Figure 7.
Kinetic parameters of ThiL determined by measuring the rate of kinase activity. Enzymatic assays were performed for isolated ThiL (10 µg) with various concentrations of TMP (0–50 μm). The assays were initiated with three ATP concentrations (25, 50, and 100 μm) to determine ThiL activity rates. TMP data were plotted in Michaelis-Menten (A) and Lineweaver-Burk (B) functions. The results indicated Km values of ThiL for ATP (111 ± 8 μm) and TMP (8.0 ± 3.5 μm) and Vmax (4.0 ± 0.2 nmol·min−1). Error bars are means ± S.D. of triplicate experimental groups.