Essential Enzyme Kinetics: A Textbook for Molecular Life Scientists describes the theoretical basis and best-practice approaches for using initial-rate, fast reaction, and kinetic isotope effect experiments to define enzyme catalysis. Because a detailed knowledge of enzyme transition-states is the main driver for the rational design of slow, tight-binding inhibitors destined to become tomorrow's small-molecule drugs, Essential Enzyme Kinetics is the must-have reference for chemists, biochemists, and pharmacologists intent on pursuing careers in Big Pharma. Given the interdisciplinary nature of contemporary drug development, this book provides a lucid short-course that will also benefit nonspecialists seeking to understand the scope and reach of modern enzyme kinetics.
Table of Contents
1. Introduction 2. Basic Chemical Kinetics 3. Initial-Rate Kinetics of One-Substrate Enzymes 4. Measuring Initial Velocities of Enzyme-catalyzed Reactions 5. Multi-substrate Enzyme Kinetic Mechanisms 6. Fast Kinetic Techniques for Probing Enzyme-Catalyzed Reactions 7. Factors Affecting Enzyme Rates 8. Kinetic Isotope Effects 9. Inhibitor Effects on Enzyme-Catalyzed Reactions 10. Enzyme Cooperativity 11. Kinetics of Force-Generating Enzymes