Fundamentals of Enzyme Kinetics - 1st Edition - ISBN: 9780408106177, 9781483161198

Fundamentals of Enzyme Kinetics

1st Edition

Authors: Athel Cornish-Bowden
eBook ISBN: 9781483161198
Imprint: Butterworth-Heinemann
Published Date: 11th October 1979
Page Count: 244
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Fundamentals of Enzyme Kinetics details the rate of reactions catalyzed by different enzymes and the effects of varying the conditions on them. The book includes the basic principles of chemical kinetics, especially the order of a reaction and its rate constraints. The text also gives an introduction to enzyme kinetics - the idea of an enzyme-substrate complex; the Michaelis-Menten equation; the steady state treatment; and the validity of its assumption. Practical considerations, the derivation of steady-state rate equations, inhibitors and activators, and two-substrate reactions are also explained. Problems after the end of each chapter have also been added, as well as their solutions at the end of the book, to test the readers' learning. The text is highly recommended for undergraduate students in biochemistry who wish to study about enzymes or focus completely on enzymology, as most of the mathematics used in this book, which have been explained in detail to remove most barriers of understanding, is elementary.

Table of Contents

Principal Symbols Used in this Book

1 Basic Principles of Chemical Kinetics

1.1 Order of a Reaction

1.2 Determination of the Order of a Reaction

1.3 Dimensions of Rate Constants

1.4 Reversible Reactions

1.5 Determination of First-Order Rate Constants

1.6 Influence of Temperature on Rate Constants

1.7 Transition-State Theory


2 Introduction to Enzyme Kinetics

2.1 Early Studies: The Idea of an Enzyme-Substrate Complex

2.2 Michaelis-Menten Equation

2.3 Steady-State Treatment

2.4 Validity of the Steady-State Assumption

2.5 Graphical Representation of the Michaelis-Menten Equation

2.6 Reversible Michaelis-Menten Mechanism

2.7 Product Inhibition

2.8 Integrated Michaelis-Menten Equation


3 Practical Considerations

3.1 Purification of Enzymes

3.2 Enzyme Assays

3.3 Coupled Assays

3.4 Protein Determination

3.5 Presentation of Results of a Purification

3.6 Detecting Enzyme Inactivation

3.7 Experimental Design: Choice of Substrate Concentrations

3.8 Choice of Ph, Temperature and Other Conditions

3.9 Use of Replicate Observations

3.10 Treatment of Ionic Equilibria


4 How to Derive Steady-State Rate Equations

4.1 King-Altman Method

4.2 Modifications to the King-Altman Method

4.3 Cha's Method for Reactions Containing Steps at Equilibrium

4.4 Analyzing Mechanisms by Inspection


5 Inhibitors and Activators

5.1 Reversible and Irreversible Inhibitors

5.2 Competitive Inhibition

5.3 Mixed Inhibition

5.4 Uncompetitive Inhibition

5.5 Plotting Inhibition Results

5.6 Inhibition by a Competing Substrate

5.7 Activation

5.8 Hyperbolic Inhibition and Activation

5.9 Design of Inhibition Experiments

5.10 Non-Productive Binding

5.11 Substrate Inhibition

5.12 Chemical Modification as a Means of Identifying Essential Groups


6 Two-Substrate Reactions

6.1 Introduction

6.2 Types of Mechanism

6.3 Rate Equations

6.4 Initial-Velocity Measurements in the Absence of Products

6.5 Substrate Inhibition

6.6 Product Inhibition

6.7 Design of Experiments

6.8 Isotope Exchange

6.9 Reactions with Three or More Substrates


7 Effects of pH and Temperature on Enzymes

7.1 pH and Enzyme Kinetics

7.2 Acid-Base Properties of Proteins

7.3 Ionization of a Dibasic Acid

7.4 Effect of pH on Enzyme Kinetic Constants

7.5 Ionization of the Substrate

7.6 More Complex pH Effects

7.7 Temperature Dependence of Enzyme-Catalyzed Reactions


8 Control of Enzyme Activity

8.1 Necessity for Metabolic Control

8.2 Binding of Oxygen to Hemoglobin

8.3 Hill Equation

8.4 Adair Equation

8.5 Definition of Co-operativity

8.6 Induced Fit

8.7 Symmetry Model of Monod, Wyman and Changeux

8.8 Sequential Model of Koshland, Nꮥthy and Filmer

8.9 Other Models for Co-operativity at Equilibrium

8.10 Kinetic Models of Co-operativity


9 Fast Reactions

9.1 Limitations of Steady-State Measurements

9.2 Active-Site Titration: 'Burst' Kinetics

9.3 Flow Methods

9.4 Relaxation Methods

9.5 Transient-State Kinetics of Systems Far from Equilibrium

9.6 Simplification of Complex Mechanisms

9.7 Kinetics of Systems Close to Equilibrium


10 Estimation of Kinetic Constants

10.1 Cautionary Note

10.2 Least-Squares Fit to the Michaelis-Menten Equation

10.3 Statistical Aspects of the Direct Linear Plot

10.4 Precision of Km and V Estimates

10.5 Examination of Residuals



Solutions to Problems



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About the Author

Athel Cornish-Bowden

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