Enzyme Kinetic Equations

The rate of a chemical reaction is usually expressed in terms of a change in the concentration of a reactant or of a product in a given time interval. Any convenient experimental method can be used to monitor changes in concentration. In a reaction of the form A + B P, where A and B are reactants and P is the product, the rate of the reaction can be expressed either in terms of the rate of disappearance of one of the reactants or in terms of the rate of appearance of the product. The rate of disappearance of A is —A [A]/At, where A symbolizes change, [A] is the concentration of A in moles per liter, and t is time. Likewise, the rate of disappearance of B is —A [B] / At, and the rate of appearance of P is A[P]/At. The rate of the reaction can be expressed in terms of any of these changes because the rates of appearance of product and disappearance of reactant are related by the stoichiometric equation for the reaction. 

The negative signs for the changes in concentration of A and B indicate that A and B are being used up in the reaction, while P is being produced. 

It has been established that the rate of a reaction at a given time is proportional to the product of the concentrations of the reactants raised to the appropriate powers, 

The exponents in the rate equation are usually small whole numbers, such as 1 or 2. (There are also some cases in which the exponent 0 occurs.) The values of the exponents are related to the number of molecules involved in the detailed steps that constitute the mechanism. The overall order of a reaction is the sum of all the exponents. If, for example, the rate of a reaction A P is given by the rate equation 

Many common reactions are first or second order. After the order of the reaction is determined experimentally, proposals can be made about the mechanism of a reaction. 

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P. J. Mulquiney and P. W. Kuchel, Model of 2,3 bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations Computer simulation and metabolic control analysis. Biochem. J. 342 (3), 597 604 (1999). 

STEADY-STATE TREATMENT. During the steady state, the concentrations of various enzyme intermediates are essentially unchanged that is, the rate of formation of a given intermediate is equal to its rate of disappearance. This assumption was first introduced to the derivation of enzyme kinetic equations by Briggs and Haldane ... 

ENZYME KINETIC EQUATIONS MICHAELIS CONSTANT UNI UNI MECHANISM Koppel-Palm solvent parameters,... 

DOUBLE-RECIPROCAL PLOT ENZYME KINETIC EQUATIONS (1. The... 

ENZYME KINETIC EQUATIONS REDOX-ACTIVE AMINO ACIDS TOPAQUINONE REDOX POTENTIAL Redox reactions,... 

Time-course of enzyme-catalyzed reactions, ENZYME KINETIC EQUATIONS TIME-OF-FLIGHT MASS SPECTROMETRY Time of relaxation,... 

ENZYME KINETIC EQUATIONS MICHAELIS-MENTEN EQUATION UNI UNI MECHANISM ENZYME RATE EQUATIONS 1. The Basics... 

The Michaelis-Menten equation (Equation 4.2) is simply derived from enzyme kinetics equations, by substituting for... 

Strictly considered, the Walker plot applies to reactions in which only substrate is consumed the growth of cells is not anticipated and there is no other reaction. This linearization starts from the enzyme kinetic equation... 

You need one more thing When the concentration of substrate is so high that almost no free enzyme is left in the solution, that is, when [ ]tot [R S], the initial rate, Vq = k2X[ S], reaches the maximum reaction rate, Vroax- This will give you the enzyme kinetics equation known as the Michaelis-Menten or the MM equation ... 

VoUcenstein, M.V., Goldstein, B.N., 1966b. Method for derivation of enzyme kinetics equations. Biokhimiya 31, 541-547 (in Russian). 

Modular enzyme kinetic equation buiiding 3.1 Unified modifier equation... 

Pseudo steady state enzyme kinetic equations in time course modeiiing of substrate hydroiysis... 

Lineweaver-Burk plot A double-reciprocal plot used to determine the two constants featured in simple enzyme kinetic equations such as Michaelis-Menten kinetics, Monod kinetics, and in similar adsorption isotherm models such as the Langmuir adsorption isotherm. The constants are determined from the intercept with the y-axis and the gradient (see Fig. 26). It was devised and published in 1934 by American chemist Hans Lineweaver (1907-2009) and American biochemist Dean Burk (1904-1988). 

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