Figure 5.

Enzymatic kinetics of phosphatase activity with two different substrates, pNPP and pSer. A, Michaelis-Menten plot of AtTLP18.3 with pNPP used as the substrate. The K_m for pNPP is 42.56 mm, and the V_max is 8.11 nmol min⁻¹ mg⁻¹. B, Michaelis-Menten plot of AtTLP18.3 with pSer used as the substrate. The K_m for pSer is 47.51 mm, and the V_max is 14.55 nmol min⁻¹ mg⁻¹. The kinetics assay of AtTLP18.3 shows a classical hyperbolic saturation with pNPP but an allosteric sigmoid with pSer. Error bars represent se.