Table 1.
Substrate kinetic parameters.
| Glc1P | ATP | ||||
|---|---|---|---|---|---|
| 3PGA | |||||
| Enzyme | (mM) | S0.5 (mM) | nH | S0.5 (mM) | nH |
| OtaS/OtaL | 0 | 2.2 ± 0.4 | 1.0 | 0.87 ± 0.05 | 1.1 |
| 5 | 0.086 ± 0.002 | 1.5 | 0.37 ± 0.01 | 1.5 | |
| OtaS/OtaLR466K | 0 | 1.8 ± 0.4 | 1.0 | 1.28 ± 0.07 | 1.1 |
| 5 | 0.103 ± 0.005 | 1.5 | 0.25 ± 0.01 | 1.4 | |
| OtaSK443R/OtaL | 0 | 1.5 ± 0.9 | 0.9 | 0.9 ± 0.2 | 1.6 |
| 5 | 0.37 ± 0.04 | 0.9 | 0.58 ± 0.07 | 1.9 | |
| OtaSK443R/OtaLR466K | 0 | 1.9 ± 0.5 | 0.8 | 1.7 ± 0.7 | 0.9 |
| 5 | 0.28 ± 0.01 | 1.7 | 0.35 ± 0.05 | 1.3 | |
Saturation curves for Glc1P and ATP were performed in absence or presence of 5 mM 3PGA. Enzyme activity was assayed using the colorimetric method, as described in Section “Materials and Methods.”