Figure 3

PLproSARS displays a higher catalytic efficiency than PLproCoV2 toward Ub-AMC. (a,b) Progress curves for the hydrolysis of Ub-AMC by PLproSARS (a) and PLproCoV2 (b). The concentrations of Ub-AMC are shown in the legend in nM, PLproSARS and PLproCoV2 were10 nM. (c) Four steps of the Approximate Bayesian Computation (ABC) for calculating values of kinetic constants kcat and KM. (d,e) A comparison of measurements (in blue) and solutions of the Michaelis–Menten model for given parameters of enzymatic constants found by the ABC method (in red) for PLproSARS (d) and PLproCoV2 (e) at 500 nM substrate concentration (kcat and KM are expressed in s−1 and μM, respectively). (f) The kinetic data (kcat, KM, kcat/KM) for the Ub-AMC substrate of PLproSARS and PLproCoV2.