Optimal designs for variations of the Michaelis- Menten model
The rate of enzymatic reactions generally follows the Michaelis-Menten (MM) model, extensively used in biochemistry. However, there are cases in which, although the MM equation is obeyed at lower substrate concentrations, an inhibition effect occurs at high concentrations and the velocity falls off, deviating significantly from the anticipated behaviour. Two different models, describing the kinetic reaction when this type of inhibition occurs, are introduced. Optimal experimental designs methods are used in order to find the best estimation of the parameters in these models.
Keywords: Optimal design of experiments Michaelis-Menten model D-optimality c-optimality inhibition enzyme reaction
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