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Literature summary extracted from

  • Varela, E.; Guillen, F.; Martinez, A.T.; Martinet, M.J.
    Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans purification and characterization of the recombinant enzyme (2001), Biochim. Biophys. Acta, 1546, 107-113 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.7 expression in Aspergillus nidulans Pleurotus eryngii

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.7 synthesis expression of AAO in the ascomycete Aspergillus nidulans. The activity of the recombinant enzyme in Aspergillus nidulans cultures is much higher than found in the extracellular fluid of Pleurotus eryngii. The recombinant enzyme shows the same molecular mass, pI and catalytic properties as that of the mature protein secreted by Pleurotus eryngii Pleurotus eryngii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.7 0.03
-
 4-anisyl alcohol recombinant enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.04
-
 4-anisyl alcohol native enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.22
-
 3-anisyl alcohol native enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.3
-
 3-anisyl alcohol recombinant enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.41
-
 veratryl alcohol native enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.56
-
 veratryl alcohol recombinant enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.63
-
 benzyl alcohol recombinant enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii
1.1.3.7 0.85
-
 benzyl alcohol native enzyme, pH 6, temperature not specified in the publication Pleurotus eryngii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.7 70000
-
 gel filtration Pleurotus eryngii

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.7 Pleurotus eryngii O94219
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.1.3.7 glycoprotein enzyme contains about 14% N-linked carbohydrates Pleurotus eryngii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.7 3-anisyl alcohol + O2
-
 Pleurotus eryngii 3-anisyl aldehyde + H2O2
-
 ?
1.1.3.7 4-anisyl alcohol + O2
-
 Pleurotus eryngii 4-anisyl aldehyde + H2O2
-
 ?
1.1.3.7 benzyl alcohol + O2
-
 Pleurotus eryngii benzyl aldehyde + H2O2
-
 ?
1.1.3.7 veratryl alcohol + O2
-
 Pleurotus eryngii veratryl aldehyde + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.7 monomer 1 * 72500, SDS-PAGE Pleurotus eryngii

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.3.7 Pleurotus eryngii isoelectric focusing
-
 3.8