EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.1.1.27 | -999 |
- |
more |
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, kinetic analysis of the recombinant enzyme, overview |
740460 |
| 1.1.1.27 | -999 |
- |
more |
an allosteric enzyme |
688389 |
| 1.1.1.27 | -999 |
- |
more |
enzyme kinetics, ordered bibi kinetic mechanism of nLDH with the coenzyme binding first |
740458 |
| 1.1.1.27 | -999 |
- |
more |
influence of pH |
286448 |
| 1.1.1.27 | -999 |
- |
more |
isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH |
686679 |
| 1.1.1.27 | -999 |
- |
more |
kinetics analysis |
686648 |
| 1.1.1.27 | -999 |
- |
more |
kinetics, the enzyme is allosteric in presence of D-fructose 1,6-bisphosphate, overview |
711181 |
| 1.1.1.27 | -999 |
- |
more |
Km values for pyruvate, NADH, (S)-lactate and NAD+ are measured in the solubilized mirochondrial Hep G2 fractions. They differ from the values measured in the cytosolic fractions |
747163 |
| 1.1.1.27 | -999 |
- |
more |
KM-values at position of temperatur minimum |
286462 |
| 1.1.1.27 | -999 |
- |
more |
KM-values for mutant enzymes with enlarged loop |
286458 |
