Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis

Book Description

Fully updated and expanded-a solid foundation for understanding experimental enzymology.

This practical, up-to-date survey is designed for a broad spectrum of biological and chemical scientists who are beginning to delve into modern enzymology. Enzymes, Second Edition explains the structural complexities of proteins and enzymes and the mechanisms by which enzymes perform their catalytic functions. The book provides illustrative examples from the contemporary literature to guide the reader through concepts and data analysis procedures. Clear, well-written descriptions simplify the complex mathematical treatment of enzyme kinetic data, and numerous citations at the end of each chapter enable the reader to access the primary literature and more in-depth treatments of specific topics.

This Second Edition of Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis features refined and expanded coverage of many concepts, while retaining the introductory nature of the book. Important new features include:

A new chapter on protein-ligand binding equilibria
Expanded coverage of chemical mechanisms in enzyme catalysis and experimental measurements of enzyme activity
Updated and refined discussions of enzyme inhibitors and multiple substrate reactions
Coverage of current practical applications to the study of enzymology

Supplemented with appendices providing contact information for suppliers of reagents and equipment for enzyme studies, as well as a survey of useful Internet sites and computer software for enzymatic data analysis, Enzymes, Second Edition is the ultimate practical guide for scientists and students in biochemical, pharmaceutical, biotechnical, medicinal, and agricultural/food-related research.

Customer Reviews:

Good book for steady state intial velocity measurements but.....................2007-02-15

.....not many people use steady state intial velocity measurements to gain insight into mechanism of biomolecules particularly enzymes these days. With that said, I do have to confess that I gave 4 stars to this book because

1) I think this is the only book (in my opinion) that gives answers to questions like what type of parameters you can get from steady state initial velocity measurements and how far you can take steady-state measurements to.

2) Occasionally, enzymes are not available in plenty, i.e., in substrate quantities and you are stuck with doing steady state kinetics and reading this book will be of use in this situation.

Here are my thoughts on the book.

The book begins with an introduction and a brief account of atoms, how they make bonds, what reactions are and why reactions have to be accelerated (rates). One thing that I found the book introduces nicely is that it clearly states how whether a reaction can occur or not depends on free energy (thermodynamics) but this does not tell us anything about the rates(1st and 2nd chapters).

The third chapter discusses aspects of protein structure beginning with amino acids, primary, secondary structures etc., just like any other biochemical text. The only thing that it lacks is a section on RNA enzymes - because proteins are not the only molecules capable of catalyzing reactions and RNAs can be catalytic. There is the very familiar Tetrahymena ribozyme (an RNA that can act as an enzyme) discovered by Tom Cech (he got the Nobel prize for the same).The fourth chapter focusses on enzyme-ligand binding equilbria. It also introduces the concepts of dissociation and association rate constants and how you can use these in determining the equilibrium binding constants. This is of practical importance because there are systems which take very long time to reach equilibrium and you cannot do equilibrium binding experiments - the only way here is to measure association and dissociation rate constants and get the binding constant from these. the chapter also has a nice table giving values of equilibrium constants and their corresponding free energy. commendable. my ohly concern is that it introduces linearizing of data such as reciprocal and double reciprocal plots which dont make intuitive sense and therefore not many good kineticists use them.

the fifth chapter goes into introducing practical concepts such as what is expected to see in reaction plots when you mix substrate and enzymes together. does a good job but there is no mention of how concentrations of both should be taken into account - which determine whether the reaction is single turnover (Enzyme does its thing only once) or multiple turnover (enzyme does its thing more than once). remember, this book is for purely steady state analysis. you cannot get individual rate constants from doing multiple turnover reactions. all you get is kcat and Km.
the sixth talks about mechanisms and the seventh about doing practical kinetics - here, it goes into why we see lag and burst in reactions sometimes. It also describes with some depth the effect of pH, why we have to maintain the pH, and destabilization of enzyme during reactions.

chapters eight, nine, ten and eleven discuss inhibitor kinetics (reversible and tight binding) and kinetics of enzymes with multiple substrates. All of these deal with measurement of intial velocities, again, remember this is a book with steady-state kinetics. There are a lot of inverse velocity and inverse subtrate plots that I cannot make any intuitive sense out of. The final chapter deals with cooperativity. although it gives a reasonably good introduction on it, the kinetic aspect is dealt with superfically. there arent a lot of kinetic plots but again, this is steady state initial velocity measurements and you can only take it so far.

A modern account of enzymes.......2005-01-08

Writing a new book of under 400 pages to cover the whole of enzymology is a courageous endeavour. Even if one confines attention to the general aspects that apply to many enzymes, and discusses only those specific mechanisms that are well established or illustrate important points, one can hardly escape the fact that the subject has become too vast to be easily summarized. Moreover, the sort of things that students want to know about enzymes differ according to whether their primary interests are in biochemistry, medicine, chemistry, engineering or molecular biology. Robert Copeland made some rather similar points in the Preface to the first edition of his book, and was honest enough to doubt whether it would be an exception to his conclusion that no single book could fulfil all of his students' needs. Nonetheless, it was successful enough to justify revising and expanding it after just four years, and the result is a worthy addition to the shelves of any enzymologist.

The book is addressed primarily to senior undergraduates or first-year graduates studying enzymology, and the emphasis is more on chemistry than on molecular biology, with definite leanings towards industrial applications. A brief account of the history of enzymology is followed by a second chapter that provides the real introduction to the book. This makes it clear that readers are expected to be able to cope with the basic chemical theory, including molecular orbitals, valence theory, resonance, thermodynamics and the theory of acids and bases. There is a lot of valuable information in this chapter, though weaker students will find the pace very fast. Fortunately the later chapters are more leisurely.

I'm not sure if it is fair to the author to mention the most obvious competitor to his book, Alan Fersht's Structure and Mechanism in Protein Science: a Guide to Enzyme Catalysis and Protein Folding. However, it is such an obvious competitor that potential readers are likely to think of it anyway, so it may be useful to compare the two books briefly. Fersht's book is much stronger on transient-state kinetics, and is more stimulating and even exciting. His is the more likely book to take to read in bed, but Copeland's is more thorough, especially in relation to topics that need to be taught but which are not very fashionable, like the kinetics of the steady state and the mechanistic features that can be deduced from the study of enzyme inhibition. It can be warmly recommended to any teacher needing a text that offers a solid introduction to enzymology.

A very useful Guide to Enzymes.......2004-01-22

This book is written by an enzymologist who presented a course on enzymology at a pharmaceutical company, as well as at the University of Pennsylvania. It is a rather well- written book that covers both theoretical and practical aspects of enzyme studies. Black and white drawings and numerous graphs illustrate the concepts. The book begins with a general review of some chemical concepts, including a brief review of thermodynamics, transition states in chemical reactions, acid-base concepts, non-covalent interactions and rates of chemical reactions. The next chapter covers aspects of enzyme (protein) structure. In a departure from other texts, the 4th chapter introduces and develops the concepts of protein-ligand binding equilibria. The derivation of Kd, along with the Langmuir isotherm to derive measurements at equilibrium is developed, as is treatment of equilibrium ligand binding data. The detour into non-enzymatic ligand-protein interactions is a very welcome treatment of this topic, so important in many drug interactions with receptors. While not strictly speaking enzymology, this chapter serves to introduce concepts that are further developed in the next chapter, which deals with the kinetics of enzymatic catalysis. This chapter nicely develops the basic equations and treatment of enzyme kinetics, and the steady state model is developed using the treatment of Briggs and Haldane. A discussion of the significance of both Km and Kcat is followed by methods to derive these values experimentally. After covering kinetics, the book moves on to chemical mechanisms of enzyme catalysis. The importance of transition state stabilization is discussed, and covalent catalysis and acid-base catalysis are highlighted. Serine proteases as model enzyme mechanisms round out the chapter.

Chapters 7 and 8 cover practical aspects of enzymology, such as velocity measurements, continuous versus end point reactions, detection methods for assays, and separation methods for reaction products (e.g., HPLC, TLC). Some pointers on enzyme concentration, temperature, pH and buffer effects on enzyme assays are valuable. The next chapter deals with reversible inhibitors, and describes the derivation of Ki. The distinctions among competitive, non-competitive and uncompetitive inhibition are discussed, and details on how to determine these in a practical sense are illustrated. There is also some discussion around the SAR of inhibitors, and this is tied in with inhibitor and drug design. Tight binding inhibitors get their own brief chapter, and there is a separate chapter on time dependent inhibition and the methodology around measuring this phenomenon. Enzyme reactions with multiple substrates and cooperativity in enzymatic catalysis also receive individual chapter treatments. Two appendices on suppliers and software tools round out the text.

Viva la Sequel!!.......2000-08-11

I never thought this could happen to me. I picked up the book and I was hooked instantly. Never before in my forays into biochemistry have I been this enchanted by such delightful prose. I started in a thermodynamic sink and I ended as an ultra-high energy intermediate. Copeland added a section on equilibrium binding that bound me with delight. His inhibitor sections loosened all my inhibitions. Even a chowder slurping ingrate from Harvard could understand and appreciate this work.

A real page-turner.......1999-02-16

In this gripping work, professor Copeland takes the reader on a roller-coaster ride through the thrilling activation energy peaks and local free energy minima of enzymology. From friendly Michealis-Menten kinetics to frightening multi-subtrate systems, Copeland holds the readers hand while unveiling his bold vision of the enzymatic universe. Even a Yalie could understand this post-modern classic.

Average customer rating:

Practical Enzymology
Hans Bisswanger
Manufacturer: Wiley-VCH
ProductGroup: Book
Binding: Paperback

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ASIN: 3527304444

Book Description

Providing a broad experimental, this book contains a theoretical introduction together with practical protocols, considering all aspects of enzymology. The fundamental experiments in enzymology are presented in very clear and easily realizable protocols, with each experiment accompanied by a section giving the theoretical background.
Essential reading for all scientists and practitioners working with enzymes.

Enzyme Assays: A Practical Approach (The Practical Approach Series, 257)

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Enzyme Assays Explained
A good guide to the principles of enzyme assay development.

Enzyme Assays: A Practical Approach (The Practical Approach Series, 257)

Manufacturer: Oxford University Press, USA
ProductGroup: Book
Binding: Paperback

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ASIN: 0199638209

Book Description

Enzyme assays are among the most frequently performed procedures in biochemistry and are routinely used to estimate the amount of enzyme present in a cell or tissue, to follow the purification of an enzyme, or to determine the kinetic parameters of a system. The range of techniques used to measure the rate of an enzyme-catalysed reaction is limited only by the nature of the chemical change and the ingenuity of the investigator. This book describes the design and execution of enzyme assays, covering both general principles and specific chapters. Building upon the highly popular first edition, this book combines revised or rewritten chapters with entirely new contributions. Topics include experimental protocols covering photometric, radiometric, HPLC, and electrochemical assays, along with methods for determining enzyme assays after gel electrophoresis. The theory underlying each method is outlined, together with a description of the instrumentation, sensitivity and sources of error. Also included are chapters on the principles of enzyme assay and kinetic studies; techniques for enzyme extraction; high- throughout screening; statistical analysis of enzyme kinetic data; and the determination of active site concentration. This second edition of Enzyme Assays will be valuable not only to biochemists, but to researchers in all areas of the life sciences.

Customer Reviews:

Enzyme Assays Explained.......2006-01-16

In an age of computerized and automated asay systems, it is possible to gather data without understanding the chemistry or biochemistry involved. This may be suitable for lab techs who work for commercial companies, but it is not a good idea for serious scientists. This book explains how assays work, what can go wrong and what the limitations are. It also reviews the types of instrumentation commonly used in assays. It is an excellent resource for laboratory instructors and graduate students.

A good guide to the principles of enzyme assay development........1999-07-27

Enzyme Assays: A Practical Approach is a good guide to the principles of assay development. It contains excellent chapters on the theoretical development of kinetic expressions and the statistical treatment of results. Different assays are illustrated (photometric, radiometric, chromatographic, and electochemical) in their respective chapters that include important considerations for assay development/use with each system. A chapter on buffers and protein determination is also included. Although the book provides some examples (in useful detail) of each kind of assay it is NOT a comprehensive overview. The chapters on electrochemical assays and the techniques for enzyme extraction are incomplete due only to the age of the volume (>5 years old). This book would be an excellent volume for those interested in enzyme assay development and would be suitable for a first year graduate chemistry/biochemistry course.

Proteolytic Enzymes: A Practical Approach

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Proteolytic Enzymes: A Practical Approach

Manufacturer: Oxford University Press, USA
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Binding: Hardcover

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Book Description

Like the popular first edition, this new edition of Proteolytic Enzymes emphasizes practical aspects of the handling, characterization, inhibition, and use of proteolytic enzymes giving general advice and specific examples. The text and protocols have been thoroughly updated to take account of the advances made in the last 10 years in both the increased understanding of the role of peptidases in many critical cellular processes e.g. apoptosis and new technological developments e.g. in recombinant protein expression, protein sequencing, and structural studies. The topics covered are: nomenclature and classification; purification; assay methods; determination of mechanism; inhibition and prevention of unwanted proteolytic activity; characterizing natural inhibitors; proteolytic enzymes in peptide mapping and primary structure elucidation by mass spectrometry and Edman sequencing; limited proteolysis as a structural probe; synthetic function. This book will be as invaluable as the first edition in providing ideas and protocols for scientists either studying proteases or using proteases as a research tool.

Kinetic Analysis of Macromolecules: A Practical Approach (The Practical Approach Series, 267)

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Kinetic Analysis of Macromolecules: A Practical Approach (The Practical Approach Series, 267)

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Enzymatic Analysis: A Practical Guide (Biological Methods)

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Practical Clinical Enzymology (Stanford series on methods and techniques in the clinical laboratory)

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PRACTICAL CLINICAL ENZYMOLOGY AND BIOCHEMICAL PROFILING

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PRACTICAL CLINICAL ENZYMOLOGY AND BIOCHEMICAL PROFILING
Paul Wolf
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Book Description

Choice Outstanding Title! (January 2006)

The image of Antarctica as a symbol of the last great wilderness and pristine environment has changed considerably in the last two decades. Environmental problems such as the ozone hole and the break-up of ice-shelves have shown that Antarctica is inextricably linked to global processes and exposed to the impact of human activities in the rest of the world. This volume provides an overview of climate change data, its effects on the structure and functioning of Antarctic ecosystems, and the occurrence and cycling of persistent contaminants. It discusses the unique physico-chemical characteristics of the Antarctic environment, ecophysiological adaptations of terrestrial and marine organisms, the transfer of contaminants in pelagic and neritic food chains and the possible consequences for animals at higher trophic levels. The text concludes with possible future scenarios of climate change and atmospheric contamination and the role of Antarctic organisms in the early detection of environmental perturbations.

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Voyage of the Discovery
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Beautifully! illustrated with both photographs and drawings by E. A. Wilson, the expedition's assistant surgeon, The Voyage of the Discovery is the definitive account of Scott's first Antarctic expedition and a fascinating description of the wild, frozen continent that would eventually claim its author's life.

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The fragile Antarctic environment consists of a closely linked system of the lithosphere, atmosphere, cryosphere, hydrosphere and biosphere. Changes in this system have influenced global climate, oceanography and sea level for most of Cenozoic time. The geological history of this region therefore provides a special record of important interactions among the various components of the Earth System. Antarctic Marine Geology is the first comprehensive single-authored book to introduce students and researchers to the geological history of the region and the unique processes that occur there. Research literature on the region is widely disseminated, and until now no single reference has existed that provides such a summary. The book is intended as a reference for all scientists working in Antarctica, and will also serve as a textbook for graduate courses in Antarctic marine geology.

Antarctic oceanology (Antarctic research series)

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