Enzymology Enzyme kinetics

Chapters 7-9 Emphasis on basic enzymology— enzyme kinetics, mechanisms and regulation. 

Coleman, D. E., and Sprang, S. R. (1999a). Reaction dynamics of G-protein catalyzed hydrolysis of GTP as viewed by X-ray crystallographic snapshots of Gial. In Methods in Enzymology Enzyme Kinetics and Mechanism, Part E Energetics of Enzyme Catalysis (V. L. Schramm and D. L. Puvich, Eds.), Vol. 308, pp. 70-92. Academic Press, New York. 

Selected entries from Methods in Enzymology [vol, page(s)] Computer programs, 240, 312 infrared S-H stretch bands for hemoglobin A, 232, 159-160 determination of enzyme kinetic parameter, 240, 314-319 kinetics program, in finite element analysis of hemoglobin-CO reaction, 232, 523-524, 538-558 nonlinear least-squares method, 240, 3-5, 10 to oxygen equilibrium curve, 232, 559, 563 parameter estimation with Jacobians, 240, 187-191. 

It is impossible to describe and explain enzyme kinetics unless is explained by an entire book therefore, this chapter describes only briefly some aspects. It is strongly recommended to read once more a textbook on enzymology and enzyme kinetics. Especially the reaction kinetics of enzyme oligomeres, multi-enzyme complexes, and phenomena of cooperation are too complex to explain in just a few pages. 

Enzymology is a large and complex subdivision of biochemistry, and no attempt will be made to cover it in this book. The reader who requires a review of enzyme kinetics and mechanisms is referred to the many currently available and excellent textbooks of biochemistry. 

Our work deals with the necessity of creating kinetics laws for heterogeneous enzymology. There was a big gap between the classical enzyme kinetics in solution and highly structured biological systems. All the concepts of diffusion reaction are clear for our thick membrane but are also useful for lipid-protein membranes, even if the process of transport is not only classical diffusion. 

Purich, D. L., Contemporary Enzyme Kinetics and Mechanism. New York Academic Press, 1983. Selected chapters from Methods in Enzymology. Detailed information on how to analyze kinetic data and on effects of temperature, pH, and inhibitors. 

In order to avoid excessive expansion of the text, the material on enzymology and enzyme kinetics has been refocused and consolidated, reflecting changes that have taken place in the teaching of these areas in most institutions. We are grateful to Dr. Ivan Darvey for his critical comments and helpful suggestions in this endeavor. 

Anderson, K.S. (1999) Fundamental mechanisms of substrate channeling, in Schramm, V. L. and Purich, D. L. (eds.), Methods in Enzymology 308, Enzyme kinetics and Mechanism, Part E, Academic Press, San Diego, pp. 111-145. 

Schlichtich, I. and Goody, R.D. (1997) Triggering methods in crystallographic enzyme kinetics, in Carter, C. V and Sweet R. M. (eds.), Methods in Enzymology, Macromolecular Crysallography, Part B, 277, 467-. 

Bahnson, B. J., and Klinman, J. P., 1995, Hydrogen tunneling in enzyme catalysis. In Enzyme Kinetics and Mechanism, Pt D. Methods in Enzymology, 249 373fi397. 

Enzymes are proteins with catalytic properties clinical enzymology is the application of the science of enzymes to the diagnosis and treatment of disease. The principles of clinical enzymology will be mtroduced and discussed in this chapter. Individual topics include basic principles, enzyme kinetics, analytical enzymology, and diagnostic enzymology. 

A. Comish-Bowden, Principles of enzyme kinetics, Butterworth Co., London, 1976. J.A. Robinson,). Retey, Stereospecificity in organic chemistry and enzymology, VCH Verlag, Weinheim 1982. 

All enzyme-catalyzed reactions are taking place while the reactants are adsorbed on the surface of enzyme in the active site. Therefore, the concept of the active site is probably the most important kinetic and mechanistic concept in enzymology and enzyme kinetics. This concept provides a fundamental difference between the common chemical and the enzymatic reactions chemical reactions usually proceed via collision complexes, whereas enzymatic reactions proceed via adsorption complexes (Fersht, 1999). 

The method of King and Altman rendered an invaluable service to enzymology because, with its help, the rate laws for many major reaction mechanisms in enzyme kinetics were developed. It is not necessary to understand the theory of the King-Altman method in order to apply it in practice, and indeed the theory is considerably more difficult than the practice. Therefore, we shall describe in the following sections the derivation of rate laws for several simple mechanisms... 

In the practical work with enzymes, a relatively limited number of different types of titration curves is encountered for monobasic and dibasic adds. Equations (14.47) and (14.48) show the major types of equations for monobasic adds which are encountered in the technical and scientific literature (Cleland, 1977, 1982 Giimshaw et al, 1981 Purich Allison, 2000). Naturally, a rare occurrence of some rate equations and some pH profiles in the literature is in no correlation whatsoever with their importance in enzymology. A specific problem in enzyme kinetics will always raise toe need for a specific kinetic model and the corresponding rate equations. 

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