Cloned (Comment) | Organism |
---|---|
expression of the mature enzyme in Escherichia coli | Pleurotus eryngii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-anisic acid | competitive | Pleurotus eryngii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview | Pleurotus eryngii | |
0.017 | - |
O2 | with 3-fluorobenzyl alcohol, 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii | |
0.025 | - |
4-anisyl alcohol | 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii | |
0.091 | - |
2,4-hexadien-1-ol | 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii | |
0.232 | - |
O2 | with 2,4-hexadien-1-ol, 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii | |
0.348 | - |
O2 | with 4-anisyl alcohol, 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,4-hexadien-1-ol + O2 | Pleurotus eryngii | - |
? | - |
? | |
4-anisyl alcohol + O2 | Pleurotus eryngii | the substrate is an extracellular fungal metabolite | 4-anisaldehyde + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pleurotus eryngii | O94219 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant mature enzyme from Escherichia coli by anion exchange chromatography | Pleurotus eryngii |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,4-hexadien-1-ol + O2 | - |
Pleurotus eryngii | ? | - |
? | |
3-fluorobenzyl alcohol + O2 | - |
Pleurotus eryngii | ? | - |
? | |
4-anisyl alcohol + O2 | - |
Pleurotus eryngii | 4-anisaldehyde + H2O2 | - |
? | |
4-anisyl alcohol + O2 | the substrate is an extracellular fungal metabolite | Pleurotus eryngii | 4-anisaldehyde + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AAO | - |
Pleurotus eryngii |
More | the enzyme belongs to the the glucose-methanol-choline oxidase, GMC, family of oxidoreductases | Pleurotus eryngii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pleurotus eryngii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
129 | - |
4-anisyl alcohol | 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii | |
161 | - |
2,4-hexadien-1-ol | 25°C, pH 6.0, recombinant enzyme | Pleurotus eryngii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Pleurotus eryngii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
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 | pH Stability Maximum | Comment | Organism |
---|---|---|---|
9 | - |
stable up to, unstable above | Pleurotus eryngii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Pleurotus eryngii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics | Pleurotus eryngii | |
0.08 | - |
4-anisic acid | pH 6.0, 25°C, recombinant enzyme | Pleurotus eryngii |
General Information | Comment | Organism |
---|---|---|
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 |
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 |