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Literature summary extracted from
- Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation (2012), Appl. Microbiol. Biotechnol., 93, 1395-1410.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | synthesis | due to hydride-transfer stereoselectivity and specificity on substituted aldehydes, the enzyme is useful for flavor production and in production of chiral compounds. Flavor synthesis and enzyme stereoselectivity, overview | Pleurotus eryngii |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Trametes versicolor |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Fusarium solani |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Phanerodontia chrysosporium |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Botrytis cinerea |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Bjerkandera adusta |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Rigidoporus microporus |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree | Postia placenta |
| 1.1.3.7 | DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, recombinant expression in Escherichia coli | Pleurotus eryngii |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | H502A | site-directed mutagenesis, the mutant shows 3000fold and 1800fold decreased kcat and kred compared to the wild-type enzyme | 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 | mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base | Pleurotus eryngii |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.1.3.7 | extracellular | - |
Trametes versicolor | - |
- |
| 1.1.3.7 | extracellular | - |
Fusarium solani | - |
- |
| 1.1.3.7 | extracellular | - |
Phanerodontia chrysosporium | - |
- |
| 1.1.3.7 | extracellular | - |
Botrytis cinerea | - |
- |
| 1.1.3.7 | extracellular | - |
Bjerkandera adusta | - |
- |
| 1.1.3.7 | extracellular | - |
Rigidoporus microporus | - |
- |
| 1.1.3.7 | extracellular | - |
Pleurotus eryngii | - |
- |
| 1.1.3.7 | extracellular | - |
Postia placenta | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.3.7 | Cu2+ | required for catalysis | Phanerodontia chrysosporium |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.3.7 | 2,4-dimethoxybenzyl alcohol + O2 | Pleurotus eryngii | - |
2,4-dimethoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 2-naphthylmethanol + O2 | Pleurotus eryngii | best substrate | 2-naphthaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 3-methoxybenzyl alcohol + O2 | Pleurotus eryngii | - |
3-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-hydroxy-3-methoxybenzyl alcohol + O2 | Pleurotus eryngii | - |
4-hydroxy-3-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-hydroxybenzyl alcohol + O2 | Pleurotus eryngii | - |
4-hydroxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-methoxybenzyl alcohol + O2 | Pleurotus eryngii | high activity, 4-methoxybenzyl alcohol, is one of the best substrates of AAO, and 4-methoxybenzaldehyde (4-anisaldehyde) is the main extracellular aromatic metabolite in Pleurotus species | 4-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-methoxycinnamyl alcohol + O2 | Pleurotus eryngii | - |
4-methoxycinnamaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-nitrobenzyl alcohol + O2 | Pleurotus eryngii | - |
4-nitrobenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | cinnamyl alcohol + O2 | Pleurotus eryngii | high activity | cinnamaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | additional information | Trametes versicolor | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Fusarium solani | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Phanerodontia chrysosporium | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Botrytis cinerea | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Bjerkandera adusta | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Rigidoporus microporus | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Pleurotus eryngii | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | additional information | Postia placenta | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | ? | - |
? | |
| 1.1.3.7 | veratryl alcohol + O2 | Pleurotus eryngii | - |
veratraldehyde + H2O2 | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.3.7 | Bjerkandera adusta | - |
- |
- |
| 1.1.3.7 | Botrytis cinerea | - |
- |
- |
| 1.1.3.7 | Fusarium solani | - |
- |
- |
| 1.1.3.7 | Phanerodontia chrysosporium | - |
- |
- |
| 1.1.3.7 | Pleurotus eryngii | O94219 | - |
- |
| 1.1.3.7 | Postia placenta | - |
- |
- |
| 1.1.3.7 | Rigidoporus microporus | - |
syn. Fomes lignosus | - |
| 1.1.3.7 | Trametes versicolor | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 | catalytic mechanism with catalytic cycle including two half-reactions, overview. Proton transfer to His502 acting as a base, His546 plays a role in alcohol binding. Phe501 forces O2 to approach the flavin C4a, and His502 yielding hydrogen peroxide and the reoxidized flavin | Pleurotus eryngii |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.1.3.7 | additional information | the enzyme is found in the hyphal sheath (formed by secreted polysaccharide) during wheat straw degradation by Pleurotus eryngii under solid-state fermentation conditions. The enzyme shows initial location on the hyphal surface, but can penetrate degraded cell walls of phloem and parenchyma, and also the more lignified sclerenchymatic tissues | Pleurotus eryngii | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.3.7 | 2,4-dimethoxybenzyl alcohol + O2 | - |
Pleurotus eryngii | 2,4-dimethoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 2-naphthylmethanol + O2 | - |
Pleurotus eryngii | 2-naphthaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 2-naphthylmethanol + O2 | best substrate | Pleurotus eryngii | 2-naphthaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 3-methoxybenzyl alcohol + O2 | - |
Pleurotus eryngii | 3-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-hydroxy-3-methoxybenzyl alcohol + O2 | - |
Pleurotus eryngii | 4-hydroxy-3-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-hydroxybenzyl alcohol + O2 | - |
Pleurotus eryngii | 4-hydroxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-methoxybenzyl alcohol + O2 | - |
Pleurotus eryngii | 4-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-methoxybenzyl alcohol + O2 | high activity, 4-methoxybenzyl alcohol, is one of the best substrates of AAO, and 4-methoxybenzaldehyde (4-anisaldehyde) is the main extracellular aromatic metabolite in Pleurotus species | Pleurotus eryngii | 4-methoxybenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-methoxycinnamyl alcohol + O2 | - |
Pleurotus eryngii | 4-methoxycinnamaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | 4-nitrobenzyl alcohol + O2 | - |
Pleurotus eryngii | 4-nitrobenzaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | cinnamyl alcohol + O2 | - |
Pleurotus eryngii | cinnamaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | cinnamyl alcohol + O2 | high activity | Pleurotus eryngii | cinnamaldehyde + H2O2 | - |
r | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Trametes versicolor | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Fusarium solani | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Phanerodontia chrysosporium | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Botrytis cinerea | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Bjerkandera adusta | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Rigidoporus microporus | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Pleurotus eryngii | ? | - |
? | |
| 1.1.3.7 | additional information | AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively | Postia placenta | ? | - |
? | |
| 1.1.3.7 | additional information | AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds, extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Bjerkandera adusta | ? | - |
? | |
| 1.1.3.7 | additional information | extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Trametes versicolor | ? | - |
? | |
| 1.1.3.7 | additional information | extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Fusarium solani | ? | - |
? | |
| 1.1.3.7 | additional information | extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Phanerodontia chrysosporium | ? | - |
? | |
| 1.1.3.7 | additional information | extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Botrytis cinerea | ? | - |
? | |
| 1.1.3.7 | additional information | extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Rigidoporus microporus | ? | - |
? | |
| 1.1.3.7 | additional information | extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids | Postia placenta | ? | - |
? | |
| 1.1.3.7 | additional information | substrate specificity, overview. AAO also shows some activity on aromatic aldehydes, the highest activity on 4-nitrobenzaldehyde being about 5% of the activity for benzyl alcohol. Extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids, AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds | Pleurotus eryngii | ? | - |
? | |
| 1.1.3.7 | veratryl alcohol + O2 | - |
Pleurotus eryngii | veratraldehyde + H2O2 | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | monomer | - |
Trametes versicolor |
| 1.1.3.7 | monomer | - |
Fusarium solani |
| 1.1.3.7 | monomer | - |
Phanerodontia chrysosporium |
| 1.1.3.7 | monomer | - |
Botrytis cinerea |
| 1.1.3.7 | monomer | - |
Bjerkandera adusta |
| 1.1.3.7 | monomer | - |
Rigidoporus microporus |
| 1.1.3.7 | monomer | - |
Postia placenta |
| 1.1.3.7 | monomer | structure-function relationship and analysis, structure comparison, overview | Pleurotus eryngii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | AAO | - |
Trametes versicolor |
| 1.1.3.7 | AAO | - |
Fusarium solani |
| 1.1.3.7 | AAO | - |
Phanerodontia chrysosporium |
| 1.1.3.7 | AAO | - |
Botrytis cinerea |
| 1.1.3.7 | AAO | - |
Bjerkandera adusta |
| 1.1.3.7 | AAO | - |
Rigidoporus microporus |
| 1.1.3.7 | AAO | - |
Pleurotus eryngii |
| 1.1.3.7 | AAO | - |
Postia placenta |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Trametes versicolor | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Fusarium solani | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Phanerodontia chrysosporium | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Botrytis cinerea | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Bjerkandera adusta | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Rigidoporus microporus | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Pleurotus eryngii | |
| 1.1.3.7 | FAD | the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins | Postia placenta | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Trametes versicolor |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Fusarium solani |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Phanerodontia chrysosporium |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Botrytis cinerea |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Bjerkandera adusta |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Rigidoporus microporus |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Pleurotus eryngii |
| 1.1.3.7 | evolution | the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview | Postia placenta |
| 1.1.3.7 | additional information | structure-function relationship and analysis, overview. His502 activates the alcohol substrate by proton abstraction. Alcohol docking at the buried AAO active site results in only one catalytically relevant position for concerted transfer, with the pro-R alpha-hydrogen at distance for hydride abstraction, the enzyme shows hydride-transfer stereoselectivity | Pleurotus eryngii |
| 1.1.3.7 | physiological function | the enzyme is part of the extracellular enzymatic machinery of the fungus to degrade lignin. The secreted, extracellular oxidase generates H2O2 for extracellular peroxidases | Phanerodontia chrysosporium |
| 1.1.3.7 | physiological function | the enzyme is part of the extracellular enzymatic machinery of the fungus to degrade lignin. The secreted, extracellular oxidase generates H2O2 for extracellular peroxidases. O2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of 4-methoxylated benzylic metabolites secreted by the fungus. AAO provides a continuous supply of H2O2 by redox cycling phenolic benzylic alcohol compounds, in collaboration with mycelium dehydrogenases | Pleurotus eryngii |
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