Enzyme Kinetics and Mechanism, Part D: Developments in Enzyme Dynamics
Methods in Enzymology Series, Vol. 249
Editors-in-Chief: Abelson John N., Simon Melvin I.Language: Anglais
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662 p. · 15.2x22.9 cm · Hardback
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
C.A. Fierke and G.G. Hammes, Transient Kinetic Approaches to Enzyme Mechanisms.
K.A. Johnson, Rapid Quench Kinetic Analysis of Polymerases, Adenosinetriphosphatases, and Enzyme Intermediates.
R.G. Duggleby, Analysis of Enzyme Progress Curves by Nonlinear Regression.
B.V. Plapp, Site-Directed Mutagenesis: A Tool for Studying Enzyme Catalysis.
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.