Table 2.
Tenuazonic acid (μM) | K m (mM ATP) | V max (nmol Pi mg−1 min−1) |
---|---|---|
Control | 1.15 (0.59–1.71) | 332.4 (262.9–401.8) |
1.0 | 2.56 (0.74–4.38) | 219.3 (132.5–306.1) |
2.5 | 10.96 (0.0–37.0) | 83.8 (−76.6–244.2) |
ATP hydrolysis of S. oleracea PM fractions was measured at different ATP concentrations in response to various TeA doses, and enzyme kinetic constants, K m and V max, were determined from nonlinear regression of the Michaelis–Menten equation. Values are means ± SEM of four technical replicates of two independent PM fractions (n = 8).