Enzyme Kinetics and Mechanism

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. Nomenclature2. Introduction to Kinetics 3. Enzyme Assays4. Derivation of Initial Velocity Rate Equations and Data Processing5. Initial Velocity Studies in the Absence of Added Inhibitors6. Initial Velocity Studies: Presence of Added Inhibitors7. Pre-Steady State and Relaxation Kinetics8. Isotopic Probes of Kinetic Mechanism9. Isotope Effects as a Probe of Mechanism10. 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

Paul F. Cook is the Grace B. Kerr Centennial Professor of Chemistry and Biochemistry at the University of Oklahoma. His awards and achievements twice included the Alexander von Humboldt Research Fellowship and he was the recipient of the National Institutes of Health Research Career Development Award from 1983 to 1988. Professor Cook is Associate Editor of Protein and Peptide Letters and Executive Editor of Proteins and Proteomics. W.W. Cleland is the M.J. Johnson Professor and Steenbock Professor of Chemical Science at the Enzyme Institute at University of Wisconsin-Madison. In the early 1960s, Cleland's landmark papers created a theoretical framework for the study of steady-state kinetics of multisubstrate enzymes and laid the foundation for all subsequent steady-state studies. He serves on the editorial boards of Journal of Biological Chemistry and of Biochemistry. Recognized by many as the "father of modern enzyme kinetics," Professor Cleland was elected to the National Academy of Sciences in 1985.