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9 of 9 people found the following review helpful:
4.0 out of 5 stars
A modern account of enzymes, January 7, 2005
This review is from: Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis (Hardcover)
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.
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7 of 7 people found the following review helpful:
4.0 out of 5 stars
A very useful Guide to Enzymes, January 21, 2004
This review is from: Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis (Hardcover)
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.
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5 of 5 people found the following review helpful:
4.0 out of 5 stars
Good book for steady state intial velocity measurements but.............., February 14, 2007
This review is from: Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis (Hardcover)
.....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.
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