Enzyme Kinetics And Mechanism

Enzyme Kinetics and Mechanism is a comprehensive textbook on steady-state enzyme kinetics. Organized according to the experimental process, the text covers kinetic mechanism, relative rates of steps along the reaction pathway, and chemical mechanism—including acid-base chemistry and transition state structure. Practical examples taken from the literature demonstrate theory throughout. The book also features numerous general experimental protocols and how-to explanations for interpreting kinetic data. Written in clear, accessible language, the book will enable graduate students well-versed in biochemistry to understand and describe data at the fundamental level. Enzymologists and molecular biologists will find the text a useful reference.

Selected Methods in Enzymology: Contemporary Enzyme Kinetics and Mechanism provides an introduction to enzyme kinetics and mechanism at an intermediate level. This book covers a variety of topics, including temperature effects in enzyme kinetics, cryoenzymology, substrate inhibition, enol intermediates enzymology, and heavy-atom isotope effects. Organized into 19 chapters, this book begins with an overview of derivation of rate equations as an integral part of the effective usage of kinetics as a tool. This text then examines the practical aspects of initial rate enzyme assay. Other chapters consider the basic procedures used in making decisions concerning kinetic mechanisms from initial-rate data. This book discusses as well the various aspects of both the theoretical background and the applications. The final chapter deals with the importance of achieving proficiency in formulating quantitative relationships describing enzyme behavior. This book is a valuable resource for students and research workers. Enzymologists and chemists will also find this book useful.

Enzyme Kinetics and Mechanisms takes the reader through the experimental techniques and the logic by which the mechanisms of enzyme-catalyzed reactions can be elucidated by the results of steady-state kinetics and related experiments. It is meant to make these investigations both satisfying and effective. In distinction to other available descriptions, the descriptions in enzyme Kinetics and Mechanisms are limited to more commonly utilized and useful models and techniques. The logic relating the chemical models to the mathematical models and the logic of relating the mathematical models to data is presented in rather concise text, figures and equations. The development of mathematical models from chemical models is done by a unique algorithm that is both simple and quick, and the same concept are utilized to develop models for the effects of a variety of reaction conditions on the initial velocity. In addition, the various relationships of data, mathematical models and the chemical models is illustrated with examples from the scientific literature.

This enzymology textbook for graduate and advanced undergraduate students covers the syllabi of most universities where this subject is regularly taught. It focuses on the synchrony between the two broad mechanistic facets of enzymology: the chemical and the kinetic, and also highlights the synergy between enzyme structure and mechanism. Designed for self-study, it explains how to plan enzyme experiments and subsequently analyze the data collected. The book is divided into five major sections: 1] Introduction to enzymes, 2] Practical aspects, 3] Kinetic Mechanisms, 4] Chemical Mechanisms, and 5] Enzymology Frontiers. Individual concepts are treated as stand-alone chapters; readers can explore any single concept with minimal cross-referencing to the rest of the book. Further, complex approaches requiring specialized techniques and involved experimentation (beyond the reach of an average laboratory) are covered in theory with suitable references to guide readers. The book provides students, researchers and academics in the broad area of biology with a sound theoretical and practical knowledge of enzymes. It also caters to those who do not have a practicing enzymologist to teach them the subject.

The kinetic mechanisms by which enzymes interact with inhibitors and activators, collectively called modifiers, are scrutinized and ranked taxonomically into autonomous species in a way similar to that used in the biological classification of plants and animals. The systematization of the mechanisms is based on two fundamental characters: the allosteric linkage between substrate and modifier and the factor by which a modifier affects the catalytic constant of the enzyme. Combinations of the physically significant states of these two characters in an ancestor-descendant-like fashion reveal the existence of seventeen modes of interaction that cover the needs of total, partial and fine-tuning modulation of enzyme activity. These interactions comprise five linear and five hyperbolic inhibition mechanisms, five nonessential activation mechanisms and two hybrid species that manifest either hyperbolic inhibition or nonessential activation characteristics depending on substrate concentration. Five essential activation mechanisms, which are taxonomically independent of the mentioned basic species, complete the inventory of enzyme modifiers. Often masked under conventional umbrella terms or treated as anomalous cases, all seventeen basic inhibition and nonessential activation mechanisms are represented in the biochemical and pharmacological literature of this and the past century, either in the form of rapid or slow-onset reversible interactions, or as irreversible modification processes. The full potential of enzyme inhibitors and activators can only be appreciated after elucidating the details of their kinetic mechanisms of action exploring the entire range of physiologically significant reactant concentrations. This book highlights the wide spectrum of allosteric enzyme modification in physiological occurrences as well as in pharmacological and biotechnological applications that embrace simple and multiple enzyme-modifier interactions. The reader is guided in the journey through this still partly uncharted territory with the aid of mechanistically-oriented criteria aimed at showing the logical way towards the identification of a particular mechanism.

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.

Enzyme kinetics has undergone very rapid growth and development during the past fifteen years and has been well received by the biochemical community. A cursory glance at the current biochem ical literature reveals the increasing popularity of enzyme ki netics1 yet, there are very few books available to guide the enzymologist who wishes to conduct kinetic experiments. This monograph was undertaken to provide the fledgling kineticist with an outline of contemporary initial rate enzyme kinetics. A large portion of the material contained in this book is presented in a second-year, graduate-level course in biochemistry at Iowa State University. I have found that the presentation in this course has enabled students without a strong background in math ematics to undertake initial rate studies at the research bench. The monograph obviously is more comprehensive than any course could be, and should permit similar accomplishment. As the title implies, the major emphasis of this monograph is on initial rate enzyme kinetics. I considered at length the advis ability of including chapters on integrated rate equations and on the theory and application of rapid reaction kinetics, such as rapid-mixing stopped-flow, and temperature-jump kinetics. These, however, are topics that would require a good deal of space to develop if they were to be helpful to the beginner.

Principles of Enzyme Kinetics discusses the principles of enzyme kinetics at an intermediate level. It is primarily written for first-year research students in enzyme kinetics. The book is composed of 10 chapters. Chapter 1 provides the basic principles of enzyme kinetics with a brief discussion of dimensional analysis. Subsequent chapters cover topics on the essential characteristics of steady-state kinetics, temperature dependence, methods for deriving steady-state rate equations, and control of enzyme activity. Integrated rate equations, and introductions to the study of fast reactions and the statistical aspects of enzyme kinetics are provided as well. Chemists and biochemists will find the book invaluable.