Kinetic enzyme

The following experiments introduce the application of chemical kinetics, including enzyme kinetics. 

Bateman, Jr. R. C. Evans, J. A. Using the Glucose Oxidase/Peroxidase Systems in Enzyme Kinetics, /. Chem. Educ. 1995, 72, A240-A241. 

Lineweaver-Burk plot a graphical means for evaluating enzyme kinetics, (p. 638)... 

Enzyme Kinetics. A simple en2yme cataly2ed reaction can be described ... 

For a somewhat more extensive exposure to enzyme reaction kinetics, consult standard biochemistry texts and also Dixon, M. and E. C. Webb, Enzymes, 2d ed.. Academic Press, 1964 Segal, I. H., Enzyme Kinetics, Wiley, 1975 Gacesa, P. and J. Hubble, Enzyme Technology, Open University Press, England, 1987. 

The Michaehs-Menten equation and other similar nonhnear expressions characterize immobihzed enzyme kinetics. Therefore, for a spherical porous carrier particle with enzyme molecules immobilized on its external as well as internal surfaces, material balance of the substrate will result in the following ... 

Measurements of particular properties of a compound or substance (enzyme kinetics, reaction kinetics, FACS, fluorescence-activat cell sorting, assay). 

Leonor Michaelis and Maud Menten laid the foundation for enzyme kinetics as early as 1913 by proposing the following scheme ... 

The Michaelis-Menten equation is, like Eq. (3-146), a rectangular hyperbola, and it can be cast into three linear plotting forms. The double-reciprocal form, Eq. (3-152), is called the Lineweaver-Burk plot in enzyme kinetics. ... 

Usually initial rates are measured in enzyme kinetics so as to avoid problems arising from kinetic complications such as product inhibition. 

The quantitative description of enzyme kinetics has been developed in great detail by applying the steady-state approximation to all intermediate forms of the enzyme. Some of the kinetic schemes are extremely complex, and even with the aid of the steady-state treatment the algebraic manipulations are formidable. Kineticists have, therefore, developed ingenious schemes for writing down the steady-state rate equations directly from the kinetic scheme without carrying out the intermediate algebra." -" ... 

The relative fluctuations in Monte Carlo simulations are of the order of magnitude where N is the total number of molecules in the simulation. The observed error in kinetic simulations is about 1-2% when lO molecules are used. In the computer calculations described by Schaad, the grids of the technique shown here are replaced by computer memory, so the capacity of the memory is one limit on the maximum number of molecules. Other programs for stochastic simulation make use of different routes of calculation, and the number of molecules is not a limitation. Enzyme kinetics and very complex oscillatory reactions have been modeled. These simulations are valuable for establishing whether a postulated kinetic scheme is reasonable, for examining the appearance of extrema or induction periods, applicability of the steady-state approximation, and so on. Even the manual method is useful for such purposes. 

Kinetics is the branch of science concerned with the rates of chemical reactions. The study of enzyme kinetics addresses the biological roles of enzymatic catalysts and how they accomplish their remarkable feats. In enzyme kinetics, we seek to determine the maximum reaction velocity that the enzyme can attain and its binding affinities for substrates and inhibitors. Coupled with studies on the structure and chemistry of the enzyme, analysis of the enzymatic rate under different reaction conditions yields insights regarding the enzyme s mechanism of catalytic action. Such information is essential to an overall understanding of metabolism. 

Before beginning a quantitative treatment of enzyme kinetics, it will be fruitful to review briefly some basic principles of chemical kinetics. Chemical kinetics is the study of the rates of chemical reactions. Consider a reaction of overall stoichiometry... 

Lenore Michaelis and Maud L. Menten proposed a general theory of enzyme action in 1913 consistent with observed enzyme kinetics. Their theory was based on the assumption that the enzyme, E, and its substrate, S, associate reversibly to form an enzyme-substrate complex, ES ... 

Dixon, M., et al., 1979. Enzymes, 3rd ed. New York Academic Press. A classic work on enzyme kinetics and die properties of enzymes. 

Gray, C. J., 1971. Enzyme-Catalyzed Reactions. New York Van Nostrand Reinhold. A monograph on qnantitative aspects of enzyme kinetics. 

Segel, I. H., 1976. Biochemical Calculations, 2nd ed. New York John Wiley Sons. An excellent guide to solving problems in enzyme kinetics. 

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