Abstract
We consider the enzyme kinetic reaction scheme originally proposed by V. HenriВ of single enzyme-substrate dynamics where two fractions of the enzyme - free and bound - are involved. Henri's scheme involves four concentrations and three rate constants and via the mass action law it is translated into a systemВ of four ODE's. On two case studies we demonstrate how the rate constants can be computed whenever time course experimental data are available. The obtained results are compared with analogous results implied by classical Michaelis-Menten model. Our approach focuses on the uncertainties in the experimental data, as well as on the use of contemporary computational tools such as CAS Mathematica.
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