Cornish-Bowden Principles of Enzyme Kinetics

1. Auflage 2014
ISBN: 978-1-4831-6467-0
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 220 Seiten, Web PDF

Principles of Enzyme Kinetics discusses the principles of enzyme kinetics at an intermediate level. It is primarily written for first-year research students in enzyme kinetics. The book is composed of 10 chapters. Chapter 1 provides the basic principles of enzyme kinetics with a brief discussion of dimensional analysis. Subsequent chapters cover topics on the essential characteristics of steady-state kinetics, temperature dependence, methods for deriving steady-state rate equations, and control of enzyme activity. Integrated rate equations, and introductions to the study of fast reactions and the statistical aspects of enzyme kinetics are provided as well. Chemists and biochemists will find the book invaluable.

Autoren/Hrsg.

Cornish-Bowden, Athel

Inhaltsverzeichnis

1;Front Cover;1
2;Principles of Enzyme Kinetics;4
3;Copyright Page;5
4;Table of Contents;8
5;Foreword;6
6;Preface;12
7;Chapter 1. Basic Principles of Chemical Kinetics;16
7.1;1.1 Order of reaction;16
7.2;1.2 Determination of the order of a reaction;19
7.3;1.3 Dimensions of rate constants;19
7.4;1.4 Reversible reactions;20
7.5;1.5 Determination of first-order rate constants;22
7.6;1.6 Influence of temperature on rate constants;24
7.7;1.7 Transition-state theory;26
8;Chapter 2. Introduction to Enzyme Kinetics;29
8.1;2.1 Early studies;29
8.2;2.2 Work of Michaelis and Menten;31
8.3;2.3 Steady-state treatment;33
8.4;2.4 Validity of the steady-state assumption;36
8.5;2.5 Graphical representation of the Michaelis-Menten equation;38
8.6;2.6 Reversible Michaelis–Menten mechanism;43
8.7;2.7 Product inhibition;46
8.8;Appendix 2.1 Hyperbolic nature of the Michaelis–Menten equation;47
9;Chapter 3. How to Derive Steady-State Rate Equations;49
9.1;3.1 Introduction;49
9.2;3.2 Principle of the King–Altman method;49
9.3;3.3 Method of King and Altman;53
9.4;3.4 Modifications to the King-Altman method;56
9.5;3.5 Compression of patterns;59
9.6;3.6 Reactions containing steps at equilibrium;61
9.7;3.7 Analysing mechanisms by inspection;62
9.8;3.8 Rate equations in coefficient form;65
10;Chapter 4. Inhibitors and Activators;67
10.1;4.1 Reversible and irreversible inhibitors;67
10.2;4.2 Competitive inhibition;68
10.3;4.3 Mixed inhibition;69
10.4;4.4 Uncompetitive inhibition;71
10.5;4.5 Plotting inhibition results;72
10.6;4.6 Intuitive approach to linear inhibition;76
10.7;4.7 Hyperbolic inhibition and activation;77
10.8;4.8 Non-productive binding;79
10.9;4.9 Substrate inhibition;81
10.10;4.10 Inhibitors of high affinity;83
11;Chapter 5. Reaction Pathways;86
11.1;5.1 Introduction;86
11.2;5.2 Survey of two-substrate, two-product reaction mechanisms;87
11.3;5.3 Nomenclature and schematic representation of mechanisms;93
11.4;5.4 Rate equations;95
11.5;5.5 Initial-velocity measurements in absence of products;98
11.6;5.6 Substrate inhibition;102
11.7;5.7 Reverse reaction;105
11.8;5.8 Product inhibition;107
11.9;5.9 Isotope exchange;109
11.10;5.10 Induced transport;112
12;Chapter 6. Effects of pH and Temperature on Enzymes;116
12.1;6.1 pH and enzyme kinetics;116
12.2;6.2 Ionization of a dibasic acid;117
12.3;6.3 Effect of pH on enzyme kinetic constants;121
12.4;6.4 pH independence of Km;122
12.5;6.5 Ionization of groups remote from the active site;124
12.6;6.6 Change of rate-determining step with pH;125
12.7;6.7 Temperature dependence of enzyme-catalysed reactions;126
12.8;6.8 Use of temperature for studying enzyme specificity;129
13;Chapter 7. Control of Enzyme Activity;131
13.1;7.1 Necessity for metabolic control;131
13.2;7.2 Binding of oxygen to haemoglobin;133
13.3;7.3 Hill equation;135
13.4;7.4 Adair equation;138
13.5;7.5 Pauling's treatment;140
13.6;7.6 Induced fit;142
13.7;7.7 Symmetry model of Monod, Wyman and Changeux;143
13.8;7.8 Sequential model of Koshland, Nemethy and Filmer;148
13.9;7.9 Half-of-the-sites reactivity;154
13.10;7.10 Other equilibrium models of co-operativity;154
13.11;7.11 Kinetic models of co-operativity;155
14;Chapter 8. Analysis of Progress Curves;157
14.1;8.1 Integrated rate equations;157
14.2;8.2 Integrated Michaelis—Menten equation;158
14.3;8.3 Competitive product inhibition;159
14.4;8.4 Inhibition by several products;161
14.5;8.5 Mixed inhibition by products;162
14.6;8.6 More complex cases;164
14.7;8.7 Some pitfalls;165
15;Chapter 9. Fast Reactions;168
15.1;9.1 Limitations of steady-state measurements;168
15.2;9.2 Transient phase of the Michaelis—Menten mechanism;170
15.3;9.3 'Burst' kinetics;171
15.4;9.4 Reversible sequences of reactions;175
15.5;9.5 Jump kinetics;177
15.6;9.6 Sinusoidal perturbations;179
16;Chapter 10. Estimation of Rate Constants;183
16.1;10.1 Value and limitations of a statistical approach;183
16.2;10.2 Variance;185
16.3;10.3 Simple linear regression;188
16.4;10.4 Fitting the Michaelis–Menten equation;192
16.5;10.5 Final comments at the double-reciprocal plot;196
16.6;10.6 Standard errors of V and Km;197
16.7;10.7 General linear model and applications to more complex cases;199
16.8;10.8 Some difficulties in fitting data;201
16.9;10.9 Statistical aspects of the direct linear plot;204
16.10;10.10 Final note;208
17;References;209
18;Index;214