Enzyme Kinetics From Diastase to Multi-Enzyme Systems

About this book

This text covers the field of steady-state kinetics from basic principles to the control of the multi-enzyme systems which constitute metabolic pathways. Emphasis is placed on the interpretation of the kinetic behaviour of enzyme-catalyzed reactions in terms of mechanisms. Algorithms are developed which can be implemented in computer programs for the derivation of equations. The treatment of steady-state enzyme kinetics is extended to allosteric enzymes and subunit interactions in polymeric enzymes. Principles are presented which provide for mathematical analysis of the control of multi-enzyme systems. Problems are included at the end of each chapter and their solutions are found at the end of the book. This book will be a useful text for advanced undergraduates and graduate students taking courses in enzyme chemistry and enzyme kinetics.

Contents

Preface; Part I. Basic Steady State Enzyme Kinetics: 1. Derivation of a rate equation; 2. A closer look at the basic assumptions; 3. Enzyme inhibition; 4. Reversible enzyme-catalyzed reactions; Part II. Enzyme Reaction Sequence: 5. Multi-reactant enzymic reactions; 6. Analysis of multi-reactant enzyme kinetics; 7. Prediction of reaction sequence; 8. Enzyme-catalyzed isotopic exchange; 9. Kinetic isotope effect on steady state parameters; 10. The effect of pH on enzyme kinetics; Part III. Non-Hyperbolic Enzyme Kinetics: 11. The causes of non-hyperbolic enzyme kinetics; 12. Analysis of non-hyperbolic enzyme kinetics; 13. The effect of subunit interactions on enzyme kinetics; Part IV. Control of Multi-Enzyme Systems: 14. Control of linear multi-enzyme systems; 15. Control of branched multi-enzyme systems; 16. Biochemical systems theory; Part V. Solutions To Problems: Author index; Subject index.

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