Enzyme Kinetics: From Diastase to Multi-enzyme Systemsby Arthur R. Schulz
Pub. Date: 06/28/2003
Publisher: Cambridge University Press
This textbook for advanced courses in enzyme chemistry and enzyme kinetics covers the field of steady-state enzyme kinetics from the basic principles inherent in the Henri equation to the expressions that describe the control of multi-enzyme pathways. Steady-state kinetic equations are derived with the use of the connection matrix method, and an algorithm is developed that can be implemented easily for computer-based derivation of the equations. Throughout the book emphasis is placed on a proper interpretation of the kinetic behavior of multi-reactant enzymic reactions and on the interpretation of control coefficients in terms of metabolic control. Problems are included at the end of each chapter and their solutions are found at the end of the book.
- Cambridge University Press
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Table of ContentsPreface; 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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