temperature on enzyme reactions.- 16. Isotope exchange.- 17. Solvent and kinetic isotope effects.- 18. Statistical analysis of initial rate and binding data.- Subject index.