Table 2.
Compound | Ki (μM) |
---|---|
Oxaloacetate | 0.12 |
Oxalate | 0.15 |
Tartronate | 0.61 |
Alpha-ketobutyrate | n.d. |
Inhibition studies were performed by varying the concentrations of L-malate from 0.1 mM (subsaturating) to up to 1 mM (saturating) while the analogue (chosen based on its inhibitory activity from Figure 3B) was held at several fixed concentrations around its inhibition constant. Concentrations of the other components in the assay mixture were held at saturation. Reciprocal velocities were plotted as a function of reciprocal substrate concentrations and all plots were linear in the range of substrate concentrations assayed (0.1-0.5 mM). The lines were calculated from the fits of the experimentally determined values to the appropriate kinetic parameters. Abbreviations: n.d, not determined.