Table 2. Determination of sequential binding of ATP to PII-wt or PII-ST‑V variant.
Kd1 (µM) | Kd2 (µM) | Kd3 (µM) | ||||
PII-wt | 4.8 | ±0.0 | 17.4 | ±1.5 | 92.8 | ±14.1 |
PII-ST‑V | 2.3 | ±0.5 | 10.9 | ±4.0 | 57.7 | ±3.3 |
Mean values of three replicas of the calculated ATP dissociation constants for the PII binding sites 1-3 and ±SEM are shown. The original isotherms are presented in Figure S2.