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Literature summary for 1.1.3.7 extracted from
- An aryl-alcohol oxidase of Pleurotus sapidus heterologous expression, characterization, and application in a 2-enzyme system (2016), Appl. Microbiol. Biotechnol., 100, 8021-8030 .
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2 | Pleurotus sapidus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene aao, subcloning in Saccharomyces cerevisiae strain RH1385 for the plasmid construction via homologous recombination, heterologous recombinant expression in Coprinopsis cinerea strain FA2222 under control of the promotor of the glyceraldehyde-3-phosphate dehydrogenase gene 2 (gpdII) of the button mushroom Agaricus bisporus, and enzyme secretion to the culture medium. It might be that Coprinopsis cinerea does not provide the needed signal peptidase required for cleavage of the Pleurotus sapidus AAO signal peptide | Pleurotus sapidus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5 | Pleurotus sapidus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Pleurotus sapidus | |
| 0.059 | - |
anisyl alcohol | pH 6.0, 30°C | Pleurotus sapidus |  |
| 0.529 | - |
veratryl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
| 0.784 | - |
benzyl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme posseses a signal peptide, and it is secreted | Pleurotus sapidus | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 65000 | - |
native deglycosylated enzyme | Pleurotus sapidus |
| 73000 | - |
native glycosylated enzyme | Pleurotus sapidus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pleurotus sapidus | A0A145Y386 | - |
- |
| Pleurotus sapidus DSM 8266 | A0A145Y386 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme, expressed and secreted from Coprinopsis cinerea strain FA2222, 72fold from culture supernatant by cross-flow filtration, anion exchange chromatography, and two different steps of gel filtration | Pleurotus sapidus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 88.1 | - |
purified recombinant enzyme, pH 6.0, 30°C | Pleurotus sapidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| anisyl alcohol + O2 | best substrate | Pleurotus sapidus | anisaldehyde + H2O2 | - |
? | |
| anisyl alcohol + O2 | best substrate | Pleurotus sapidus DSM 8266 | anisaldehyde + H2O2 | - |
? | |
| benzyl alcohol + O2 | - |
Pleurotus sapidus | benzaldehyde + H2O2 | - |
? | |
| benzyl alcohol + O2 | - |
Pleurotus sapidus DSM 8266 | benzaldehyde + H2O2 | - |
? | |
| additional information | a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2. Addition of H2O2 instead of enzyme AAO leads to a faster degradation by the DyP enzyme in the first 4 min, but remains static afterwards for the rest of the incubation time | Pleurotus sapidus | ? | - |
? | |
| additional information | a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2. Addition of H2O2 instead of enzyme AAO leads to a faster degradation by the DyP enzyme in the first 4 min, but remains static afterwards for the rest of the incubation time | Pleurotus sapidus DSM 8266 | ? | - |
? | |
| veratryl alcohol + O2 | - |
Pleurotus sapidus | veratrylaldehyde + H2O2 | - |
? | |
| veratryl alcohol + O2 | - |
Pleurotus sapidus DSM 8266 | veratrylaldehyde + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 64000, about, sequence calculation | Pleurotus sapidus |
| More | the enzyme in SDS-PAGE gives several bands of 73, 65, 58, 47.5, and 20 kDa, peptide mapping, overview | Pleurotus sapidus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AAO | - |
Pleurotus sapidus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Pleurotus sapidus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | 50 | the enzyme loses 86% of its activity after 12 min at 50°C, while it remains stable at 37°C for more than 20 min and retains about 90% of its activity after 1 h | Pleurotus sapidus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 38 | - |
benzyl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
| 70 | - |
veratryl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
| 203 | - |
anisyl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Pleurotus sapidus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 7 | the enzyme shows more than 90% of maximal activity, measured at pH 5.0, in the pH range between pH 4 and pH 6 and more than 80% between pH 3 and pH 7 | Pleurotus sapidus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Pleurotus sapidus | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Pleurotus sapidus | isoelectric focusing | - |
4.2 |
| Pleurotus sapidus | sequence calculation | - |
4.85 |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 48 | - |
benzyl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
| 132 | - |
veratryl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
| 3466 | - |
anisyl alcohol | pH 6.0, 30°C | Pleurotus sapidus | |
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