Enzyme Kinetics and Mechanism

Book Summary

Enzyme Kinetics and Mechanism is a comprehensive textbook on steady-state enzyme kinetics.  Organized according to the experimental process, the text covers kinetic mechanism, relative rates of steps along the reaction pathway, and chemical mechanism—including acid-base chemistry and transition state structure. 

Practical examples taken from the literature demonstrate theory throughout.  The book also features numerous general experimental protocols and how-to explanations for interpreting kinetic data. 

Written in clear, accessible language, the book will enable graduate students well-versed in biochemistry to understand and describe data at the fundamental level.  Enzymologists and molecular biologists will find the text a useful reference.

1. Nomenclature  
2. Introduction to Kinetics 
3. Enzyme Assays  
4. Derivation of Initial Velocity Rate Equations and Data Processing  
5. Initial Velocity Studies in the Absence of Added Inhibitors  
6. Initial Velocity Studies: Presence of Added Inhibitors  
7. Pre-Steady State and Relaxation Kinetics  
8. Isotopic Probes of Kinetic Mechanism  
9. Isotope Effects as a Probe of Mechanism  
10. pH Dependence of Kinetic Parameters and Isotope Effects 
Appendix I. King and Altman Patterns and Distribution Equations 
Appendix II. Rate Equations, Definitions of Kinetic and Inhibition Constants, Haldanes, Distribution Equations and Rate Constants for a Number of Multireactant Mechanisms