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Literature summary extracted from

  • Munteanu, F.; Ferreira, P.; Ruiz-Duenas, F.; Martinez, A.; Cavaco-Paulo, A.
    ioelectrochemical investigations of aryl-alcohol oxidase from Pleurotus eryngii (2008), J. Electroanal. Chem., 618, 83-86.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.7 expression of wild-type enzyme in Escherichia coli, expression of wild-type and mutant enzymes in Emericella nidulans Pleurotus eryngii

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.7 F501A site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview Pleurotus eryngii
1.1.3.7 F501Y site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview Pleurotus eryngii
1.1.3.7 additional information wild-type and mutant enzymes are adsorbed on graphite electrodes or with the enzymes in solution using glassy carbon electrode as working electrode, activity analysis, overview Pleurotus eryngii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.7 additional information
-
 additional information Michaelis–Menten kinetics and redox potentials of wild-type and mutant enzymes, overview Pleurotus eryngii
1.1.3.7 0.027
-
 veratryl alcohol wild-type enzyme expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.044
-
 veratryl alcohol mutant F501A expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.05
-
 veratryl alcohol wild-type enzyme expressed in Escherichia coli Pleurotus eryngii
1.1.3.7 0.051
-
 benzyl alcohol mutant F501A expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.108
-
 anisyl alcohol mutant F501A expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.12
-
 anisyl alcohol mutant F501Y expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.123
-
 veratryl alcohol mutant F501Y expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.189
-
 benzyl alcohol mutant F501Y expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.39
-
 benzyl alcohol wild-type enzyme expressed in Escherichia coli Pleurotus eryngii
1.1.3.7 0.794
-
 anisyl alcohol wild-type enzyme expressed in Escherichia coli Pleurotus eryngii
1.1.3.7 0.836
-
 anisyl alcohol wild-type enzyme expressed in Emericella nidulans Pleurotus eryngii
1.1.3.7 0.947
-
 benzyl alcohol wild-type enzyme expressed in Emericella nidulans Pleurotus eryngii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.7 extracellular
-
 Pleurotus eryngii
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.7 additional information Pleurotus eryngii AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols ?
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.7 anisyl alcohol + O2
-
 Pleurotus eryngii anisaldehyde + H2O2
-
 ?
1.1.3.7 benzyl alcohol + O2
-
 Pleurotus eryngii benzaldehyde + H2O2
-
 ?
1.1.3.7 additional information AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols Pleurotus eryngii ?
-
 ?
1.1.3.7 additional information during catalysis the non-covalently bound FAD cofactor is reduced by the substrate and subsequently reoxidized by molecular oxygen to yield hydrogen peroxide. The AAO substrate-binding pocket is located on the si side of the flavin ring and connected to the exposed surface by a hydrophobic substrate access channel. Two putative catalytic histidines, H502 and H546, are essential in AAO activity as a possible general bases in AAO catalysis. Residue F501, located near of cofactor and the putative catalytic histidines, is also involved in substrate oxidation by AAO Pleurotus eryngii ?
-
 ?
1.1.3.7 veratryl alcohol + O2
-
 Pleurotus eryngii ? + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.7 More the molecular model of AAO from Pleurotus eryngii, PDB entry 1QJN, shows that it is a globular protein with common features with the overall structure topology of the other members of glucose-methanol-choline oxidoreductases family Pleurotus eryngii

Synonyms

EC Number Synonyms Comment Organism
1.1.3.7 AAO
-
 Pleurotus eryngii
1.1.3.7 More the enzyme belongs to the glucose-methanol-choline oxidoreductases, GMC, family Pleurotus eryngii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.7 FAD a flavoenzyme Pleurotus eryngii

General Information

EC Number General Information Comment Organism
1.1.3.7 physiological function aryl-alcohol oxidase provides hydrogen peroxide necessary for peroxidase activity during lignin biodegradation Pleurotus eryngii