EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.7.1.30 | -999 |
- |
more |
- |
641287, 641291, 641292, 641295, 641296, 641299, 641301, 641302, 641305, 641307, 641309, 641311 |
2.7.1.30 | -999 |
- |
more |
2 Km-values with respect to glycerol may correspond to two different molecular species |
641310 |
2.7.1.30 | -999 |
- |
more |
assay at 25°C, increasing pH or decreasing temperature rises Km for glycerol |
641294 |
2.7.1.30 | -999 |
- |
more |
classical Michaelis-Menten kinetic pattern for the phosphatase reaction |
760620 |
2.7.1.30 | -999 |
- |
more |
Km of unpurified enzyme |
641293 |
2.7.1.30 | -999 |
- |
more |
Michaelis-Menten kinetics, Tk-GK shows no negative cooperativity for ATP binding, the hexamer formation maintains a high ATP binding affinity |
761561 |
2.7.1.30 | -999 |
- |
more |
the enzyme exhibits two-step kinetics as a function of ATP at a fixed Mg2+ concentration due to the formation of multiple Mg-ATP complexes at different Mg2+ to ATP molar ratio. The active site of glycerol kinase shows different catalytic property with respect to different Mg-ATP complexes. Glycerol kinase exhibits high affinity (low Km) and less activity (low kcat) for complexes with a stoichiometric or over-stoichiometric constitution like Mg2+-ATP. On the other hand, the enzyme shows less affinity (high Km) and high activity (high kcat) for unsaturated complexes like [Mg(ATP)2]6-. Detailed kinetic analysis of glycerol kinase as a function of Mg2+ to ATP molar ratio, overview. The enzyme exhibits Michaelis-Menten kinetics. The two-step kinetic behavior of glycerol kinase as function of ATP at a fixed Mg2+ concentration can rather be explained due to the various Mg-ATP complexes formed at different Mg2+/ATP molar ratios that bind to the active site. In consequence, different Km and kcat values are determined with respect to the different Mg-ATP complexes |
761883 |
2.7.1.30 | 0.006 |
- |
ATP |
mutant enzyme V61L, at pH 7.0 and 25°C |
722712 |
2.7.1.30 | 0.0078 |
- |
ATP |
wild type enzyme, at pH 7.0 and 25°C |
722712 |
2.7.1.30 | 0.009 |
- |
ATP |
ATP in form of MgATP2- |
701908 |