This book provides a systematic introduction to the field of enzyme-catalyzed reactions. 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 content develops from monosubstrate to bisubstrate to trisubstrate reactions, concluding with nonhyperbolic rate equations and allosteric and cooperative effects.

Comprehensive Enzyme Kinetics also 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.

Features:

• A wide range of topics that constitute the modern enzyme kinetics
  
• The work of Michaelis and Menten
  
• Information on all topics in the various areas of kinetics
  
• and More!

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

Index

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