Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ferreira, P.; Hernandez-Ortega, A.; Herguedas, B.; Martinez, A.T.; Medina, M.
    Aryl-alcohol oxidase involved in lignin degradation: a mechanistic study based on steady and pre-steady state kinetics and primary and solvent isotope effects with two alcohol substrates (2009), J. Biol. Chem., 284, 24840-24847.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.7 expression of the mature enzyme in Escherichia coli Pleurotus eryngii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.7 4-anisic acid competitive 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 steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview Pleurotus eryngii
1.1.3.7 0.017
-
 O2 with 3-fluorobenzyl alcohol, 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii
1.1.3.7 0.025
-
 4-anisyl alcohol 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii
1.1.3.7 0.091
-
 2,4-hexadien-1-ol 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii
1.1.3.7 0.232
-
 O2 with 2,4-hexadien-1-ol, 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii
1.1.3.7 0.348
-
 O2 with 4-anisyl alcohol, 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii

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-hexadien-1-ol + O2 Pleurotus eryngii
-
 ?
-
 ?
1.1.3.7 4-anisyl alcohol + O2 Pleurotus eryngii the substrate is an extracellular fungal metabolite 4-anisaldehyde + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.7 Pleurotus eryngii O94219
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.7 recombinant mature enzyme from Escherichia coli by anion exchange chromatography Pleurotus eryngii

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.7 an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 a sequential mechanism in which O2 reacts with reduced enzyme before release of the aldehyde product, the AAO reductive half-reaction is essentially irreversible and rate limiting during catalysis, a synchronous mechanism in which hydride transfer from substrate alpha-carbon to FAD and proton abstraction from hydroxyl occur simultaneously, reaction mechanism, overview. The AAO catalytic mechanism proceeds via electrophilic attack and direct transfer of a hydride to the flavin Pleurotus eryngii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.7 2,4-hexadien-1-ol + O2
-
 Pleurotus eryngii ?
-
 ?
1.1.3.7 3-fluorobenzyl alcohol + O2
-
 Pleurotus eryngii ?
-
 ?
1.1.3.7 4-anisyl alcohol + O2
-
 Pleurotus eryngii 4-anisaldehyde + H2O2
-
 ?
1.1.3.7 4-anisyl alcohol + O2 the substrate is an extracellular fungal metabolite Pleurotus eryngii 4-anisaldehyde + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.7 AAO
-
 Pleurotus eryngii
1.1.3.7 More the enzyme belongs to the the glucose-methanol-choline oxidase, GMC, family of oxidoreductases Pleurotus eryngii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.7 25
-
 assay at Pleurotus eryngii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.7 129
-
 4-anisyl alcohol 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii
1.1.3.7 161
-
 2,4-hexadien-1-ol 25°C, pH 6.0, recombinant enzyme Pleurotus eryngii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.7 6
-
 assay at Pleurotus eryngii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.3.7 4 9 AAO shows no pH dependence of kcat or catalytic efficiency for the substrates analyzed, AAO is unstable above pH 9.0 Pleurotus eryngii

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.3.7 9
-
 stable up to, unstable above Pleurotus eryngii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.7 FAD
-
 Pleurotus eryngii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.3.7 additional information
-
 additional information inhibition kinetics Pleurotus eryngii
1.1.3.7 0.08
-
 4-anisic acid pH 6.0, 25°C, recombinant enzyme Pleurotus eryngii

General Information

EC Number General Information Comment Organism
1.1.3.7 metabolism aryl-alcohol oxidase, AAO, participates in fungal degradation of lignin, a process of high ecological and biotechnological relevance, by providing the hydrogen peroxide required by ligninolytic peroxidases, mechanism, overview Pleurotus eryngii
1.1.3.7 physiological function aryl-alcohol oxidase, AAO, participates in fungal degradation of lignin, a process of high ecological and biotechnological relevance, by providing the hydrogen peroxide required by ligninolytic peroxidases, mechanism, overview Pleurotus eryngii