Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Pseudomonas sp. |
Crystallization (Comment) | Organism |
---|---|
complexed with L-Phe and L-Met, vapor diffusion method, using 0.1 M HEPES (pH 7.5) and 1.0 M ammonium sulfate | Pseudomonas sp. |
crystal structure of PAOpt individually complexed with L-Phe and L-Met is constructed at constructed at 1.0-1.25 A resolution. The benzene ring of L-Phe is packed in six hydrophobic amino acid side chains versus the two hydrophobic side chains of L-amino acid oxidase. The distance between the substrate Calpha atom and water is shorter in the PAOpt-L-Met complex than in the PAOpt-L-Phe complex | Pseudomonas sp. |
Protein Variants | Comment | Organism |
---|---|---|
R143A | inactive | Pseudomonas sp. |
R143A | mutant enzyme shows no activity | Pseudomonas sp. |
R143K | mutant enzyme shows 400fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants | Pseudomonas sp. |
R143K | the mutant has about 400fold lower activity than the wild type enzyme | Pseudomonas sp. |
Y536A | inactive | Pseudomonas sp. |
Y536A | mutant enzyme shows no activity | Pseudomonas sp. |
Y536F | mutant enzyme shows 17fold lower activity compared to wild-type. Wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but PAM is not produced by the R143K and Y536F mutants | Pseudomonas sp. |
Y536F | the mutant has about 17fold lower activity than the wild type enzyme | Pseudomonas sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Phe + O2 | Pseudomonas sp. | highly specific for L-phenylalanine | 2-phenylacetamide + CO2 + H2O | - |
? | |
L-Phe + O2 | Pseudomonas sp. P-501 | highly specific for L-phenylalanine | 2-phenylacetamide + CO2 + H2O | - |
? | |
additional information | Pseudomonas sp. | the enzyme also catalyzes the oxidative deamination of L-methionine | ? | - |
? | |
additional information | Pseudomonas sp. P-501 | the enzyme also catalyzes the oxidative deamination of L-methionine | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas sp. | Q5W9R9 | - |
- |
Pseudomonas sp. P-501 | Q5W9R9 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pseudomonas sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Met + O2 | - |
Pseudomonas sp. | ? + CO2 + H2O | - |
? | |
L-Met + O2 | - |
Pseudomonas sp. P-501 | ? + CO2 + H2O | - |
? | |
L-Phe + O2 | highly specific for L-phenylalanine | Pseudomonas sp. | 2-phenylacetamide + CO2 + H2O | - |
? | |
L-Phe + O2 | wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but phenylacetamide is not produced by the R143K and Y536F mutants | Pseudomonas sp. | 2-phenylacetamide + CO2 + H2O | - |
? | |
L-Phe + O2 | highly specific for L-phenylalanine | Pseudomonas sp. P-501 | 2-phenylacetamide + CO2 + H2O | - |
? | |
L-Phe + O2 | wild-type PAOpt produces higher amounts of phenylacetamide (PAM) than phenylpyruvate (PPV) as expected, but phenylacetamide is not produced by the R143K and Y536F mutants | Pseudomonas sp. P-501 | 2-phenylacetamide + CO2 + H2O | - |
? | |
additional information | the enzyme also catalyzes the oxidative deamination of L-methionine | Pseudomonas sp. | ? | - |
? | |
additional information | the enzyme also catalyzes the oxidative deamination of L-methionine | Pseudomonas sp. P-501 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
L-Phe oxidase | - |
Pseudomonas sp. |
L-phenylalanine oxidase | - |
Pseudomonas sp. |
L-phenylalanine oxidase (deaminating and decarboxylating) | - |
Pseudomonas sp. |
PAOpt | - |
Pseudomonas sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pseudomonas sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Pseudomonas sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Pseudomonas sp. |