This volume, as do the other Enzyme Kinetics and Mechanism volumes in the Methods in Enzymology series, provides treatment of dynamic and chemical approaches for investigating enzyme catalysis and regulation, as well as designing metabolic inhibitors. It will greatly interest those involved in enzyme chemistry, metabolic control, and drug design. It should also interest those developing commercial applications for enzymes whose properties have been re-engineered using recombinant DNA technology and site-directed mutagenesis.
General Description of the Series:
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
- Mechanisms of enzyme catalysis and inhibition- Enzyme structure and function- Regulatory control of enzymes- Action of catalytic antibodies and ribozymes
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Inhibitors as Mechanistic Probes:H.J. Fromm, Reversible Enzyme Inhibitors as Mechanistic Probes.S.E. Szedlacsek and R.G. Duggleby, Kinetics of Slow and Tight-Binding Inhibitors.W.W. Cleland, Kinetic Method for Determination of Dissociation Constants of Metal Ion(Nucleotide Complexes.B.F.Cooper and F.B. Rudolph, Product Inhibition Applications.K.L. Rebholz and D.B. Northrop, Kinetics of Iso Mechanisms.R.B. Silverman, Mechanism-Based Enzyme Inactivators.A. Radzicka and R. Wolfenden, Transition State and Multisubstrate Analog Inhibitors.
Isotopic Probles of Enzyme Action:I.A. Rose, Partition Analysis: Detecting Enzyme Reaction Cycle Intermediates.W.W. Cleland, Isotope Effects: Determination of Enzyme Transition State Structure.B.J. Bahnson and J.P. Klinman, Hydrogen Tunneling in Enzyme Catalysis.L.S. Mullins and F.M. Raushel, Positional Isotope Exchange as Probe of Enzyme Action.M.-D. Tsai, R.-T. Jiang, T. Dahnke, and Z. Shi, Manipulating Phosphorus Stereospecificity of Adenylate Kinase by Site-Directed Mutagenesis.F.C. Wedler, Equilibrium Isotope Exchange in Enzyme Catalysis.D.N. Silverman, Proton Transfer in Carbonic Anhydrase Measured by Equilibrium Isotope Exchange.
Kinetics of Specialized Systems:J.D. Stewart, I. Lee, B.A. Posner, and S.J. Benkovic, Expression of Properly Folded Catalytic Antibodies in Escherichia coli.K.E. Neet, Cooperativity in Enzyme Function: Equilibrium and Kinetic Aspects.M.K. Jain, M.H. Gelb, J. Rogers, and O.G. Berg, Kinetic Basis for Interfacial Catalysis by Phospholipase A2.
Simon, Melvin I.
Purich, Daniel L.
Daniel Lee Purich has been at the forefront of biochemistry research for more than 25 years. He was awarded the National Institutes of Health Research Career Development Award from 1977-1982, the Plous Teaching Award (the University of California Santa Barbara Campus-Wide Teaching Award) in 1977, has been a member of the National Institutes of Health Biochemistry Study Section from 1982-1985, and a member of the <i>Journal of Biological Chemistry</i> Editorial Board from 1981-1986. He has been a member of the American Society of Biological Chemists, the American Chemical Society, the New York Academy of Sciences, the Biochemical Society, and the American Society for Cell Biology. Dr. Purich is currently a Professor and Chairman of the Department of Biochemistry and Molecular Biology at the Florida College of Medicine. He is the author and editor of numerous scientific publications.