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Literature summary for 1.1.3.7 extracted from

  • Hernandez-Ortega, A.; Ferreira, P.; Martinez, A.T.
    Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation (2012), Appl. Microbiol. Biotechnol., 93, 1395-1410.
    View publication on PubMed

Application

Application Comment Organism
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)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Trametes versicolor
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Fusarium solani
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Phanerodontia chrysosporium
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Botrytis cinerea
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Bjerkandera adusta
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Rigidoporus microporus
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree Postia placenta
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, recombinant expression in Escherichia coli Pleurotus eryngii

Protein Variants

Protein Variants Comment Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Trametes versicolor
-
-
extracellular
-
Fusarium solani
-
-
extracellular
-
Phanerodontia chrysosporium
-
-
extracellular
-
Botrytis cinerea
-
-
extracellular
-
Bjerkandera adusta
-
-
extracellular
-
Rigidoporus microporus
-
-
extracellular
-
Pleurotus eryngii
-
-
extracellular
-
Postia placenta
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ required for catalysis Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,4-dimethoxybenzyl alcohol + O2 Pleurotus eryngii
-
2,4-dimethoxybenzaldehyde + H2O2
-
r
2-naphthylmethanol + O2 Pleurotus eryngii best substrate 2-naphthaldehyde + H2O2
-
r
3-methoxybenzyl alcohol + O2 Pleurotus eryngii
-
3-methoxybenzaldehyde + H2O2
-
r
4-hydroxy-3-methoxybenzyl alcohol + O2 Pleurotus eryngii
-
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
r
4-hydroxybenzyl alcohol + O2 Pleurotus eryngii
-
4-hydroxybenzaldehyde + H2O2
-
r
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
4-methoxycinnamyl alcohol + O2 Pleurotus eryngii
-
4-methoxycinnamaldehyde + H2O2
-
r
4-nitrobenzyl alcohol + O2 Pleurotus eryngii
-
4-nitrobenzaldehyde + H2O2
-
r
cinnamyl alcohol + O2 Pleurotus eryngii high activity cinnamaldehyde + H2O2
-
r
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
veratryl alcohol + O2 Pleurotus eryngii
-
veratraldehyde + H2O2
-
r

Organism

Organism UniProt Comment Textmining
Bjerkandera adusta
-
-
-
Botrytis cinerea
-
-
-
Fusarium solani
-
-
-
Phanerodontia chrysosporium
-
-
-
Pleurotus eryngii O94219
-
-
Postia placenta
-
-
-
Rigidoporus microporus
-
syn. Fomes lignosus
-
Trametes versicolor
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,4-dimethoxybenzyl alcohol + O2
-
Pleurotus eryngii 2,4-dimethoxybenzaldehyde + H2O2
-
r
2-naphthylmethanol + O2
-
Pleurotus eryngii 2-naphthaldehyde + H2O2
-
r
2-naphthylmethanol + O2 best substrate Pleurotus eryngii 2-naphthaldehyde + H2O2
-
r
3-methoxybenzyl alcohol + O2
-
Pleurotus eryngii 3-methoxybenzaldehyde + H2O2
-
r
4-hydroxy-3-methoxybenzyl alcohol + O2
-
Pleurotus eryngii 4-hydroxy-3-methoxybenzaldehyde + H2O2
-
r
4-hydroxybenzyl alcohol + O2
-
Pleurotus eryngii 4-hydroxybenzaldehyde + H2O2
-
r
4-methoxybenzyl alcohol + O2
-
Pleurotus eryngii 4-methoxybenzaldehyde + H2O2
-
r
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
4-methoxycinnamyl alcohol + O2
-
Pleurotus eryngii 4-methoxycinnamaldehyde + H2O2
-
r
4-nitrobenzyl alcohol + O2
-
Pleurotus eryngii 4-nitrobenzaldehyde + H2O2
-
r
cinnamyl alcohol + O2
-
Pleurotus eryngii cinnamaldehyde + H2O2
-
r
cinnamyl alcohol + O2 high activity Pleurotus eryngii cinnamaldehyde + H2O2
-
r
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
additional information extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids Trametes versicolor ?
-
?
additional information extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids Fusarium solani ?
-
?
additional information extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids Phanerodontia chrysosporium ?
-
?
additional information extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids Botrytis cinerea ?
-
?
additional information extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids Rigidoporus microporus ?
-
?
additional information extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids Postia placenta ?
-
?
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 ?
-
?
veratryl alcohol + O2
-
Pleurotus eryngii veratraldehyde + H2O2
-
r

Subunits

Subunits Comment Organism
monomer
-
Trametes versicolor
monomer
-
Fusarium solani
monomer
-
Phanerodontia chrysosporium
monomer
-
Botrytis cinerea
monomer
-
Bjerkandera adusta
monomer
-
Rigidoporus microporus
monomer
-
Postia placenta
monomer structure-function relationship and analysis, structure comparison, overview Pleurotus eryngii

Synonyms

Synonyms Comment Organism
AAO
-
Trametes versicolor
AAO
-
Fusarium solani
AAO
-
Phanerodontia chrysosporium
AAO
-
Botrytis cinerea
AAO
-
Bjerkandera adusta
AAO
-
Rigidoporus microporus
AAO
-
Pleurotus eryngii
AAO
-
Postia placenta

Cofactor

Cofactor Comment Organism Structure
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
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
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
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
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
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
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
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

General Information Comment Organism
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Trametes versicolor
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Fusarium solani
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Phanerodontia chrysosporium
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Botrytis cinerea
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Bjerkandera adusta
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Rigidoporus microporus
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Pleurotus eryngii
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview Postia placenta
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
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
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