EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    4.3.3.7 | -999 |
- |
more |
kinetic mechanism |
33920 |
| 4.3.3.7 | -999 |
- |
more |
kinetic modeling |
729237 |
| 4.3.3.7 | -999 |
- |
more |
kinetic study: the wild-type enzyme shows a ping pong mechanism, while the monomeric mutant L197D/Y107W shows ternary-complex mechanism |
713953 |
| 4.3.3.7 | -999 |
- |
more |
Michaelis-Menten kinetics |
730624 |
| 4.3.3.7 | -999 |
- |
more |
Michaelis-Menten kinetics for wild-type and mutant enzymes, overview |
714351 |
| 4.3.3.7 | 0.05 |
- |
L-aspartate 4-semialdehyde |
mutant L170E/G191E, at 30°C |
704696 |
| 4.3.3.7 | 0.05 |
- |
pyruvate |
pH not specified in the publication, 30°C, recombinant mutant DELTAAsp237 |
714351 |
| 4.3.3.7 | 0.052 |
- |
L-aspartate 4-semialdehyde |
at 30°C, in 100 mM HEPES buffer, pH 8.0 |
702445 |
| 4.3.3.7 | 0.07 |
- |
L-aspartate-4-semialdehyde |
pH 8.0, 30°C |
749039 |
| 4.3.3.7 | 0.07 |
- |
pyruvate |
pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171 |
714351 |
