ENZYME KINETICS - PRINCIPLES AND METHODS

This new, expanded and updated edition of the user-friendly and comprehensive treatise on enzyme kinetics expertly balances theory and practice. With its easy-to-use program on CD-ROM containing examples allowing for the interpretation of experimental data, this is an indispensable aid for advanced students and professionals working with enzymes, whether biochemists, biotechnologists, chemical biologists, pharmacologists or bioengineers in academia, industry and clinical research.

Prof. Dr. Hans Bisswanger is currently at the Interfaculty Institute of Biochemistry at the University of T?n. He has developed and leads an intensive course on enzyme kinetics, enzyme technology and ligand binding, while his main focus is on structural and regulatory mechanisms of multi-enzyme complexes and temperature stable enzyme complexes. He is also working on the gentle immobilization of enzyme activities on synthetic surfaces, a method which has been favorably applied for the restoration of damaged documents.

Enzyme kinetics is not a new area in biochemistry. Thirty years ago, enzyme kinetics was one of the most important tools for deconstructing enzymatic mechanisms. With advances in enzyme structure determination and molecular genetics, enzyme kinetics is no longer as prominent. However, enzyme kinetics is still useful to gain insight into enzymes that are too large for NMR studies and that cannot be crystallized. Many enzymes that fit into this category are membrane bound, the kinetics of which are much more complicated. In this new edition (1st ed., 2002), Bisswanger (Univ. of Tübingen, Germany) does a nice job of extending solution enzyme kinetics to membrane-bound enzymes. Setting it apart from other works on the subject, Enzyme Kinetics does not simply deal with substrate binding as a part of the reaction kinetics, but instead devotes about one-third of the text to equilibrium binding between macromolecules and ligands in which no reaction catalysis follows the binding. This binding is then directly connected with enzyme catalyzed reaction kinetics. Enzyme Kinetics was written to serve as a graduate-level course resource and would serve this population well. The inclusion of student problems would be an improvement. Summing Up: Recommended. Graduate students, researchers, and faculty. -- L. J. Liotta, Stonehill College (Choice, February 2009)

Preface to the Second English Edition.
Preface to the First English Edition.
Symbols and Abbreviations.
Introduction and Definitions.
References.
1 Multiple Equilibria.
1.1 Diffusion.
1.2 Interaction between Macromolecules and Ligands.
1.3 Macromolecules with Identical Independent Binding Sites.
1.4 Macromolecules with Non-identical, Independent Binding Sites.
1.5 Macromolecules with Identical, Interacting Binding Sites, Cooperativity.
1.6 Non-identical, Interacting Binding Sites.
References.
2 Enzyme Kinetics.
2.1 Reaction Order.
2.2 Steady-State Kinetics and the Michaelis-Menten Equation.
2.3 Analysis of Enzyme Kinetic Data.
2.4 Reversible Enzyme Reactions.
2.5 Enzyme Inhibition.
2.6 Multi-substrate Reactions.
2.7 Derivation of Rate Equations of Complex Enzyme Mechanisms.
2.8 Kinetic Treatment of Allosteric Enzymes.
2.9 pH and Temperature Dependence of Enzymes.
2.10 Isotope Exchange.
2.11 Special Enzyme Mechanisms.
2.12 Application of Statistical Methods in Enzyme Kinetics.
References.
3 Methods.
3.1 Methods for Investigation of Multiple Equilibria.
3.2 Electrochemical Methods.
3.3 Calorimetry.
3.4 Spectroscopic Methods.
3.5 Measurement of Fast Reactions.
References.
Subject Index.