EC Number   |
pH Minimum |
pH Maximum |
Reference |
|---|
   1.11.1.13 | -999 |
- |
MnP is active in a broad pH-range |
439838 |
| 1.11.1.13 | 2 |
6 |
active in the range, below pH 2 and above pH 6: completely inactive |
439845 |
| 1.11.1.13 | 3 |
3.5 |
pH 3.5: decrease of 95% of oxidation of Mn2+, pH 3: nearly no oxidation of Mn2+ |
439847 |
| 1.11.1.13 | 3 |
5 |
oxidation of veratryl alcohol decreases more than 95% when the pH is increased from 3 to 4.5 and nearly absent at pH 5 |
439847 |
| 1.11.1.13 | 3 |
8 |
activity range, profile overview |
765759 |
| 1.11.1.13 | 3 |
8 |
the highest activity of all enzymes with all tested substrates is at pH 3, except for the WT with 2,6-DMP as a substrate, for which the activity is almost twice as high at pH 8 than that at pH 3. Although the activity of the mutants towards ABTS drops to 5-10% at pH 5 and higher, the residual activities of the mutants towards Reactive Black 5 and veratryl alcohol drops less at higher pH values (20-40% residual activity at pH 5). For 2,6-dimethoxyphenol as a substrate, the activities of MrMnP1 and mutants are lowest at pH 6, but increase at pH 7 and pH 8. The activity at high pH values is transient, presumably due to Ca2+ loss and inactivation of the enzyme. Autoxidation of 2,6-DMP in Britton Robinson buffer at pH 8 in the presence of H2O2 is not detected |
764473 |
| 1.11.1.13 | 3.1 |
6.1 |
veratryl alcohol oxidation, activity increases with increasing pH |
439831 |
| 1.11.1.13 | 3.1 |
8.3 |
in presence of H2O2 the formation of enzyme compound I is independent of pH over the range |
439816 |
| 1.11.1.13 | 3.5 |
4.5 |
optima for Mn2+-independent 2,6-dimethoxyphenol oxidation |
699016 |
| 1.11.1.13 | 3.5 |
5.5 |
over 50% of maximal activity within this range |
765693 |
