Table 1. Rate Constants Determined (in Black) Directly from the Experiments or (in Blue) Indirectly from the Best Fitting between the Numerical Kinetic Simulations and the Experimental Kinetic Plots^d.

^aMichaelis–Menten-type reactions are characterized by two parameters: the Michaelis constant (K_i^M) and the turnover rate (k′).

^bDetermined from the best fit of the simulated kinetic traces to the experimental ones (see Figure 5 and the text for details).

^cThe absolute rate constants in green were estimated by assuming a diffusion-controlled bimolecular reaction.

^dThe other rate constants (in green) were estimated by the assumption that Ca²⁺ can bind to the enzyme according to a diffusion-controlled reaction.