EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.3.1.37 | -999 |
- |
more |
- |
486815, 486820, 486845 |
2.3.1.37 | -999 |
- |
more |
kinetics analysis of wild-type and mutant enzymes, single and multiple turnover and stopped flow measurements, substrate protection study, overview |
736116 |
2.3.1.37 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics, overview |
735711 |
2.3.1.37 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics, two-step sequential kinetic mechanism , and thermodynamics. Both the reaction for wild-type hALAS2 and those for the X-linked protoporphyria variants comprised a single kinetic step associated with quinonoid intermediate formation followed by one decay step. Rates for the two steps range from 9.8-14.3/s and from 1.37-1.97 s for the reactions of the XLPP variants, whereas those for the wild-type hALAS2-catalyzed reaction are 6.6/s and 0.70/s |
735684 |
2.3.1.37 | -999 |
- |
more |
overview |
486820 |
2.3.1.37 | -999 |
- |
more |
pre-steady state and steady state kinetics, overview |
736454 |
2.3.1.37 | -999 |
- |
more |
pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, stopped-flow measurements, single and mutiple turnover rates, equilibrium dissociation constants, binding isotherms, detailed overview |
736491 |
2.3.1.37 | 0.00032 |
- |
glycine |
pH 7.5, 30°C, ALAS(K313A mutant)/ALAS |
718696 |
2.3.1.37 | 0.00045 |
- |
glycine |
pH 7.5, 30°C, ALAS/ALAS |
718696 |
2.3.1.37 | 0.00054 |
- |
butanoyl-CoA |
mutant R85L/T430V, pH 7.5, 30°C |
706627 |