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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | MichaelisMenten 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Pleurotus eryngii | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pleurotus eryngii | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
AAO | - |
Pleurotus eryngii |
More | the enzyme belongs to the glucose-methanol-choline oxidoreductases, GMC, family | Pleurotus eryngii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | a flavoenzyme | Pleurotus eryngii |
General Information | Comment | Organism |
---|---|---|
physiological function | aryl-alcohol oxidase provides hydrogen peroxide necessary for peroxidase activity during lignin biodegradation | Pleurotus eryngii |