EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.6.1.42 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics of the first half-reaction |
758848 |
2.6.1.42 | -999 |
- |
more |
MtIlvE displays a ping-pong kinetic mechanism. Analysis of steady-state and pre-steady-state kinetic isotope effects. Michaelis-Menten kinetics |
758794 |
2.6.1.42 | -999 |
- |
more |
steady-state kinetic analysis, recombinant enzyme |
758688 |
2.6.1.42 | -999 |
- |
more |
stopped-flow kinetics analysis of half-transamination reactions, steady-state kinetics |
758697 |
2.6.1.42 | 0.034 |
- |
2-oxo-3-methylvalerate |
half transamination reaction, pH 8.0, 90°C |
738188 |
2.6.1.42 | 0.045 |
- |
4-methyl-2-oxopentanoate |
pH 8.0, 30°C |
738632 |
2.6.1.42 | 0.045 |
- |
4-methylsulfanyl-2-oxobutanoate |
- |
676421 |
2.6.1.42 | 0.06 |
- |
(R)-3-methyl-2-oxopentanoate |
pH 8.0, 25°C, substrate L-glutamate |
640031 |
2.6.1.42 | 0.06 |
- |
2-oxocaproate |
half transamination reaction, pH 8.0, 90°C |
738188 |
2.6.1.42 | 0.06 |
- |
2-oxoisocaproate |
half transamination reaction, pH 8.0, 90°C |
738188 |