EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.13.12.9 | Pronase | - |
Pseudomonas sp. | |
1.13.12.9 | Trypsin | - |
Pseudomonas sp. |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.12.9 | expression of the proenzyme in Escherichia coli, site-directed mutation introduced on the wild-type proenzyme gene in the plasmid pPAO+15, expression of proenzyme mutants in Escherichia coli BL21(DE3) | Pseudomonas sp. |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.13.12.9 | crystals of noncatalytic proenzyme, activated enzyme, and enzyme o-amino benzoate complex, purified protein in 10 mM Tris-HCl (pH 8.0), concentrated, mixed with 0.1 M HEPES (pH 7.5) and 1.7 M ammonium sulfate (for the proenzyme) or 1.0 M ammonium sulfate (for the active enzyme), 30% glycerol in buffer as cryoprotectant, the enzyme amino benzoate complex is prepared by a soaking method with the cryoprotectant | Pseudomonas sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.12.9 | K478A | catalytic activity 1/200 of the wild-type enzyme | Pseudomonas sp. |
1.13.12.9 | M142A | kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased | Pseudomonas sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.13.12.9 | 2-amino benzoate | - |
Pseudomonas sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.12.9 | 0.0159 | - |
L-phenylalanine | active enzyme comparable to native enzyme, 20 mM Tris-HCl, pH 8.0, 25°C | Pseudomonas sp. | |
1.13.12.9 | 3.4 | - |
L-phenylalanine | M142A mutant (elevated compared to 1.8 mM for wild-type), 20 mM Tris-HCl, pH 8.0, 25°C | Pseudomonas sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.9 | L-phenylalanine + O2 | Pseudomonas sp. | oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine | 2-phenylacetamide + CO2 + H2O | - |
? | |
1.13.12.9 | L-phenylalanine + O2 | Pseudomonas sp. P-501 | oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine | 2-phenylacetamide + CO2 + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.12.9 | Pseudomonas sp. | - |
P-501 | - |
1.13.12.9 | Pseudomonas sp. P-501 | - |
P-501 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.12.9 | cell disruption by sonication, centrifugation, supernatant applied to HisTrap HP column equilibrated with 20 mM Tris-HCl (pH 8.0) containing 500 mM NaCl, elution with linear gradient of imidazole from 0-0.5 M, ammonium sulfate added to eluted fractions, centrifugation of precipitate, solution in 20 mM Tris-HCl (pH 8.0) containing 300 mM ammonium sulfate, several chromatographic steps using HiTrap Phenyl FF, Resource Q, and HiLoad 16/60 Superdex 200 prep grade, activated enzyme purified by HiTrap Q HP and gel filtration | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.9 | L-phenylalanine + O2 | oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine | Pseudomonas sp. | 2-phenylacetamide + CO2 + H2O | - |
? | |
1.13.12.9 | L-phenylalanine + O2 | oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine | Pseudomonas sp. P-501 | 2-phenylacetamide + CO2 + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.12.9 | homodimer | 2 * x, N-terminal 14 residue prosequence, alpha subunit, dipeptide, beta subunit | Pseudomonas sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.12.9 | L-phenylalanine oxidase | - |
Pseudomonas sp. |
1.13.12.9 | PAOpt | activated enzyme | Pseudomonas sp. |
1.13.12.9 | proPAO | noncatalytic proenzyme, activated by proteolytic cleavage | Pseudomonas sp. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.12.9 | 115 | - |
L-phenylalanine | active enzyme comparable to native enzyme, 20 mM Tris-HCl, pH 8.0, 25°C | Pseudomonas sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.13.12.9 | flavin adenine dinucleotide | FAD | Pseudomonas sp. |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.12.9 | 0.87 | - |
2-amino benzoate | 20 mM Tris-HCl, pH 8.0, 25°C | Pseudomonas sp. |