Cloned (Comment) | Organism |
---|---|
gene aao, expression of wild-type and mutant emzymes in Escherichia coli | Pleurotus eryngii |
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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten steady-state and transient-state kinetics of overall and half-reactions of wild-type and mutant enzymes by (anaerobic) stopped-flow spectrophotometry, changes in the flavin redox state, detailed overview | Pleurotus eryngii | |
0.049 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, wild-type enzyme | Pleurotus eryngii | |
0.31 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H546A | Pleurotus eryngii | |
1.16 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H546S | Pleurotus eryngii | |
1.289 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H502S | Pleurotus eryngii | |
3.82 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H502A | Pleurotus eryngii |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Pleurotus eryngii | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pleurotus eryngii | O94219 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant emzymes from Escherichia coli to homogeneity | Pleurotus eryngii |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 | two conserved histidine residues, His502 and His546, are involved in catalysis and play roles in the two half-reactions, with a stronger histidine involvement in the reductive than in the oxidative half-reaction. His502 is the catalytic base in the AAO reductive half-reaction. The His502 proton transfer does not limit the oxidative half-reaction, stereoselective hydride transfer. Quantum mechanical/molecular mechanical study, mutational analysis, and computational simulations, detailed overview | Pleurotus eryngii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-methoxybenzyl alcohol + O2 | i.e. 4-anisyl alcohol | Pleurotus eryngii | 4-methoxybenzaldehyde + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AAO | - |
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 |
---|---|---|---|---|---|
0.069 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H502S | Pleurotus eryngii | |
0.072 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H502A | Pleurotus eryngii | |
3.5 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H546A | Pleurotus eryngii | |
17 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H546S | Pleurotus eryngii | |
197 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, wild-type enzyme | Pleurotus eryngii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Pleurotus eryngii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 9 | pH-dependencies of wild-type and mutant enzymes, overview | Pleurotus eryngii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | changes in the flavin redox state during catalysis, overview | Pleurotus eryngii |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the glucosemethanolcholine oxidase superfamily | Pleurotus eryngii |
physiological function | the flavoenzyme aryl-alcohol oxidase is involved in lignin degradation | Pleurotus eryngii |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.019 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H502S | Pleurotus eryngii | |
0.054 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H502A | Pleurotus eryngii | |
3 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H546S | Pleurotus eryngii | |
53 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, mutant H546A | Pleurotus eryngii | |
3980 | - |
4-methoxybenzyl alcohol | pH 6.0, 25°C, wild-type enzyme | Pleurotus eryngii |