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Literature summary for 1.1.3.7 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)

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

Protein Variants

Protein Variants Comment Organism
F501A site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview Pleurotus eryngii
F501Y site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview Pleurotus eryngii
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]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Pleurotus eryngii
-
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pleurotus eryngii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
anisyl alcohol + O2
-
Pleurotus eryngii anisaldehyde + H2O2
-
?
benzyl alcohol + O2
-
Pleurotus eryngii benzaldehyde + H2O2
-
?
additional information AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols Pleurotus eryngii ?
-
?
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 ?
-
?
veratryl alcohol + O2
-
Pleurotus eryngii ? + H2O2
-
?

Subunits

Subunits Comment Organism
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

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

Cofactor

Cofactor Comment Organism Structure
FAD a flavoenzyme Pleurotus eryngii

General Information

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