Features
- Cover Type: Hard Cover with 397 pages
- Published by: Wiley-VCH
- Edition: 2nd Edition March 15, 2000
- Written in: English
- ISBN 10 Number: 0471359297
- ISBN 13 Number: 978-0471359296
-
Book Dimensions:
9.3 x 6 x 1 inches
- Weighs: 1.6 pounds
Product Review
"a welcome volume for any reader concerned with this important class of biological. The book is interesting, informative, and very readable." (
Choice, Vol. 38, No. 7, March 2001)
"an introductory textbook intended for senior undergraduate or graduate studentscoverage includes chemical bonds and reactions, structural components of enzymes" (
SciTech Book News, March 2001)
"to describe this text in one word, I would say that it is thorougha good text for those interested in enzyme mechanisms and kinetics." (
Journal of Medicinal Chemistry, Vol. 45, No. 235, 2002)
SciTech Book News, March 2001
"an introductory textbook intended for senior undergraduate or graduate studentscoverage includes chemical bonds and reactions, structural components of enzymes"
Reader Reviews
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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