Biological enzyme modeling rate constant

In this context, Berry [277] studied the enzyme reaction using Monte Carlo simulations in 2-dimensional lattices with varying obstacle densities as models of biological membranes. That author found that the fractal characteristics of the kinetics are increasingly pronounced as obstacle density and initial concentration increase. In addition, the rate constant controlling the rate of the complex formation was found to be, in essence, a time-dependent coefficient since segregation effects arise due to the fractal structure of the reaction medium. In a similar vein, Fuite et al. [278] proposed that the fractal structure of the liver with attendant kinetic properties of drug elimination can explain the unusual... 

When accurate data can be obtained over a range of both concentrations and temperatures, it is possible from the Michaelis-Menton model to obtain data on the first-order rate constant kz and the constant Km = kz + kz)/ki and their apparent activation energies Ez and Unfortunately, most of the values quoted in the literature for the activation energies of enzyme-catalyzed reactions are derived from the use of overly simple first-order equations to describe the reaction. Consequently these values are a composite of Kmj kzy and the other constants in the Michaelis-Menton equation and cannot be used for interpretive purposes. Where the constants have been separated it is found that the values of Ez are low and of order of magnitude of 5 to 15 Kcal/mole. It is of interest to note that enzyme preparations from different biological sources, which may show different specific activity for a given reaction, have very nearly the same temperature coefficient for their specific rate constants. ... 

The feasibility of the carrier model for metal-ion transport across biological membranes has been explored by Lauger in terms of the known rate constants for the K+-valinomycin system. He makes an interesting comparison between the action of a carrier molecule and that of an enzyme. An enzyme... 

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