EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.7.2.4 | -999 |
- |
more |
at 37°C, but not at 25°C, the apparent Km for L-aspartate is highly dependent on enzyme concentration, increasing from 0.4 mM to about 50 mM. As the enzyme concentration decreases from 13.4 to 0.17 units per ml, the presence of dioxane increases apparent Km for L-aspartate |
642308 |
2.7.2.4 | -999 |
- |
more |
Km for MgCl2 3.3 mM |
642315 |
2.7.2.4 | -999 |
- |
more |
steady-state kinetics analysis of wild-type and mutant enzymes, overview |
738419 |
2.7.2.4 | 0.18 |
- |
ATP |
aspartokinase I |
642314 |
2.7.2.4 | 0.19 |
- |
L-aspartate |
pH 7.5, 60°C, mutant A157L |
642333 |
2.7.2.4 | 0.26 |
- |
ATP |
mutant K18R |
660862 |
2.7.2.4 | 0.27 |
- |
ATP |
pH 7.5, 60°C, mutant G177A |
642333 |
2.7.2.4 | 0.27 |
- |
L-aspartate |
pH 7.5, 60°C, mutant E202A |
642333 |
2.7.2.4 | 0.29 |
- |
ATP |
pH 7.5, 60°C, mutant G149A |
642333 |
2.7.2.4 | 0.32 |
- |
L-aspartate |
pH 7.5, 60°C, mutant Y8A, S12A |
642333 |