EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   1.11.1.16 | 1-methylanthracene + H2O2 |
at 43% of the rate with 9-methylanthracene |
Bjerkandera adusta |
1-methylanthraquinone + H2O |
- |
? |
| 1.11.1.16 | 1-naphthol + H2O2 |
- |
Bjerkandera adusta |
? + H2O |
- |
? |
| 1.11.1.16 | 2 Mn(II) + 2 H+ + H2O2 |
- |
Bjerkandera adusta |
2 Mn(III) + 2 H2O |
- |
? |
| 1.11.1.16 | 2 Mn(II) + 2 H+ + H2O2 |
oxidation of Mn2+ to Mn3+ (manganese peroxidase activity) is measured as the H2O2-dependent formation of the complex malonate-Mn3+ |
Bjerkandera adusta |
2 Mn(III) + 2 H2O |
- |
? |
| 1.11.1.16 | 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2 |
- |
Bjerkandera adusta |
? |
- |
? |
| 1.11.1.16 | 2,6-dimethoxyphenol + 2 H+ + H2O2 |
substrate 2,6-dimethoxyphenol (DMP) is transformed at the distal site of heme prosthetic group (lignin peroxidase activity) |
Bjerkandera adusta |
oxidized 2,6-dimethoxyphenol + 2 H2O |
- |
? |
| 1.11.1.16 | 2,6-dimethoxyphenol + H+ + H2O2 |
- |
Bjerkandera adusta |
? |
- |
? |
| 1.11.1.16 | 2-methylanthracene + H2O2 |
at 24% of the rate with 9-methylanthracene |
Bjerkandera adusta |
2-methylanthraquinone + H2O |
- |
? |
| 1.11.1.16 | 3-methyl-2-benzothiazolinone hydrazone + H2O2 |
enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+ |
Bjerkandera adusta |
? + H2O |
- |
? |
| 1.11.1.16 | 9-methylanthracene + H2O2 |
- |
Bjerkandera adusta |
10-methylanthracene-9-one + H2O |
- |
? |
