TABLE 1.
Comparison of kinetic constants determined for phosphorylation of Tide by His6-S6K1 (ΔAID)-T389E
| Constant | Steady statea | Pre-steady stateb | Equation |
|---|---|---|---|
| kcat (s-1) | 0.18-0.19 | 0.22 | 1 |
| KmATP (μm) | 4.9-5.5 | 5.9 | 2 |
| KdATP (μm) | 5.0-5.5 | 5.9 | 3 |
| KmTide (μm) | 4.1 | 5.1 | 4 |
| KdADP (μm) | 5.5-6.0 | 5.8 | 5 |
| KipTide (μm) | 170-180 | 185 | 6 |
a
These numbers represent the range of values obtained from global and secondary fits of data obtained in both two-substrate and product inhibition steady-state kinetics. A detailed listing of all determined values ± S.E. is given in supplemental Table S1.
b
These numbers were calculated using the designated equation and microscopic rate constant values in Table 2.