{"product_id":"enzymes-isbn-9781119793250","title":"Enzymes","description":"\u003cb\u003eENZYMES\u003c\/b\u003e \u003cp\u003e\u003cb\u003eA complete and approachable introduction to the study of enzymes, from theory to practice\u003c\/b\u003e \u003c\/p\u003e\u003cp\u003eEnzymes catalyze the bulk of important biological processes, both metabolic and biochemical. They are specialized proteins whose function is determined  by their structure, understanding which is therefore a key focus of biological, pharmacological, and agrarian research, among many others. A thorough  knowledge of enzyme structure, pathways, and mechanisms is a fundamental building block of the life sciences and all others connected to them. \u003c\/p\u003e\u003cp\u003e\u003ci\u003eEnzymes \u003c\/i\u003eoffers a detailed introduction to this critical subject. It analyzes enzyme proteins at the structural level and details the mechanisms by which they perform their catalyzing functions. The book’s in-depth engagement with primary literature and up-to-date research allows it to continuously deploy illustrative examples and connect readers with further research on key subjects. Fully updated after decades as the standard text, this book unlocks a thriving field of biological and biochemical research. \u003c\/p\u003e\u003cp\u003eReaders of the third edition of \u003ci\u003eEnzymes\u003c\/i\u003e will also find: \u003c\/p\u003e\u003cul\u003e\n\u003cli\u003eExpanded chapters on steady-state and transient-state enzyme kinetics, structural components of enzymes, and more\u003c\/li\u003e \u003cli\u003eNew chapters on enzyme regulation, enzyme-macromolecule interactions, enzyme evolution, and enzymes in human health\u003c\/li\u003e \u003cli\u003eKey Learning Points at the beginning of each chapter to assist students and instructors\u003c\/li\u003e\n\u003c\/ul\u003e \u003cp\u003e\u003ci\u003eEnzymes\u003c\/i\u003e promises to continue as the standard reference on this subject for practitioners of the life sciences and related fields in both academia and industry.Eine umfassende und leicht verständliche Einführung in das Studium der Enzyme, von Theorie bis Praxis\u003cbr\u003e \u003cbr\u003e Bei den meisten wichtigen biologischen Prozessen auf metabolischer und biochemischer Ebene dienen Enzyme als Katalysator. Dabei handelt es sich um spezialisierte Proteine, deren Funktion durch ihre Struktur bestimmt wird. Die Struktur der Enzyme zu verstehen, ist ein Forschungsschwerpunkt insbesondere in der Biologie, Pharmakologie und Agrarwissenschaft. Umfassende Kenntnisse der Struktur, Wege und Mechanismen von Enzymen sind ein grundlegendes Element der Biowissenschaften und aller damit verbundenen Fachbereiche.\u003cbr\u003e \u003cbr\u003e Das Werk Enzymes gibt eine detaillierte Einführung in dieses wichtige Thema. Die Proteine der Enzyme werden auf struktureller Ebene analysiert, und die Mechanismen, über die sie ihre katalysierende Wirkung entfalten, werden exakt dargestellt. Da in diesem Werk umfangreich auf weitere Primärliteratur und aktuelle Forschungsergebnisse Bezug genommen wird, können durchgängig anschauliche Beispiele gegeben werden, und die Leserinnen und Leser erhalten Einblicke in die weitergehende Forschung zu wichtigen Themen. Das Buch gilt bereits seit Jahrzehnten als Standardwerk und wurde jetzt vollständig aktualisiert. So bietet es einen Zugang zu dem sich ständig weiterentwickelnden Gebiet der biologischen und biochemischen Forschung.\u003cbr\u003e \u003cbr\u003e Die dritte Ausgabe von Enzymes bietet den Leserinnen und Lesern außerdem:\u003cbr\u003e * Erweiterte Kapitel zur Kinetik von Enzymen im stationären und instationären Zustand, zu strukturellen Bestandteilen von Enzymen und weiteren Themen\u003cbr\u003e * Neue Kapitel über die Enzymregulierung, Wechselwirkungen zwischen Enzymen und Makromolekülen, die Entwicklung von Enzymen und die Rolle von Enzymen für die menschliche Gesundheit\u003cbr\u003e * Jedes Kapitel beginnt mit einer Auflistung der jeweiligen Lernziele als Unterstützung für Studierende und Lehrende\u003cbr\u003e \u003cbr\u003e Das Werk Enzymes dürfte für Forscher und Anwender an Universitäten und in der Industrie in den Biowissenschaften und verwandten Bereichen weiterhin als Standardlehrwerk zu diesem Thema dienen. \u003c\/p\u003e\u003cp\u003ePreface to the Third Edition xvii\u003c\/p\u003e \u003cp\u003ePreface to the Second Edition xix\u003c\/p\u003e \u003cp\u003ePreface to the First Edition xxi\u003c\/p\u003e \u003cp\u003eAcknowledgments xxiii\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 A Brief History of Enzymology 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 1\u003c\/p\u003e \u003cp\u003e1.1 Enzymes in Antiquity 2\u003c\/p\u003e \u003cp\u003e1.2 Early Enzymology 3\u003c\/p\u003e \u003cp\u003e1.3 The Development of Mechanistic Enzymology 4\u003c\/p\u003e \u003cp\u003e1.4 Studies of Enzyme Structure 5\u003c\/p\u003e \u003cp\u003e1.5 Enzymology Today 7\u003c\/p\u003e \u003cp\u003e1.6 Summary 9\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 9\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Chemical Bonds and Reactions in Biochemistry 11\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 11\u003c\/p\u003e \u003cp\u003e2.1 Atomic and Molecular Orbitals 12\u003c\/p\u003e \u003cp\u003e2.2 Thermodynamics of Chemical Reactions 22\u003c\/p\u003e \u003cp\u003e2.3 Acid–base Chemistry 27\u003c\/p\u003e \u003cp\u003e2.4 Noncovalent Interactions in Reversible Binding 29\u003c\/p\u003e \u003cp\u003e2.5 Rates of Chemical Reactions 33\u003c\/p\u003e \u003cp\u003e2.6 Summary 38\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 38\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Structural Components of Enzymes 39\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 39\u003c\/p\u003e \u003cp\u003e3.1 The Amino Acids 40\u003c\/p\u003e \u003cp\u003e3.2 The Peptide Bond 48\u003c\/p\u003e \u003cp\u003e3.3 Amino Acid Sequence or Primary Structure 51\u003c\/p\u003e \u003cp\u003e3.4 Secondary Structure 54\u003c\/p\u003e \u003cp\u003e3.5 Tertiary Structure 60\u003c\/p\u003e \u003cp\u003e3.6 Subunits and Quaternary Structure 64\u003c\/p\u003e \u003cp\u003e3.7 Cofactors in Enzymes 67\u003c\/p\u003e \u003cp\u003e3.8 Conformational Dynamics and Enzyme Function 70\u003c\/p\u003e \u003cp\u003e3.9 Methods of Protein Structure Determination 75\u003c\/p\u003e \u003cp\u003e3.10 Summary 79\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 80\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Protein–Ligand Binding Equilibria 83\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learnings Points 83\u003c\/p\u003e \u003cp\u003e4.1 The Equilibrium Dissociation Constant, K d 84\u003c\/p\u003e \u003cp\u003e4.2 The Kinetic Approach to Equilibrium 86\u003c\/p\u003e \u003cp\u003e4.3 Binding Measurements at Equilibrium 88\u003c\/p\u003e \u003cp\u003e4.4 Graphic Analysis of Equilibrium Ligand-Binding Data 94\u003c\/p\u003e \u003cp\u003e4.5 Equilibrium Binding with Ligand Depletion (Tight Binding Interactions) 100\u003c\/p\u003e \u003cp\u003e4.6 Competition Among Ligands for a Common Binding Site 101\u003c\/p\u003e \u003cp\u003e4.7 Protein Dynamics in Receptor–Ligand Binding 102\u003c\/p\u003e \u003cp\u003e4.8 Orthosteric and Allosteric Ligand Binding Sites 104\u003c\/p\u003e \u003cp\u003e4.9 Experimental Methods for Measuring Ligand Binding 105\u003c\/p\u003e \u003cp\u003e4.10 Summary 122\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 122\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Steady-State Kinetics of Single-Substrate Enzyme Reactions 125\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 125\u003c\/p\u003e \u003cp\u003e5.1 The Time Course of Enzymatic Reactions 126\u003c\/p\u003e \u003cp\u003e5.2 Effects of Substrate Concentration on Velocity 127\u003c\/p\u003e \u003cp\u003e5.3 The Rapid Equilibrium Model of Enzyme Kinetics 129\u003c\/p\u003e \u003cp\u003e5.4 The Steady-State Model of Enzyme Kinetics 131\u003c\/p\u003e \u003cp\u003e5.5 The Significance of k cat and K m 134\u003c\/p\u003e \u003cp\u003e5.6 Experimental Measurement of k cat and K m 139\u003c\/p\u003e \u003cp\u003e5.7 Other Linear Transformations of Enzyme Kinetic Data 147\u003c\/p\u003e \u003cp\u003e5.8 Measurements at Low Substrate Concentrations 149\u003c\/p\u003e \u003cp\u003e5.9 Deviations From Hyperbolic Kinetics 150\u003c\/p\u003e \u003cp\u003e5.10 Summary 153\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 153\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Chemical Mechanisms in Enzyme Catalysis 155\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 155\u003c\/p\u003e \u003cp\u003e6.1 Substrate–Active Site Complementarity 156\u003c\/p\u003e \u003cp\u003e6.2 Rate Enhancement Through Transition State Stabilization 159\u003c\/p\u003e \u003cp\u003e6.3 Chemical Mechanisms for Transition State Stabilization 162\u003c\/p\u003e \u003cp\u003e6.4 The Serine Proteases: An Illustrative Example 182\u003c\/p\u003e \u003cp\u003e6.5 Enzymatic Reaction Nomenclature 187\u003c\/p\u003e \u003cp\u003e6.6 Summary 191\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 191\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Experimental Measures of Steady-State Enzyme Activity 193\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 193\u003c\/p\u003e \u003cp\u003e7.1 Initial Velocity Measurements 194\u003c\/p\u003e \u003cp\u003e7.2 Detection Methods 208\u003c\/p\u003e \u003cp\u003e7.3 Separation Methods in Enzyme Assays 224\u003c\/p\u003e \u003cp\u003e7.4 Factors Affecting the Velocity of Enzymatic Reactions 236\u003c\/p\u003e \u003cp\u003e7.5 Reporting Enzyme Activity Data 252\u003c\/p\u003e \u003cp\u003e7.6 Enzyme Stability 253\u003c\/p\u003e \u003cp\u003e7.7 Summary 258\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 258\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Transient-State Kinetics 261\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 261\u003c\/p\u003e \u003cp\u003e8.1 Timescale of Pre-Steady-State Turnover 262\u003c\/p\u003e \u003cp\u003e8.2 Instrumentation for Transient Kinetic Measurements 264\u003c\/p\u003e \u003cp\u003e8.3 Estimating Initial Conditions for Transient Kinetic Measurements 266\u003c\/p\u003e \u003cp\u003e8.4 Examples of Some Common Transient Kinetic Reaction Mechanisms 267\u003c\/p\u003e \u003cp\u003e8.5 Examples of Transient Kinetic Studies from the Literature 272\u003c\/p\u003e \u003cp\u003eDeformylase 275\u003c\/p\u003e \u003cp\u003e8.6 Summary 277\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 278\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Enzyme Regulation 279\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 279\u003c\/p\u003e \u003cp\u003e9.1 Active and Inactive Conformational States 280\u003c\/p\u003e \u003cp\u003e9.2 Post-Translational Modifications 281\u003c\/p\u003e \u003cp\u003e9.3 Enzyme Regulation Through Protein–Protein Interactions 294\u003c\/p\u003e \u003cp\u003e9.4 Small-Molecule Allosteric Ligands 297\u003c\/p\u003e \u003cp\u003e9.5 Quantitative Measurements of Enzyme Activation and Inhibition 302\u003c\/p\u003e \u003cp\u003e9.6 Regulation of Protein Kinases 308\u003c\/p\u003e \u003cp\u003e9.7 Summary 314\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 315\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Reversible Inhibitors 317\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 317\u003c\/p\u003e \u003cp\u003e10.1 Equilibrium Treatment of Reversible Inhibition 319\u003c\/p\u003e \u003cp\u003e10.2 Thermodynamic Modes of Reversible Inhibition 321\u003c\/p\u003e \u003cp\u003e10.3 Effects of Inhibitors on Steady-State Parameters 324\u003c\/p\u003e \u003cp\u003e10.4 Concentration-Response Plots of Enzyme Inhibition 333\u003c\/p\u003e \u003cp\u003e10.5 Effects of Substrate Concentration on Inhibitor Concentration–Response Curves 337\u003c\/p\u003e \u003cp\u003e10.6 Mutually Exclusive Binding of Two Inhibitors 340\u003c\/p\u003e \u003cp\u003e10.7 Structure–Activity Relationships and Inhibitor Design 343\u003c\/p\u003e \u003cp\u003e10.8 Summary 353\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 354\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Tight-Binding Inhibitors 357\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 357\u003c\/p\u003e \u003cp\u003e11.1 Identifying Tight-Binding Inhibition 358\u003c\/p\u003e \u003cp\u003e11.2 Distinguishing Inhibitor Type for Tight-Binding Inhibitors 359\u003c\/p\u003e \u003cp\u003e11.3 Determining K I for Tight-binding Inhibitors 362\u003c\/p\u003e \u003cp\u003e11.4 Use of Tight-Binding Inhibitors to Determine Active Enzyme Concentration 365\u003c\/p\u003e \u003cp\u003e11.5 Summary 368\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 368\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Time-Dependent Inhibition 371\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 371\u003c\/p\u003e \u003cp\u003e12.1 Progress Curves for Slow-Binding Inhibitors 375\u003c\/p\u003e \u003cp\u003e12.2 Distinguishing Between Slow-Binding Schemes 378\u003c\/p\u003e \u003cp\u003e12.3 Distinguishing Between Modes of Inhibitor Interaction with Enzyme 382\u003c\/p\u003e \u003cp\u003e12.4 Determining Reversibility 384\u003c\/p\u003e \u003cp\u003e12.5 Examples of Slow-Binding Enzyme Inhibitors 386\u003c\/p\u003e \u003cp\u003e12.6 Summary 398\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 398\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Enzyme Reactions with Multiple Substrates 401\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 401\u003c\/p\u003e \u003cp\u003e13.1 Reaction Nomenclature 402\u003c\/p\u003e \u003cp\u003e13.2 Bi–Bi Reaction Mechanisms 403\u003c\/p\u003e \u003cp\u003e13.3 Distinguishing Between Random and Compulsory-Ordered Mechanisms by Inhibition Pattern 407\u003c\/p\u003e \u003cp\u003e13.4 Isotope Exchange Studies for Distinguishing Reaction Mechanisms 409\u003c\/p\u003e \u003cp\u003e13.5 Using the King–Altman Method to Determine Velocity Equations 411\u003c\/p\u003e \u003cp\u003e13.6 Cleland’s Net Rate Constant method for Determining v max and v max @k m 414\u003c\/p\u003e \u003cp\u003e13.7 Summary 416\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 417\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Enzyme–Macromolecule Interactions 419\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 419\u003c\/p\u003e \u003cp\u003e14.1 Mutlitprotein Enzyme Complexes 420\u003c\/p\u003e \u003cp\u003e14.2 Enzyme Reactions on Macromolecular Substrates 422\u003c\/p\u003e \u003cp\u003e14.3 Summary 436\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 436\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Cooperativity in Enzyme Catalysis 439\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 439\u003c\/p\u003e \u003cp\u003e15.1 Historic Examples of Cooperativity and Allostery in Proteins 441\u003c\/p\u003e \u003cp\u003e15.2 Models of Allosteric Behavior 445\u003c\/p\u003e \u003cp\u003e15.3 Effects of Cooperativity on Velocity Curves 449\u003c\/p\u003e \u003cp\u003e15.4 Sigmoidal Kinetics for Nonallosteric Enzymes 452\u003c\/p\u003e \u003cp\u003e15.5 Summary 453\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 453\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Evolution of Enzymes 455\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 455\u003c\/p\u003e \u003cp\u003e16.1 Early Earth Conditions 456\u003c\/p\u003e \u003cp\u003e16.2 Natural Selection 456\u003c\/p\u003e \u003cp\u003e16.3 Genetic Alterations 459\u003c\/p\u003e \u003cp\u003e16.4 Enzyme Families and Superfamilies 463\u003c\/p\u003e \u003cp\u003e16.5 Enzyme Promiscuity as a Springboard of Evolution 467\u003c\/p\u003e \u003cp\u003e16.6 Protein Dynamics and Conformational Selection in Evolution of Neofunctionality 474\u003c\/p\u003e \u003cp\u003e16.7 Ancestral Enzyme Reconstruction 475\u003c\/p\u003e \u003cp\u003e16.8 Contemporary Enzyme Evolution 480\u003c\/p\u003e \u003cp\u003e16.9 Summary 483\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 483\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Enzymes in Human Health 487\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eKey Learning Points 487\u003c\/p\u003e \u003cp\u003e17.1 Enzymes as Therapeutic Agents 487\u003c\/p\u003e \u003cp\u003e17.2 Enzyme Inhibitors as Therapeutic Agents 488\u003c\/p\u003e \u003cp\u003e17.3 Enzyme Essentiality in Disease 492\u003c\/p\u003e \u003cp\u003e17.4 Enzyme-Mediated Target Protein Degradation 524\u003c\/p\u003e \u003cp\u003e17.5 The Role of Enzymology in Drug Discovery and Development 527\u003c\/p\u003e \u003cp\u003e17.6 Summary 537\u003c\/p\u003e \u003cp\u003eReferences and Further Reading 537\u003c\/p\u003e \u003cp\u003eIndex 543\u003c\/p\u003e \u003cp\u003e\u003cb\u003eRobert A. Copeland, PhD, \u003c\/b\u003eis founder, President, and Chief Scientific Officer (CSO) of Accent Therapeutics, Inc. and the President of Ki Consultant, LLC. Previously, he was President of Research and CSO of Epizyme, Inc., and Vice President for Cancer Biology at the Oncology Center of Excellence in Drug Discovery for GlaxoSmithKline. He is a fellow of the American Association for the Advancement of Science and the Royal Society of Chemistry, and has published very widely on enzymes and related subjects.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989149303013,"sku":"NP9781119793250","price":215.0,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781119793250.jpg?v=1761782996","url":"https:\/\/k12savings.com\/products\/enzymes-isbn-9781119793250","provider":"K12savings","version":"1.0","type":"link"}