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Rating: 
Summary: Viva la Sequel!!
Review: 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.
Rating:
Summary: Viva la Sequel!!
Review: 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.
Rating:
Summary: A real page-turner
Review: 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.
Rating: 
Summary: A very useful Guide to Enzymes
Review: 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.
Rating:
Summary: A very useful Guide to Enzymes
Review: 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.
Rating:
Summary: A modern account of enzymes
Review: 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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