Protein Variants | Comment | Organism |
---|---|---|
E190Q | the mutation drastically diminishes the kinetic affinity of this site for Mg2+ and Mn2+ | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.007 | - |
D-fructose 6-phosphate | mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.007 | - |
D-fructose 6-phosphate | mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.008 | - |
ATP | wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.012 | - |
ATP | wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.018 | - |
D-fructose 6-phosphate | wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.037 | - |
D-fructose 6-phosphate | wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.049 | - |
ATP | mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.117 | - |
ATP | mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required to obtain full activity of the enzyme | Escherichia coli | |
Mn2+ | required to obtain full activity of the enzyme. The affinity for Mn2+ is 13fold higher compared to that of Mg2+ | Escherichia coli | |
additional information | Cu2+, Zn2+ and Cd2+ do not significantly support the enzymatic activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-fructose 6-phosphate | - |
Escherichia coli | ADP + D-fructose 1,6-bisphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Pfk-2 | - |
Escherichia coli |
phosphofructokinase-2 | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.037 | - |
ATP | wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
0.24 | - |
ATP | mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
9 | - |
ATP | mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
62 | - |
ATP | wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2 | - |
ATP | mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
180 | - |
ATP | mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
5200 | - |
ATP | wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli | |
7000 | - |
ATP | wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication | Escherichia coli |