EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.11.1.11 | -999 |
- |
more |
- |
439855 |
| 1.11.1.11 | -999 |
- |
more |
ascorbate can saturate the ascorbate-dependent hemoperoxidase activity indicating that the enzyme obeys Michaelis-Menten kinetics |
439880 |
| 1.11.1.11 | -999 |
- |
more |
both forms of the enzyme show a very high affinity for H2O2, Km values below 0.005 |
439856 |
| 1.11.1.11 | -999 |
- |
more |
kinetics, overview |
764715 |
| 1.11.1.11 | -999 |
- |
more |
Km of recombinant enzyme-B produced in E. coli |
439881 |
| 1.11.1.11 | -999 |
- |
more |
Km values comparable with those of higher plants |
439876 |
| 1.11.1.11 | -999 |
- |
more |
pre-steady state and steady-state kinetic analysis of wild-type and mutant enzymes, formation of high-valent Compound I and Compound II intermediates, detailed overview. The steady-state oxidation of ascorbate by APX does not obey simple Michaelis-Menten kinetics, and a sigmoidal dependence of rate on substrate concentration is observed. The mutant A134P variant behaves similarly. In contrast, oxidation of guaiacol by A134P exhibits conventional Michaelis-Menten type kinetics |
765196 |
| 1.11.1.11 | -999 |
- |
more |
steady-state Michaelis-Menten kietics |
764871 |
| 1.11.1.11 | -999 |
- |
more |
the reaction does not follow Michaelis-Menten kinetics, Hill plots |
439855 |
| 1.11.1.11 | -999 |
- |
more |
untreated cells, sigmoidal dependence of reaction rate on ascorbate concentration, in heat shock cells, hyperbolic dependence of reaction rate on ascorbate concentration and 5-fold decrease in Km-value |
657063 |
