KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.013 | - |
methylene blue | lignine peroxidas activity, pH 3.5, 25°C | Bjerkandera adusta |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10% | Bjerkandera adusta |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bjerkandera adusta | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
methylene blue + H2O2 | - |
Bjerkandera adusta | ? + H2O | - |
? | |
additional information | manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity | Bjerkandera adusta | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
lignin peroxidase activity in absence of Mn2+ | Bjerkandera adusta |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
methylene blue | lignin peroxidase activity, pH 3.5, 25°C | Bjerkandera adusta |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
3 | 3.5 | lignin peroxidase activity in absence of Mn2+ | Bjerkandera adusta |