EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.4.3.4 | -999 |
- |
more |
- |
394551, 394562, 394572, 394573, 394577, 656683 |
| 1.4.3.4 | -999 |
- |
more |
comparison of Km of MAO expressed in Saccharomyces cerevisiae and Pichia pastoris |
394552 |
| 1.4.3.4 | -999 |
- |
more |
comparison of Km of mutant enzymes using serotonin, phenylethylamine, tyramine, tryptamine as substrates |
394556 |
| 1.4.3.4 | -999 |
- |
more |
comparison of MAO-A mutants using kynuramine, benzylamine and para-substituted benzylamine analogues as substrates |
394553 |
| 1.4.3.4 | -999 |
- |
more |
determination of substrate-dependent steady-state and stopped flow kinetics, pH dependence, overview |
703627 |
| 1.4.3.4 | -999 |
- |
more |
effect of phospholipids on Km |
394570, 394571 |
| 1.4.3.4 | -999 |
- |
more |
kinetic constants for pure hMAO-B oxidising different substrates in the presence of reversible competitive inhibitors or reversible non-competitive/mixed inhibitors |
720287 |
| 1.4.3.4 | -999 |
- |
more |
kinetics |
706847 |
| 1.4.3.4 | -999 |
- |
more |
kinetics with substrate kynuramine |
701958 |
| 1.4.3.4 | -999 |
- |
more |
Km of membrane-bound and 1-O-n-octyl-beta-D-glucopyranoside-treated enzyme |
394566, 394567 |
