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Literature summary for 1.1.3.47 extracted from

  • Ferreira, P.; Hernandez-Ortega, A.; Lucas, F.; Carro, J.; Herguedas, B.; Borrelli, K.W.; Guallar, V.; Martinez, A.T.; Medina, M.
    Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase (2015), FEBS J., 282, 3091-3106 .
    View publication on PubMed
Search for more literature for 1.1.3.47

Cloned(Commentary)

Cloned (Comment) Organism
gene aao, recombinant enzyme expression in Escherichia coli Pleurotus eryngii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6
-
 5-hydroxymethylfurfural pH 6.0, 25°C Pleurotus eryngii
3.3
-
 2,5-diformylfuran pH 6.0, 25°C Pleurotus eryngii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Pleurotus eryngii
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,5-diformylfuran + 2 O2 Pleurotus eryngii
-
 2,5-furandicarboxylic acid + H2O2
-
 ir
5-hydroxymethylfurfural + O2 Pleurotus eryngii
-
 2,5-diformylfuran + H2O2
-
 ?
additional information Pleurotus eryngii the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pleurotus eryngii O94219
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Pleurotus eryngii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,5-diformylfuran + 2 O2
-
 Pleurotus eryngii 2,5-furandicarboxylic acid + H2O2
-
 ir
2,5-hydroxymethylfurancarboxylic acid + O2 very low activity Pleurotus eryngii 2,5-furandicarboxylic acid + H2O2
-
 ?
5-(hydroxymethyl)furan-2-carboxylic acid + O2 very low activity Pleurotus eryngii 2,5-furandicarboxylic acid + ?
-
 ?
5-hydroxymethylfurfural + O2
-
 Pleurotus eryngii 2,5-diformylfuran + H2O2
-
 ?
5-hydroxymethylfurfural + O2
-
 Pleurotus eryngii 5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
 ?
5-hydroxymethylfurfural + O2
-
 Pleurotus eryngii 5-hydroxymethylfuran-2-carboxylic acid + H2O2
-
 ?
additional information the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid Pleurotus eryngii ?
-
 ?
additional information enzyme AAO is also able to oxidize some furanic compounds such as 5-hydroxymethylfurfural (HMF) and 2,5-diformylfuran (DFF), it has very low activity on 2,5-hydroxymethylfurancarboxylic acid, no activity with 2,5-formylfurancarboxylic acid. NMR analysis of the compounds Pleurotus eryngii ?
-
 ?

Synonyms

Synonyms Comment Organism
AAO
-
 Pleurotus eryngii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Pleurotus eryngii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
20.1
-
 5-hydroxymethylfurfural pH 6.0, 25°C Pleurotus eryngii
31.4
-
 2,5-diformylfuran pH 6.0, 25°C Pleurotus eryngii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Pleurotus eryngii

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Pleurotus eryngii

General Information

General Information Comment Organism
metabolism the enzyme is important in the 5-hydroxymethylfurfural degradation pathway, verview Pleurotus eryngii
physiological function the enzyme is involved in lignin degradation. Within this multienzymatic process, which enables the recycling of carbon fixed by photosynthesis in land ecosystems, AAO reduces O2, providing the H2O2 required by ligninolytic peroxidases to oxidize the recalcitrant lignin polymer Pleurotus eryngii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0167
-
 5-(hydroxymethyl)furan-2-carboxylic acid pH 6.0, 25°C Pleurotus eryngii
0.0167
-
 2,5-hydroxymethylfurancarboxylic acid pH 6.0, 25°C Pleurotus eryngii
0.157
-
 2,5-diformylfuran pH 6.0, 25°C Pleurotus eryngii
0.215
-
 5-hydroxymethylfurfural pH 6.0, 25°C Pleurotus eryngii