November 30, 2020

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Essential Enzyme Kinetics

Essential Enzyme Kinetics
Author : Daniel L. Purich
Publisher : Academic Press
Release Date : 2020-06-01
Category : Science
Total pages :425
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Essential Enzyme Kinetics: A Textbook for Molecular Life Scientists describes the theoretical basis and best-practice approaches for using initial-rate, fast reaction, and kinetic isotope effect experiments to define enzyme catalysis. Because a detailed knowledge of enzyme transition-states is the main driver for the rational design of slow, tight-binding inhibitors destined to become tomorrow's small-molecule drugs, Essential Enzyme Kinetics is the must-have reference for chemists, biochemists, and pharmacologists intent on pursuing careers in Big Pharma. Given the interdisciplinary nature of contemporary drug development, this book provides a lucid short-course that will also benefit nonspecialists seeking to understand the scope and reach of modern enzyme kinetics. Provides practical information about how to work with enzymes and design experiments to identify new inhibitors or activators Includes detailed step-by-step derivations of rate equations, showing tried-and-true ways to confirm that the equations obtained are correct Arranged for use both as a desk reference (with over 200 equations and more than 400 key references) or as a textbook (with 8-10 problems/exercises at the end of each chapter)

Kinetics of Enzyme Action

Kinetics of Enzyme Action
Author : Ross L. Stein
Publisher : John Wiley & Sons
Release Date : 2011-08-08
Category : Science
Total pages :320
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Few scientists have the knowledge to perform the studies that are necessary to discover and characterize enzyme inhibitors, despite the vested interest the pharmaceutical industry has in this field. Beginning with the most basic principles pertaining to simple, one-substrate enzyme reactions and their inhibitors, and progressing to a thorough treatment of two-substrate enzymes, Kinetics of Enzyme Action: Essential Principles for Drug Hunters provides biochemists, medicinal chemists, and pharmaceutical scientists with numerous case study examples to outline the tools and techniques necessary to perform, understand, and interpret detailed kinetic studies for drug discovery.

Principles of Enzyme Kinetics

Principles of Enzyme Kinetics
Author : Athel Cornish-Bowden
Publisher : Elsevier
Release Date : 2014-05-20
Category : Science
Total pages :220
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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.

Fundamentals of Enzyme Kinetics

Fundamentals of Enzyme Kinetics
Author : Athel Cornish-Bowden
Publisher : Elsevier
Release Date : 2014-05-20
Category : Science
Total pages :244
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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.

Fundamentals of Enzyme Kinetics

Fundamentals of Enzyme Kinetics
Author : Athel Cornish-Bowden
Publisher : Elsevier
Release Date : 2014-05-20
Category : Science
Total pages :244
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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.

Essentials of Enzymology

Essentials of Enzymology
Author : Rufus O. Okotore
Publisher : Xlibris Corporation
Release Date : 2015-03-13
Category : Medical
Total pages :221
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Essentials of Enzymology provides concise information on an important area of the subject, Biochemistry. This may serve as course material for an advanced treatise in Enzymology designed for undergraduate science degree programs, especially B.Sc. (Hons ) Biochemistry and Chemistry. The book is in 12 chapters which has been divided into four distinct sections, thus (1) Basic enzyme chemistry and physiology. (2) Enzyme Kinetics, (3) Enzyme catalysis, Mechanisms and Regulation,(4)Applications of Enzymology. The Part 1 consists of four chapters that deal with the nature of enzymes- (history, properties and classifi cation), enzyme physiology; structure of enzymes, and analytical enzymology. Part 2 deals with Enzyme Kinetics which is treated in three chapters, and Part 3, made up of three chapters discuss Enzyme catalysis, mechanisms and regulation. Lastly, Part 4 consisting of two chapters deal with the applications of enzymology. Signifi cantly, the kinetics of enzyme catalyzed reactions in diverse experimental conditions, and also under various inhibition types are presented in a simple, mathematical lucid approach. The mechanisms of action for two atypical proteins-chymotrypsin and lysozyme, so also the identifi cation of active sites of enzymes by specifi c labels are discussed concisely. Lastly, the specifi c applications of enzymes in diagnostic medicine, industry, and also the new emerging area of enzyme biotechnology and enzyme bioinformatics are presented

Enzyme Kinetics and Regulation

Enzyme Kinetics and Regulation
Author : Aaren Bennett
Publisher : Scientific e-Resources
Release Date : 2018-07-07
Category :
Total pages :328
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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.

Enzyme Kinetics and Mechanisms, Part E, Energetics of Enzyme Catalysis

Enzyme Kinetics and Mechanisms, Part E, Energetics of Enzyme Catalysis
Author : Anonim
Publisher : Elsevier
Release Date : 1999-09-06
Category : Science
Total pages :460
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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.

Enzyme Kinetics: Catalysis and Control

Enzyme Kinetics: Catalysis and Control
Author : Daniel L. Purich
Publisher : Elsevier
Release Date : 2010-06-16
Category : Science
Total pages :920
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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

Contemporary Enzyme Kinetics and Mechanism

Contemporary Enzyme Kinetics and Mechanism
Author : Anonim
Publisher : Academic Press
Release Date : 2009-10-24
Category : Science
Total pages :704
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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

Kinetics of Enzyme-Modifier Interactions

Kinetics of Enzyme-Modifier Interactions
Author : Antonio Baici
Publisher : Springer
Release Date : 2015-06-24
Category : Science
Total pages :489
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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.

Enzyme Kinetics and Mechanism, Part B: Isotopic Probes and Complex Enzyme Systems

Enzyme Kinetics and Mechanism, Part B: Isotopic Probes and Complex Enzyme Systems
Author : Sidney P. Colowick,Nathan Oram Kaplan
Publisher : Academic Press
Release Date : 1980
Category : Science
Total pages :418
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The critically acclaimed laboratory standard, 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. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Enzyme Kinetics and Mechanism

Enzyme Kinetics and Mechanism
Author : Vern L. Schramm,Daniel L. Purich
Publisher : Elsevier
Release Date : 1999
Category : Science
Total pages :460
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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.

Essentials of Enzymology

Essentials of Enzymology
Author : John Herald
Publisher : Unknown
Release Date : 2016-06-03
Category : Science
Total pages :260
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Enzymology deals with in-depth study and analysis of enzymes and is crucial for the understanding of many physiological processes. The aim of this book is to provide an understanding of the multiple aspects of enzymology through discussions on topics like metabolism, enzyme kinetics, industrial applications, etc. A number of latest researches have been included to keep the readers up-to-date with the global progress in this area of study. This book is an essential guide for both researchers and students who wish to delve deeper into the scientific study of enzymes.

Contemporary Enzyme Kinetics and Mechanism

Contemporary Enzyme Kinetics and Mechanism
Author : Daniel L. Purich
Publisher : Academic Press
Release Date : 1983-01-01
Category : Science
Total pages :566
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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.