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Literature summary for 1.1.3.7 extracted from

  • Hernandez-Ortega, A.; Borrelli, K.; Ferreira, P.; Medina, M.; Martinez, A.T.; Guallar, V.
    Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase (2011), Biochem. J., 436, 341-350.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene aao Pleurotus eryngii

Protein Variants

Protein Variants Comment Organism
H502A site-directed mutagenesis, the mutant shows over 1800fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity, compared to the wild-type enzyme Pleurotus eryngii
H502S site-directed mutagenesis, the mutant shows over 1200fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme Pleurotus eryngii
H546A site-directed mutagenesis, the mutant shows over 35fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme Pleurotus eryngii
H546S site-directed mutagenesis, the mutant shows decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity 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 Michaelis-Menten steady-state and transient-state kinetics of wild-type and mutant enzymes, overview Pleurotus eryngii
0.048
-
4-methoxybenzyl alcohol pH 60, 25°C, wild-type enzyme Pleurotus eryngii
0.31
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H546A Pleurotus eryngii
1.16
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H546S Pleurotus eryngii
1.289
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H502S Pleurotus eryngii
3.82
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H502A 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.
4-methoxybenzyl alcohol + O2 Pleurotus eryngii i.e. 4-anisyl alcohol 4-methoxybenzaldehyde + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Pleurotus eryngii O94219 gene aao
-

Reaction

Reaction Comment Organism Reaction ID
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 modeling protein-ligand recognition mechanisms, substrate diffusion into the AAO active site, two conserved histidine residues, His502 and His546, are involved in catalysis, structure-function analysis, overview Pleurotus eryngii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methoxybenzyl alcohol + O2 i.e. 4-anisyl alcohol Pleurotus eryngii 4-methoxybenzaldehyde + H2O2
-
?

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
0.069
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H502S Pleurotus eryngii
0.072
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H502A Pleurotus eryngii
3.5
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H546A Pleurotus eryngii
17
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H546S Pleurotus eryngii
208
-
4-methoxybenzyl alcohol pH 60, 25°C, wild-type enzyme Pleurotus eryngii

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD binding structure, overview Pleurotus eryngii

General Information

General Information Comment Organism
evolution the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis by mixed quantum mechanics/molecular mechanics studies, overview Pleurotus eryngii
additional information mixed quantum mechanics/molecular mechanics studies and molecular dynamics, overview Pleurotus eryngii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.019
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H502S Pleurotus eryngii
0.054
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H502A Pleurotus eryngii
3
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H546S Pleurotus eryngii
53
-
4-methoxybenzyl alcohol pH 60, 25°C, mutant H546A Pleurotus eryngii
4330
-
4-methoxybenzyl alcohol pH 60, 25°C, wild-type enzyme Pleurotus eryngii