TABLE 1.
Kinetic values of autophosphorylation and dephosphorylation reactions
Protein | Kinetic valueb
|
Reference | |||
---|---|---|---|---|---|
Autophosphorylation
|
Dephosphorylation
|
||||
KmATP (μM) | k (10−4) (s−1) | KmADP (μM) | −k (s−1) | ||
MBP-NarX185a | 2.4 ± 0.7 | 0.5 ± 0.2 | 2.3 ± 0.6 | 0.029 ± 0.01 | This study |
MBP-NarQ182a | 22.8 ± 9.3 | 2.2 ± 1.1 | 1.8 ± 0.7 | 0.013 ± 0.003 | This study |
CheA | 300 ± 75 | 260 ± 40 | 42 ± 8 | 0.028 ± 0.003 | 35 |
NRII (NtrB) | 31 ± 1.4 | 118 ± 2.5 | 40 | − | 16, 34 |
KinA | 74 ± 11 | 19 ± 5 | 16 ± 2.6 | − | 15 |
EnvZ | 218 | 0.81c | − | − | 17 |
PhoQ | 20.1 ± 13.1 | −d | − | − | 21 |
Values were determined as described under Materials and Methods and Results expressed per monomer.
± standard errors of the mean. For the Nar sensors, these values were determined from three independent measurements and different protein preparations.
−, not determined or published.