Enzyme Catalysis and Regulation
- 1st Edition - January 28, 1982
- Imprint: Academic Press
- Author: Gorden Hammes
- Language: English
- Paperback ISBN:9 7 8 - 0 - 1 2 - 4 3 3 5 0 5 - 9
- eBook ISBN:9 7 8 - 0 - 3 2 3 - 1 5 8 1 7 - 6
Enzyme Catalysis and Regulation is an introduction to enzyme catalysis and regulation and covers topics ranging from protein structure and dynamics to steady-state enzyme kinetics,… Read more
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Request a sales quoteEnzyme Catalysis and Regulation is an introduction to enzyme catalysis and regulation and covers topics ranging from protein structure and dynamics to steady-state enzyme kinetics, multienzyme complexes, and membrane-bound enzymes. Case studies of selected enzyme mechanisms are also presented. This book consists of 11 chapters and begins with a brief overview of enzyme structure, followed by a discussion on methods of probing enzyme structure such as X-ray crystallography and optical spectroscopy. Kinetic methods are then described, with emphasis on the general principles of steady-state and transient kinetics. The chemical principles involved in enzyme catalysis are also discussed, and case studies of a few well-documented enzymes are presented. The regulation of enzyme activity is analyzed from a nongenetic viewpoint, with particular reference to binding isotherms and models for allosterism. Two particular enzymes, aspartate transcarbamoylase and phosphofructokinase, are used as examples of well-studied regulatory enzymes. The last two chapters focus on multienzyme complexes and membrane-bound enzymes. This monograph is intended for graduate students, advanced undergraduates, and research workers in molecular biology and biochemistry.
Preface1. Protein Structure and Dynamics References General References on Proteins and Enzymes2. Probes of Enzyme Structure Introduction Amino Acid Sequencing X-Ray Crystallography Chemical Modification Optical Spectroscopy Nuclear Magnetic Resonance Spin Labels References3. Steady-State Enzyme Kinetics Introduction Single Substrate-Single Product King-Altman Method Inhibition of Enzyme Catalysis Multiple Substrates Isotope Exchange at Equilibrium pH Dependence of Enzyme Catalysis Temperature Dependence of Enzyme Catalysis Conclusion References4. Transient Kinetic Methods for Studying Enzymes Introduction Rapid Mixing Methods Chemical Relaxation Methods General Solutions of Kinetic Equations Rate Equations near Equilibrium References5. Some Chemical Aspects of Enzyme Catalysis Catalysis Acid-Base Catalysis Nucleophilic Catalysis Electrophilic Catalysis Stereochemistry Kinetic Isotope Effects References6. Elementary Steps in Enzyme Catalysis Introduction Binding of Substrates Conformational Changes Acid-Base Catalysis Covalent Intermediates Advantages of Enzymes References7· Case Studies of Selected Enzyme Mechanisms Introduction Pancreatic Ribonuclease Chymotrypsin Lysozyme Creatine Kinase References8· Regulation of Enzyme Activity Introduction Experimental Manifestations of Regulatory Enzymes Equilibrium Binding Isotherms Molecular Models for Allosterism Steady-State Kinetics Protein Polymerization-Depolymerization Hysteretic Enzymes Transient Kinetics Conclusion References9. Case Studies of Selected Regulatory Enzymes Introduction Aspartate Transcarbamoylase Phosphofructokinase References10. Multienzyme Complexes Introduction General Mechanistic Principles Tryptophan Synthase Pyruvate and α-Ketoglutarate Dehydrogenase Fatty Acid Synthase Conclusion References11. Membrane-Bound Enzymes Introduction Membrane Structure and Function ß-Hydroxybutyrate Dehydrogenase (Na+ + K+)-Activated ATPase ATP Synthesis Adenylate Cyclase Conclusion References Appendix: Practice ProblemsIndex
- Edition: 1
- Published: January 28, 1982
- No. of pages (eBook): 276
- Imprint: Academic Press
- Language: English
- Paperback ISBN: 9780124335059
- eBook ISBN: 9780323158176
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