First published in 1990, this comprehensive monograph consists of two parts: Volume I, entitled Enzyme Catalysis, Kinetics, and Substrate Binding; and Volume II, entitled Mechanism of Enzyme Action. Volume I focuses on several aspects of enzyme catalytic behavior, their steady-state and transient-state kinetics, and the thermodynamic properties of substrate binding. Packed with figures, tables, schemes, and photographs, this volume contains over 1,000 references, including references regarding enzymology's fascinating history. This comprehensive book is of particular interest to enzymology students, teachers, and researchers.
Volume II presents selected "cutting edge" examples of techniques and approaches being pursued in biochemistry. This up-to-date resource includes 11 chapters, which illustrate important theoretical and practical aspects of enzyme mechanisms. It also features selected examples in which today's most important techniques, ideas, and theories are used to elaborate on the intricate nature of enzyme action mechanisms. This particular volume provides important information for both the novice and the seasoned investigator.
Table of Contents
Enzyme Catalysis and Steady-State Kinetics: Historical Introduction, Theories of Enzyme Catalysis, and Some Elementary Considerations of Enzyme Kinetics. A Description of Steady-State Kinetics and Quasi- or Rapid Equilibrium Kinetics by a Development of the Rate Expressions for Several Selected Mechanisms and Their Characteristics. Inhibition and Product Inhibition. Effects of pH and Temperature. Effect of Metal Cofactors on the Reaction Velocity. Enzyme Kinetics and Substrate Binding: Some Remarks on Isotope Exchange Studies and Kinetic Isotope Effects. Non-Michaelis-Menten Kinetics and Allosteric Kinetics. Equilibrium Ligand Binding-Multiple Equilibria. Some Complex Kinetic Mechanisms and Treatment of Enzyme Kinetic Data. Kinetics of the Transient Phase or Pre-Steady-State Phase of Enzyme Reactions. Appendix 1. Appendix 2. References. Index.