Figure 5: Kinetic analysis of the NES and GES1 purified recombinant proteins.

The catalytic activities of the purified enzymes were measured in the presence of the metal ions Mg²⁺ (0, 5, 10, 15 and 20 mM) and K⁺ (0, 50, 100, 150 and 200 mM). Under the optimum concentrations of Mg²⁺ and K⁺ (TwNES, 20 mM MgCl₂ and 200 mM KCl; TwGES1, 20 mM MgCl₂), the basic kinetic properties of TwNES and TwGES1 for the substrates (E,E)-FPP and GGPP were examined. All assays were incubated for 10 min at 30 °C. K_m (Michaelis-Menten constant), V_max (maximal velocity), K_cat (turnover number) and K_cat/K_m values of the were calculated by using the GraphPad Prism software. Values shown are means ± SD of three replicates.