EC Number   |
pH Minimum |
pH Maximum |
Reference |
|---|
   1.3.3.5 | -999 |
- |
inactive at pH 9.2 |
745422 |
| 1.3.3.5 | 3 |
9.5 |
activity range, inactive above and below. In reaction with electron donor substrates, the enzyme exhibits the maximal activity at acidic pH values: pH 4.0 for 2,2'-azino-bis-[3-ethylbenzthiazoline-6-sulfonic acid] (ABTS) and pH 3.0 for potassium ferricyanide. Catalytic activity decreases on pH increase, and the enzyme becomes completely inactive at pH above 9.5. At neutral pH values, bilirubin oxidase retains about 50% maximal activity in oxidation of both substrates. In reaction with a hydrogen atom donor (catechol), the pH profile of the enzyme activity is shifted to alkaline values: enzymatic activity is not exhibited at pH below 6.0. This is probably related with the higher reactivity of the substrate as a phenolate anion |
744280 |
| 1.3.3.5 | 3.5 |
4.5 |
using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate |
684405 |
| 1.3.3.5 | 4 |
9 |
analysis of pH dependence of the enzyme immobilized on electrodes, detailed overview |
744449 |
| 1.3.3.5 | 4 |
9 |
for the indigo carmine dye decolorization reaction |
686900 |
| 1.3.3.5 | 4 |
9 |
using Remazol Brilliant Blue R as subsrate |
687851 |
| 1.3.3.5 | 4.5 |
8.2 |
under acidic condition enzyme oxidizes only conjugated bilirubin |
391034 |
| 1.3.3.5 | 5 |
8.5 |
activity range with substrate remazol brilliant blue R, profile overview |
712520 |
| 1.3.3.5 | 6 |
7.6 |
- |
673257 |
| 1.3.3.5 | 6.5 |
8 |
using p-phenylenediamine or o-aminophenol as a substrate |
684405 |
