Figure 1.
Steady-state kinetics of KAN acetylation by MtEis and their analysis.
A. Representative dependences of the steady-state rate of acetylation of KAN on the concentration of KAN at different concentrations of AcCoA, as specified. B. Representative dependences of the steady-state rate of acetylation of KAN on the concentration of AcCoA at different concentrations of KAN, as specified. C. Dependence of the apparent rate constant (kcat,AG), as obtained from data shown in panel A, on the concentration of AcCoA. D. Dependence of the apparent Km,AG, as obtained from data shown in panel A, on the concentration of AcCoA. The theoretical curve in D is the best simultaneous fit of eq. (3) to these values and those for acetylation of NEO as described in the text.
Figure 2.
Steady-state kinetics of NEO acetylation by MtEis and their analysis.
A. Representative dependences of the steady-state rate of acetylation of NEO on the concentration of NEO at different concentrations of AcCoA, as specified. B. Representative dependences of the steady-state rate of acetylation of NEO on the concentration of AcCoA at different concentrations of NEO, as specified. C. Dependence of the apparent rate constant (kcat,AG), as obtained from data shown in panel A, on the concentration of AcCoA. D. Dependence of the apparent Km,AG, as obtained from data shown in panel A, on the concentration of AcCoA. The theoretical curve in D is the best simultaneous fit of eq. (3) to these values and those for acetylation of KAN as described in the text.