Kinetics of the enzyme titration process by reversible modifiers

The effect of reversible modifiers on the initial rate of enzyme catalysed reactions has been investigated in a quasi-equilibrium approximation using the general modifier mechanism of Botts and Morales. It has been shown that, when investigating the dependence of the initial rate on the modifier concentration at a fixed substrate concentration, the kinetics of enzyme titration by reversible modifiers can generally be described using two kinetic constants. Just as the dependence of the initial rate on the substrate concentration (at a fixed modifier concentration) is described using two kinetic constants: the Michaelis constant Km and the limiting rate Vm. Only one constant M50 is needed to describe the kinetics of linear inhibition, and in the case of nonlinear inhibition and activation, along with M50 the constant QM is also needed.