Enzymes
A Practical Introduction to Structure, Mechanism, and Data Analysis
(Sprache: Englisch)
ENZYMES
A complete and approachable introduction to the study of enzymes, from theory to practice
Enzymes catalyze the bulk of important biological processes, both metabolic and biochemical. They are specialized proteins whose function is...
A complete and approachable introduction to the study of enzymes, from theory to practice
Enzymes catalyze the bulk of important biological processes, both metabolic and biochemical. They are specialized proteins whose function is...
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ENZYMESA complete and approachable introduction to the study of enzymes, from theory to practice
Enzymes catalyze the bulk of important biological processes, both metabolic and biochemical. They are specialized proteins whose function is determined by their structure, understanding which is therefore a key focus of biological, pharmacological, and agrarian research, among many others. A thorough knowledge of enzyme structure, pathways, and mechanisms is a fundamental building block of the life sciences and all others connected to them.
Enzymes offers a detailed introduction to this critical subject. It analyzes enzyme proteins at the structural level and details the mechanisms by which they perform their catalyzing functions. The book's in-depth engagement with primary literature and up-to-date research allows it to continuously deploy illustrative examples and connect readers with further research on key subjects. Fully updated after decades as the standard text, this book unlocks a thriving field of biological and biochemical research.
Readers of the third edition of Enzymes will also find:
* Expanded chapters on steady-state and transient-state enzyme kinetics, structural components of enzymes, and more
* New chapters on enzyme regulation, enzyme-macromolecule interactions, enzyme evolution, and enzymes in human health
* Key Learning Points at the beginning of each chapter to assist students and instructors
Enzymes promises to continue as the standard reference on this subject for practitioners of the life sciences and related fields in both academia and industry.
Inhaltsverzeichnis zu „Enzymes “
Preface to the Third Edition xviiPreface to the Second Edition xix
Preface to the First Edition xxi
Acknowledgments xxiii
1 A Brief History of Enzymology 1
Key Learning Points 1
1.1 Enzymes in Antiquity 2
1.2 Early Enzymology 3
1.3 The Development of Mechanistic Enzymology 4
1.4 Studies of Enzyme Structure 5
1.5 Enzymology Today 7
1.6 Summary 9
References and Further Reading 9
2 Chemical Bonds and Reactions in Biochemistry 11
Key Learning Points 11
2.1 Atomic and Molecular Orbitals 12
2.2 Thermodynamics of Chemical Reactions 22
2.3 Acid-base Chemistry 27
2.4 Noncovalent Interactions in Reversible Binding 29
2.5 Rates of Chemical Reactions 33
2.6 Summary 38
References and Further Reading 38
3 Structural Components of Enzymes 39
Key Learning Points 39
3.1 The Amino Acids 40
3.2 The Peptide Bond 48
3.3 Amino Acid Sequence or Primary Structure 51
3.4 Secondary Structure 54
3.5 Tertiary Structure 60
3.6 Subunits and Quaternary Structure 64
3.7 Cofactors in Enzymes 67
3.8 Conformational Dynamics and Enzyme Function 70
3.9 Methods of Protein Structure Determination 75
3.10 Summary 79
References and Further Reading 80
4 Protein-Ligand Binding Equilibria 83
Key Learnings Points 83
4.1 The Equilibrium Dissociation Constant, K d 84
4.2 The Kinetic Approach to Equilibrium 86
4.3 Binding Measurements at Equilibrium 88
4.4 Graphic Analysis of Equilibrium Ligand-Binding Data 94
4.5 Equilibrium Binding with Ligand Depletion (Tight Binding Interactions) 100
4.6 Competition Among Ligands for a Common Binding Site 101
4.7 Protein Dynamics in Receptor-Ligand Binding 102
4.8 Orthosteric and
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Allosteric Ligand Binding Sites 104
4.9 Experimental Methods for Measuring Ligand Binding 105
4.10 Summary 122
References and Further Reading 122
5 Steady-State Kinetics of Single-Substrate Enzyme Reactions 125
Key Learning Points 125
5.1 The Time Course of Enzymatic Reactions 126
5.2 Effects of Substrate Concentration on Velocity 127
5.3 The Rapid Equilibrium Model of Enzyme Kinetics 129
5.4 The Steady-State Model of Enzyme Kinetics 131
5.5 The Significance of k cat and K m 134
5.6 Experimental Measurement of k cat and K m 139
5.7 Other Linear Transformations of Enzyme Kinetic Data 147
5.8 Measurements at Low Substrate Concentrations 149
5.9 Deviations From Hyperbolic Kinetics 150
5.10 Summary 153
References and Further Reading 153
6 Chemical Mechanisms in Enzyme Catalysis 155
Key Learning Points 155
6.1 Substrate-Active Site Complementarity 156
6.2 Rate Enhancement Through Transition State Stabilization 159
6.3 Chemical Mechanisms for Transition State Stabilization 162
6.4 The Serine Proteases: An Illustrative Example 182
6.5 Enzymatic Reaction Nomenclature 187
6.6 Summary 191
References and Further Reading 191
7 Experimental Measures of Steady-State Enzyme Activity 193
Key Learning Points 193
7.1 Initial Velocity Measurements 194
7.2 Detection Methods 208
7.3 Separation Methods in Enzyme Assays 224
7.4 Factors Affecting the Velocity of Enzymatic Reactions 236
7.5 Reporting Enzyme Activity
4.9 Experimental Methods for Measuring Ligand Binding 105
4.10 Summary 122
References and Further Reading 122
5 Steady-State Kinetics of Single-Substrate Enzyme Reactions 125
Key Learning Points 125
5.1 The Time Course of Enzymatic Reactions 126
5.2 Effects of Substrate Concentration on Velocity 127
5.3 The Rapid Equilibrium Model of Enzyme Kinetics 129
5.4 The Steady-State Model of Enzyme Kinetics 131
5.5 The Significance of k cat and K m 134
5.6 Experimental Measurement of k cat and K m 139
5.7 Other Linear Transformations of Enzyme Kinetic Data 147
5.8 Measurements at Low Substrate Concentrations 149
5.9 Deviations From Hyperbolic Kinetics 150
5.10 Summary 153
References and Further Reading 153
6 Chemical Mechanisms in Enzyme Catalysis 155
Key Learning Points 155
6.1 Substrate-Active Site Complementarity 156
6.2 Rate Enhancement Through Transition State Stabilization 159
6.3 Chemical Mechanisms for Transition State Stabilization 162
6.4 The Serine Proteases: An Illustrative Example 182
6.5 Enzymatic Reaction Nomenclature 187
6.6 Summary 191
References and Further Reading 191
7 Experimental Measures of Steady-State Enzyme Activity 193
Key Learning Points 193
7.1 Initial Velocity Measurements 194
7.2 Detection Methods 208
7.3 Separation Methods in Enzyme Assays 224
7.4 Factors Affecting the Velocity of Enzymatic Reactions 236
7.5 Reporting Enzyme Activity
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Autoren-Porträt von Robert A. Copeland
Robert A. Copeland, PhD, is founder, President, and Chief Scientific Officer (CSO) of Accent Therapeutics, Inc. and the President of Ki Consultant, LLC. Previously, he was President of Research and CSO of Epizyme, Inc., and Vice President for Cancer Biology at the Oncology Center of Excellence in Drug Discovery for GlaxoSmithKline. He is a fellow of the American Association for the Advancement of Science and the Royal Society of Chemistry, and has published very widely on enzymes and related subjects.
Bibliographische Angaben
- Autor: Robert A. Copeland
- 2023, 3. Aufl., 576 Seiten, Maße: 18,3 x 26 cm, Gebunden, Englisch
- Verlag: Wiley & Sons
- ISBN-10: 1119793254
- ISBN-13: 9781119793250
- Erscheinungsdatum: 08.02.2023
Sprache:
Englisch
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