ENZO: A Web Tool for Derivation and Evaluation of Kinetic Models of Enzyme Catalyzed Reactions
Autoactivation of procathepsin B.
The data originally presented in  were used. The total amount of protein was determined by Pace et al.  and used as a fixed value for each substrate/precursor concentration. The initial values of ES is zero and E is fitted in the interval [0, 1]. The initial value of rate constant k0 is set to diffusion rate value of 108 M−1 min−1 and fixed, while initial values of k1 and k2 are 200 min−1 and 7.2 min−1 respectively, and fitted in the interval of [0, 1020]. The sum of free active enzyme (E) and the instantaneusly dissociated complex (ES) is the measured species. Y-axis represents the concentration of cathepsin B in molar concentration and the X-axis represents time in minutes. The final estimated values of rate constants and initial concentrations of active enzyme portion for each individual curve are displayed under the Evaluated Parameters.