Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-nitrotoluene | the low extent of 4-nitrotoluene oxidation is attributable to inhibition of the enzyme by the substrate | Cyclocybe aegerita |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyclocybe aegerita | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Cyclocybe aegerita |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
117 | - |
using 3,4-dimethoxybenzyl alcohol as substrate, at 23°C, pH not specified in the publication | Cyclocybe aegerita |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3,4-dimethoxybenzyl alcohol + H2O2 | - |
Cyclocybe aegerita | 3,4-dimethoxybenzaldehyde + H2O | - |
? | |
4-nitrobenzaldehyde + H2O2 | - |
Cyclocybe aegerita | 4-nitrobenzoic acid + H2O | - |
? | |
4-nitrobenzyl alcohol + H2O2 | - |
Cyclocybe aegerita | 4-nitrobenzaldehyde + H2O | - |
? | |
4-nitrotoluene + H2O2 | APO hydroxylates 4-nitrotoluene to 4-nitrobenzyl alcohol, then to 4-nitrobenzaldehyde and then to 4-nitrobenzoic acid. The reactions proceed stepwise with total conversions of 12% for 4-nitrotoluene | Cyclocybe aegerita | 4-nitrobenzyl alcohol + H2O | - |
? | |
benzaldehyde + H2O2 | - |
Cyclocybe aegerita | benzoic acid + H2O | - |
? | |
benzyl alcohol + H2O2 | - |
Cyclocybe aegerita | benzaldehyde + H2O | - |
? | |
toluene + H2O2 | the initial product of toluene oxidation is benzyl alcohol, which then declines with concomitant production of benzaldehyde, which in turn declines with concomitant production of benzoic acid. The reactions proceed stepwise with total conversions of 93% for toluene | Cyclocybe aegerita | benzyl alcohol + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
APO | - |
Cyclocybe aegerita |
aromatic peroxygenase | - |
Cyclocybe aegerita |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Cyclocybe aegerita | isoform II, isoelectric focusing | - |
5.6 |
General Information | Comment | Organism |
---|---|---|
physiological function | APO-catalyzed reactions resemble the benzylic hydroxylations catalyzed by P450s via their H2O2-dependent peroxide shunt mechanism | Cyclocybe aegerita |