EC Number   |
Inhibitors  |
Structure |
|---|
   1.13.11.50 | Cu2+ |
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate |
   |
| 1.13.11.50 | EDTA |
largely irreversible losses |
|
| 1.13.11.50 | H2O2 |
0.1 mM, immediate and total inhibition |
|
| 1.13.11.50 | H2O2 |
1 M H2O2 causes complete loss of enzyme activity in less than 10 min, contains no Fe2+ (probably oxidized to Fe3+), partial reconstitution (40%) with 2 mM Fe2+, 20 mM Tris/HCl buffer, pH 7.5, 25°C |
|
| 1.13.11.50 | hexacyanoferrate(III) |
2.5 mM, 80% decrease in activity within 10 min |
|
| 1.13.11.50 | KCN |
largely irreversible losses |
|
| 1.13.11.50 | Mn2+ |
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate |
|
| 1.13.11.50 | more |
no inactivation effect of Fe3+ |
|
| 1.13.11.50 | Ni2+ |
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate |
|
| 1.13.11.50 | o-phenanthroline |
largely irreversible losses |
|
