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Literature summary extracted from
- Induction and purification by three-phase partitioning of aryl alcohol oxidase (AAO) from Pleurotus ostreatus (2011), Appl. Biochem. Biotechnol., 163, 423-432.
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.3.7 | 0.6 | - |
veratryl alcohol | pH 6.0, 40°C | Pleurotus ostreatus |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.7 | 67000 | - |
gel filtration | Pleurotus ostreatus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.3.7 | Pleurotus ostreatus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.3.7 | three-phase partitioning with 30% (w/v) of ammonium sulfate and t-butanol (1:1 ratio) | Pleurotus ostreatus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.7 | 0.155 | - |
crude enzyme, using veratryl alcohol as substrate, at pH 6.0, 40°C | Pleurotus ostreatus |
| 1.1.3.7 | 1.58 | - |
after 10.19fold purification, using veratryl alcohol as substrate, at pH 6.0, 40°C | Pleurotus ostreatus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.3.7 | 4-anisyl alcohol + O2 | best substrate | Pleurotus ostreatus | 4-anisaldehyde + H2O2 | - |
? | |
| 1.1.3.7 | benzyl alcohol + O2 | - |
Pleurotus ostreatus | benzaldehyde + H2O2 | - |
? | |
| 1.1.3.7 | veratryl alcohol + O2 | - |
Pleurotus ostreatus | veratraldehyde + H2O2 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | AAO | - |
Pleurotus ostreatus |
| 1.1.3.7 | aryl alcohol oxidase | - |
Pleurotus ostreatus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.7 | 40 | - |
- |
Pleurotus ostreatus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.7 | 30 | 60 | the enzyme completely loses its activity at 60°C | Pleurotus ostreatus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.7 | 5.5 | 6 | - |
Pleurotus ostreatus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.7 | 4 | 7 | the enzyme displays over 63% of its activity in the pH range of 4.0-7.0. A further increase of these pH values decreases the relative activity to 17% | Pleurotus ostreatus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.3.7 | FAD | - |
Pleurotus ostreatus | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.1.3.7 | Pleurotus ostreatus | compared with the control, inducers increased the AAO production in Pleurotus ostreatus in the following order: L-tyrosine (5 mM) > veratryl alcohol (7 mM) > benzyl alcohol (10 mM) > L-phenylalanine (5 mM) > 4-anisyl alcohol (9 mM) | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | physiological function | aryl alcohol oxidase is involved in lignin degradation | Pleurotus ostreatus |
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