Enzyme Kinetics

Book Description :

Now in full color for a more intuitive learning experience, this new edition of the long-selling reference also features a number of new developments in methodology and the application of enzyme kinetics. Starting with a description of ligand binding equilibria, the experienced author goes on to discuss simple and complex enzyme reactions in kinetic terms. Special cases such as membrane-bound and immobilized enzymes are considered, as is the influence of external conditions, such as temperature and pH value. The final part of the book then covers a range of widely used measurement methods and compares their performance and scope of application. With its unique mix of theory and practical advice, this is an invaluable aid for teaching as well as for experimental work.

Book Description :

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.

Book Description :

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.

Book Description :

Practical Enzyme Kinetics provides a practical how-to guide for beginning students, technicians, and non-specialists for evaluating enzyme kinetics using common software packages to perform easy enzymatic analyses.

Book Description :

Welcome to your study of enzyme kinetics, the subject that underlies all enzymology, which in turn underlies all aspects of biochemistry. This text will give you an introduction to a wide range of topics that constitute the modern enzyme kinetics. This textbook is directed at graduate students in biochemistry, chemistry, and life sciences, for advanced courses in enzyme kinetics, enzymology, and enzyme chemistry. For this reason, the whole book is organized in a systematic and scholarly fashion. It is unlikely that the student will be expected to cover everything in the text, but in a later career she or he may find it an invaluable reference for topics that are needed in practice. The concepts, definitions and detailed algebra of enzyme kinetics are laid out in accurate detail. For that reason, this textbook can also serve as a handbook for enzyme kinetics for research workers in the field. The research worker will find it a useful source, which can be used for solving the daily experimental problems in the laboratory. The preparation of the manuscript for this book was under the constant surveillance of W. Wallace Cleland, Professor of Chemical Science at the University of Wisconsin in Madison, and one of the founders of modern enzyme kinetics. Without his help and advice, this bookwould not be possible. Several versions of the manuscript were constantly corrected and improved by Svetlana Professor of Biochemistry at the University of Novi Sad.

Book 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. Historical analysis of kinetic principles including advanced enzyme science Provides both theoretical and practical measurements tools Coverage of single molecular kinetics Examination of force generation mechanisms Discussion of organic and inorganic enzyme reactions

Book Description :

Download Enzyme Kinetics book written by Irwin H. Segel, available in PDF, EPUB, and Kindle, or read full book online anywhere and anytime. Compatible with any devices.

Book Description :

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.

Book Description :

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.

Book Description :

Download The Physical Properties of Lysophospholipids and Enzyme Kinetics of Lysophospholipases book written by Richard E. Stafford, available in PDF, EPUB, and Kindle, or read full book online anywhere and anytime. Compatible with any devices.

Book Description :

Rapid-Equilibrium Enzyme Kinetics helps readers emphasize the estimation of kinetic parameters with the minimum number of velocity measurements, thereby reducing the amount of laboratory work necessary, and allowing more time for the consideration of complicated mechanisms. The book systematically progresses through six levels of understanding the enzyme-catalyzed reaction, and includes a CD-ROM so that the reader may use the programs in the book to input their own experimental data.

Book Description :

This book introduces fundamental concepts in kinetics that relate to system biology. Topics include basic kinetics, enzyme kinetics, generalized rate laws, gene regulation and introduction to elasticities. The text is suitable for junior/senior undergraduates and graduates who need access to information relevant to modeling biochemical pathways.

Book Description :

Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents. Contemporary Enzyme Kinetics and Mechanism, Second Edition presents key articles from Volumes 63, 64, 87, 249, 308 and 354 of Methods in Enzymology. The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics. The book will aid the reader to design, execute, and analyze kinetic experiments on enzymes. Its emphasis on enzyme inhibition will also make it attractive to pharmacologists and pharmaceutical chemists interested in rational drug design. Of the seventeen chapters presented in this new edition, ten did not previously appear in the first edition. Transient kinetic approaches to enzyme mechanisms Designing initial rate enzyme assay Deriving initial velocity and isotope exchange rate equations Plotting and statistical methods for analyzing rate data Cooperativity in enzyme function Reversible enzyme inhibitors as mechanistic probes Transition-state and multisubstrate inhibitors Affinity labeling to probe enzyme structure and function Mechanism-based enzyme inactivators Isotope exchange methods for elucidating enzymatic catalysis Kinetic isotope effects in enzyme catalysis Site-directed mutagenesis in studies of enzyme catalysis

Book Description :

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.

Book Description :

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.

Book Description :

Physical Chemistry for the Biosciences has been optimized for a one-semester introductory course in physical chemistry for students of biosciences.

Book Description :

We live in the age of science-the human and numerous other living beings' genomes have been sequenced and we are beginning to understand the capacity of the metabolic machinery responsible for life on our planet. A huge number of new genes have been discovered, a significant number of these coding for enzymes of yet obscure capacity. Understanding the kinetic behavior of an enzyme provides clues to its possible physiological role. From a biotechnological perspective, knowledge of the reactant properties of an enzyme is required for the design of immobilized enzyme-based modern processes. Biotransformations are of key importance to the pharmaceutical and sustenance industries, and knowledge of the reactant properties of enzymes, essential. This book is tied in with understanding the principles of enzyme kinetics and knowing how to use mathematical models to describe the reactant capacity of an enzyme. Coverage of the material is in no way, shape or form exhaustive. There exist many books on enzyme kinetics that offer intensive, in-depth treatises of the subject. Intracellular and extracellular physiological cascades are regulated by initiation and hindrance of different enzymes involved in these pathways. Investigating and understanding the mechanism of enzyme hindrance has become the premise of development of pharmaceutical agents. Organically active regular and synthetic inhibitors have been developed and special emphasis has been placed on investigations that define their structure-work relationships in an effort to understand the inception of their natural properties. A powerful complement to the assessment of these agents is the preparation and subsequent examination of key fractional structures, deep-seated auxiliary adjustments and the corresponding unnatural enantiomers of characteristic items. We sincerely hope that this book will represent an element in the tool kit of graduate students in applied science and chemical and biochemical engineering and furthermore of undergraduate students with formal preparing in natural chemistry, biochemistry, thermodynamics and chemical reaction kinetics.

Book Description :

Now in its fourth edition, this textbook is one of the few titles worldwide to cover enzyme kinetics in its entire scope and the only one to include its implications for bioinformatics and systems biology. Multi-enzyme complexes and cooperativity are therefore treated in more detail than in any other textbook on the market. The respected and well known author is one of the most experienced researchers into the topic and writes with outstanding style and didactic clarity. As with the previous editions, he presents here steady-state kinetics and fast reactions, supplementing each chapter with problems and solutions. For the first time, this edition features a companion website providing all figures in colour www.wiley-vch.de/home/fundenzykinet

Book Description :

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.

Book Description :

This volume supplements Volumes 63, 64, 87, and 249 of Methods in Enzymology. These volumes provide a basic source for the quantitative interpretation of enzyme rate data and the analysis of enzyme catalysis. Among the major topics covered are Engergetic Coupling in Enzymatic Reactions, Intermediates and Complexes in Catalysis, Detection and Properties of Low Barrier Hydrogen Bonds, Transition State Determination, and Inhibitors. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.