Enzyme Kinetics. Catalysis & Control. a Reference of Theory and Best-Practice Methods

Description

Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, Enzyme Kinetics: Catalysis & Control develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes.

Contents

An Introduction to Enzyme Rate Processes
Active Sites & Their Chemical Properties
Fundamentals of Chemical Kinetics
Practical Aspects of Measuring Rates & Kinetic
Initial-Rate Kinetics of One-Substrate Enzyme-Catalyzed Reactions
Initial-Rate Kinetics of Multi-Substrate Enzyme-Catalyzed Reactions
Other Factors Influencing Enzyme Activity
Kinetic Behavior of Enzyme Inhibitors
Isotopic Probes of Biological Catalysis
Probing Fast Enzyme Processes
Regulatory Behavior of Enzymes
Single-Molecule Enzyme Kinetics
Force Generation in Mechanoenzyme Catalysis
On Keeping a Research Notebook
Steady-State Rate Equations for Selected One- & Two-Substrate Enzyme-Catalyzed Reactions
Summary of Enzyme Kinetic Mechanisms Abbreviations & Symbols References

Author Information

By Daniel L. Purich, Professor of Biochemistry & Molecular Biology University of Florida Health Science Center