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Literature summary extracted from
- High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism (2011), J. Biochem., 150, 659-669.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.12.9 | expressed in Escherichia coli | Pseudomonas sp. |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.13.12.9 | 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. |
| 1.13.12.9 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.12.9 | R143A | inactive | Pseudomonas sp. |
| 1.13.12.9 | R143A | mutant enzyme shows no activity | Pseudomonas sp. |
| 1.13.12.9 | 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. |
| 1.13.12.9 | R143K | the mutant has about 400fold lower activity than the wild type enzyme | Pseudomonas sp. |
| 1.13.12.9 | Y536A | inactive | Pseudomonas sp. |
| 1.13.12.9 | Y536A | mutant enzyme shows no activity | Pseudomonas sp. |
| 1.13.12.9 | 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. |
| 1.13.12.9 | Y536F | the mutant has about 17fold lower activity than the wild type enzyme | Pseudomonas sp. |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.12.9 | L-Phe + O2 | Pseudomonas sp. | highly specific for L-phenylalanine | 2-phenylacetamide + CO2 + H2O | - |
? |  |
| 1.13.12.9 | L-Phe + O2 | Pseudomonas sp. P-501 | highly specific for L-phenylalanine | 2-phenylacetamide + CO2 + H2O | - |
? | |
| 1.13.12.9 | additional information | Pseudomonas sp. | the enzyme also catalyzes the oxidative deamination of L-methionine | ? | - |
? | |
| 1.13.12.9 | additional information | Pseudomonas sp. P-501 | the enzyme also catalyzes the oxidative deamination of L-methionine | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.12.9 | Pseudomonas sp. | Q5W9R9 | - |
- |
| 1.13.12.9 | Pseudomonas sp. P-501 | Q5W9R9 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.12.9 | - |
Pseudomonas sp. |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.12.9 | L-Met + O2 | - |
Pseudomonas sp. | ? + CO2 + H2O | - |
? | |
| 1.13.12.9 | L-Met + O2 | - |
Pseudomonas sp. P-501 | ? + CO2 + H2O | - |
? | |
| 1.13.12.9 | L-Phe + O2 | highly specific for L-phenylalanine | Pseudomonas sp. | 2-phenylacetamide + CO2 + H2O | - |
? | |
| 1.13.12.9 | 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 | - |
? | |
| 1.13.12.9 | L-Phe + O2 | highly specific for L-phenylalanine | Pseudomonas sp. P-501 | 2-phenylacetamide + CO2 + H2O | - |
? | |
| 1.13.12.9 | 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 | - |
? | |
| 1.13.12.9 | additional information | the enzyme also catalyzes the oxidative deamination of L-methionine | Pseudomonas sp. | ? | - |
? | |
| 1.13.12.9 | additional information | the enzyme also catalyzes the oxidative deamination of L-methionine | Pseudomonas sp. P-501 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.12.9 | L-Phe oxidase | - |
Pseudomonas sp. |
| 1.13.12.9 | L-phenylalanine oxidase | - |
Pseudomonas sp. |
| 1.13.12.9 | L-phenylalanine oxidase (deaminating and decarboxylating) | - |
Pseudomonas sp. |
| 1.13.12.9 | PAOpt | - |
Pseudomonas sp. |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.9 | 25 | - |
assay at | Pseudomonas sp. |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.9 | 7 | - |
assay at | Pseudomonas sp. |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.12.9 | FAD | - |
Pseudomonas sp. | |
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