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Literature summary for 1.13.12.9 extracted from

  • Ida, K.; Suguro, M.; Suzuki, H.
    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.
    View publication on PubMed
Search for more literature for 1.13.12.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Pseudomonas sp.

Crystallization (Commentary)

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Pseudomonas sp. Q5W9R9
-
-
Pseudomonas sp. P-501 Q5W9R9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp.

Substrates and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Pseudomonas sp.