EC Number   |
KM Value [mM] |
KM Value Maximum [mM]  |
Substrate |
Reference |
|---|
    2.7.2.1 | -999 |
- |
more |
assay methods for both directions of reaction |
659856 |
| 2.7.2.1 | -999 |
- |
more |
lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods |
691204 |
| 2.7.2.1 | -999 |
- |
more |
Michaelis-Menten kinetics |
738717 |
| 2.7.2.1 | -999 |
- |
more |
Michaelis-Menten kinetics, kinetic analysis and mechanism, detailed overview |
739218 |
| 2.7.2.1 | -999 |
- |
more |
Michaelis-Menten kinetics, thermodynamics |
739591 |
| 2.7.2.1 | -999 |
- |
more |
the dependence of the activity on acetate and acetyl phosphate concentrations obeys the Michaelis-Menten kinetics, whereas the dependence on ATP and ADP concentrations is sigmoidal |
737465 |
| 2.7.2.1 | -999 |
- |
more |
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics |
738528 |
| 2.7.2.1 | 0.0026 |
- |
acetyl phosphate |
carried out at various temperatures |
642183 |
| 2.7.2.1 | 0.016 |
- |
ATP |
mutant R91A, pH 7.0 |
659446 |
| 2.7.2.1 | 0.0222 |
- |
acetyl phosphate |
at pH 8.0 and 37°C |
757471 |
