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Results 1 - 10 of 96 > >>
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30-999 - more - 641287, 641291, 641292, 641295, 641296, 641299, 641301, 641302, 641305, 641307, 641309, 641311
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30-999 - more 2 Km-values with respect to glycerol may correspond to two different molecular species 641310
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30-999 - more assay at 25°C, increasing pH or decreasing temperature rises Km for glycerol 641294
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30-999 - more classical Michaelis-Menten kinetic pattern for the phosphatase reaction 760620
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30-999 - more Km of unpurified enzyme 641293
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 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
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.300.006 - ATP mutant enzyme V61L, at pH 7.0 and 25°C 722712
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.300.0078 - ATP wild type enzyme, at pH 7.0 and 25°C 722712
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.300.009 - ATP ATP in form of MgATP2- 701908
Results 1 - 10 of 96 > >>