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EC Tree
IUBMB Comments The reaction shown above is about 80% of the reaction catalysed; the remaining 20% is: L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid + ammonia + H2O2 a reaction similar to that of EC 1.4.3.2, L-amino-acid oxidase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
propao, paopt, l-phenylalanine oxidase (deaminating and decarboxylating), l-phe oxidase,
more
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L-phenylalanine oxidase (deaminating and decarboxylating)
oxidase, phenylalanine (deaminating, decarboxylating)
-
-
-
-
L-Phe oxidase
-
L-phenylalanine oxidase
-
-
L-phenylalanine oxidase
-
L-phenylalanine oxidase
-
-
L-phenylalanine oxidase (deaminating and decarboxylating)
-
-
-
-
L-phenylalanine oxidase (deaminating and decarboxylating)
-
L-phenylalanine oxidase (deaminating and decarboxylating)
-
-
PAOpt
-
activated enzyme
PAOpt
-
activated enzyme
-
proPAO
-
noncatalytic proenzyme, activated by proteolytic cleavage
proPAO
-
noncatalytic proenzyme, activated by proteolytic cleavage
-
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L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
mechanism
-
L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
mechanism
-
-
L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
-
-
-
-
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oxidative decarboxylation
-
-
-
-
decarboxylation
-
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L-phenylalanine:oxygen 2-oxidoreductase (decarboxylating)
The reaction shown above is about 80% of the reaction catalysed; the remaining 20% is: L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid + ammonia + H2O2 a reaction similar to that of EC 1.4.3.2, L-amino-acid oxidase.
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beta-2-thienyl-DL-Ala + O2
? + CO2 + H2O
-
-
-
-
?
beta-2-thienyl-DL-Ala + O2
? + NH3 + H2O2
DL-m-Tyr + O2
? + CO2 + H2O
-
-
-
-
?
DL-m-Tyr + O2
? + NH3 + H2O2
-
-
-
-
?
DL-o-Tyr + O2
? + CO2 + H2O
DL-o-Tyr + O2
? + NH3 + H2O2
-
-
-
-
?
L-Ala + O2
? + CO2 + H2O
-
9% of the activity with L-Phe
-
-
?
L-Ile + O2
? + CO2 + H2O
-
8% of the activity with L-Phe
-
-
?
L-Met + O2
2-oxo-methiolbutyrate + NH3 + H2O2
-
-
-
?
L-norleucine + O2
? + NH3 + H2O2
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
L-Phe + O2
beta-phenylpyruvate + NH3 + H2O2
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
L-Tyr + O2
? + NH3 + H2O2
p-fluoro-DL-Phe + O2
? + CO2 + H2O
-
-
-
-
?
p-fluoro-DL-Phe + O2
? + NH3 + H2O2
-
-
-
-
?
additional information
?
-
beta-2-thienyl-DL-Ala + O2
? + NH3 + H2O2
-
-
-
-
?
beta-2-thienyl-DL-Ala + O2
? + NH3 + H2O2
-
-
-
-
?
DL-o-Tyr + O2
? + CO2 + H2O
-
-
-
-
?
DL-o-Tyr + O2
? + CO2 + H2O
-
-
-
-
?
L-Met + O2
? + CO2 + H2O
-
-
-
-
?
L-Met + O2
? + CO2 + H2O
-
-
-
?
L-Met + O2
? + CO2 + H2O
-
19% of the activity with L-Phe
-
-
?
L-Met + O2
? + CO2 + H2O
-
19% of the activity with L-Phe
-
-
?
L-Met + O2
? + CO2 + H2O
-
-
-
-
?
L-Met + O2
? + CO2 + H2O
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
enzyme produces both beta-phenylpyruvate and alpha-phenylacetamide from L-Phe: 0.2 mol each of beta-phenylpyruvate, ammonia and H2O2 and 0.8 mol each of alpha-phenylacetamide and CO2 under aerobic conditions
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
highly specific for L-phenylalanine
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
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
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
enzyme produces both beta-phenylpyruvate and alpha-phenylacetamide from L-Phe: 0.2 mol each of beta-phenylpyruvate, ammonia and H2O2 and 0.8 mol each of alpha-phenylacetamide and CO2 under aerobic conditions
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
-
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
highly specific for L-phenylalanine
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-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
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
-
-
?
L-Phe + O2
beta-phenylpyruvate + NH3 + H2O2
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-
-
-
?
L-Phe + O2
beta-phenylpyruvate + NH3 + H2O2
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enzyme produces both beta-phenylpyruvate and alpha-phenylacetamide from L-Phe: 0.2 mol each of beta-phenylpyruvate, ammonia and H2O2 and 0.8 mol each of alpha-phenylacetamide and CO2 under aerobic conditions
-
-
?
L-Phe + O2
beta-phenylpyruvate + NH3 + H2O2
-
enzyme produces both beta-phenylpyruvate and alpha-phenylacetamide from L-Phe: 0.2 mol each of beta-phenylpyruvate, ammonia and H2O2 and 0.8 mol each of alpha-phenylacetamide and CO2 under aerobic conditions
-
-
?
L-Phe + O2
beta-phenylpyruvate + NH3 + H2O2
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-
-
-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
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-
-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
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oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine
-
-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
-
oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine
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-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
-
-
-
?
L-Trp + O2
? + CO2 + H2O
-
9% of the activity with L-Phe
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-
?
L-Trp + O2
? + CO2 + H2O
-
9% of the activity with L-Phe
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-
?
L-Tyr + O2
? + CO2 + H2O
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-
-
-
?
L-Tyr + O2
? + CO2 + H2O
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44% of the activity with L-Phe
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-
?
L-Tyr + O2
? + CO2 + H2O
-
44% of the activity with L-Phe
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-
?
L-Tyr + O2
? + CO2 + H2O
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-
-
-
?
L-Tyr + O2
? + NH3 + H2O2
-
-
-
-
?
L-Tyr + O2
? + NH3 + H2O2
-
-
-
-
?
additional information
?
-
-
purple intermediates consist of the reduced enzyme and an imino acid derived from a substrate, structure determination of the intermediates by resonance Raman spectroscopy
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-
?
additional information
?
-
the enzyme also catalyzes the oxidative deamination of L-methionine
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-
?
additional information
?
-
-
the enzyme also catalyzes the oxidative deamination of L-methionine
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-
?
additional information
?
-
-
purple intermediates consist of the reduced enzyme and an imino acid derived from a substrate, structure determination of the intermediates by resonance Raman spectroscopy
-
-
?
additional information
?
-
the enzyme also catalyzes the oxidative deamination of L-methionine
-
-
?
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L-Phe + O2
2-phenylacetamide + CO2 + H2O
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
additional information
?
-
L-Phe + O2
2-phenylacetamide + CO2 + H2O
highly specific for L-phenylalanine
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-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
highly specific for L-phenylalanine
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-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
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-
-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
-
oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine
-
-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
-
oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine
-
-
?
L-phenylalanine + O2
2-phenylacetamide + CO2 + H2O
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-
-
?
additional information
?
-
the enzyme also catalyzes the oxidative deamination of L-methionine
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-
?
additional information
?
-
-
the enzyme also catalyzes the oxidative deamination of L-methionine
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-
?
additional information
?
-
the enzyme also catalyzes the oxidative deamination of L-methionine
-
-
?
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flavin adenine dinucleotide
-
FAD
FAD
-
FAD
-
contains 2 mol of FAD per mol of enzyme
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1,10-phenanthroline
-
slight
3-Phenylpropionic acid
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competitive towards L-Phe
4-phenylbutyric acid
-
competitive towards L-Phe
8-hydroxyquinoline
-
slight
CuSO4
-
preferentially inhibits oxidase activity versus oxygenase activity
FeSO4
-
preferentially inhibits oxidase activity versus oxygenase activity
phenylacetic acid
-
inhibits both oxidation and oxygenation of L-Phe
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0.052
beta-2-thienyl-DL-Ala
-
calculation from oxygen consumption due to oxidation and/or oxygenation
0.071
beta-2-Thienylalanine
-
-
0.189
DL-o-Tyr
-
calculation from oxygen consumption due to oxidation and/or oxygenation
0.83
L-norleucine
-
calculation from oxygen consumption due to oxidation and/or oxygenation
0.0159 - 3.4
L-phenylalanine
0.012
p-fluoro-DL-Phe
-
calculation from oxygen consumption due to oxidation and/or oxygenation
0.502
L-Met
-
calculation from oxygen consumption due to oxidation and/or oxygenation
0.0107
L-Phe
-
-
0.011
L-Phe
-
oxygenation
0.0159
L-phenylalanine
-
active enzyme comparable to native enzyme, 20 mM Tris-HCl, pH 8.0, 25°C
0.017
L-phenylalanine
pH 8.0, 25°C
3.4
L-phenylalanine
-
M142A mutant (elevated compared to 1.8 mM for wild-type), 20 mM Tris-HCl, pH 8.0, 25°C
0.275
L-Tyr
-
calculation from oxygen consumption due to oxidation and/or oxygenation
1.82
O2
-
-
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103 - 115
L-phenylalanine
103
L-phenylalanine
pH 8.0, 25°C
115
L-phenylalanine
-
active enzyme comparable to native enzyme, 20 mM Tris-HCl, pH 8.0, 25°C
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0.87
2-amino benzoate
-
20 mM Tris-HCl, pH 8.0, 25°C
0.017
3-phenylpropanoate
-
-
0.056
4-phenyl-n-butyrate
-
-
0.93
5-phenylpentanoate
-
-
0.098
phenylacetic acid
-
-
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11
-
formation of beta-phenylpyruvate
6 - 9.5
-
formation of alpha-phenylacetamide
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9.8 - 11.8
-
50% of maximal activity at pH 9.8 and 11.8, formation of beta-phenylpyruvate
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45
-
formation of alpha-phenylacetamide
65
-
formation of beta-phenylpyruvate
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20 - 70
-
20°C: about 65% of maximal activity, 70°C: about 50% of maximal activity, formation of alpha-phenylacetamide
40 - 85
-
40°C: about 50% of maximal activity 40°C and 85°C, formation of beta-phenylpyruvate
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Uniprot
brenda
-
-
-
brenda
-
Uniprot
brenda
P-501
-
-
brenda
-
Uniprot
brenda
-
-
-
brenda
-
Uniprot
brenda
P-501
-
-
brenda
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PAO_PSESP
714
0
76883
Swiss-Prot
-
A0A0S4V151_RALSL
707
0
76060
TrEMBL
-
A0A0S4U9S9_RALSL
707
0
76007
TrEMBL
-
A0A0S4TZR4_RALSL
707
0
76356
TrEMBL
-
A3RQV8_RALSU
Ralstonia solanacearum (strain UW551)
713
0
77572
TrEMBL
-
A0A0S4W8G9_RALSL
707
0
76081
TrEMBL
-
A0A0S4WXD9_RALSL
707
0
76067
TrEMBL
-
A0A3B0J8T7_9GAMM
165
0
18403
TrEMBL
-
A0A3B0JAD1_9GAMM
445
0
50355
TrEMBL
-
A0A0U2JT37_MONRU
436
0
48307
TrEMBL
other Location (Reliability: 2 )
A0A3B0J4H6_9GAMM
121
0
13399
TrEMBL
-
A0A0S4X7Q0_RALSL
707
0
76033
TrEMBL
-
A0A5E6P0M9_PSEFL
721
0
79152
TrEMBL
-
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68000
-
2 * 68000, SDS-PAGE
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dimer
-
2 * 68000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
-
homodimer
-
2 * x, N-terminal 14 residue prosequence, alpha subunit, dipeptide, beta subunit
homodimer
-
2 * x, N-terminal 14 residue prosequence, alpha subunit, dipeptide, beta subunit
-
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complexed with L-Phe and L-Met, vapor diffusion method, using 0.1 M HEPES (pH 7.5) and 1.0 M ammonium sulfate
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
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
-
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K478A
-
catalytic activity 1/200 of the wild-type enzyme
M142A
-
kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased
K478A
-
catalytic activity 1/200 of the wild-type enzyme
-
M142A
-
kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased
-
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
-
R143A
inactive
R143A
mutant enzyme shows no activity
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
R143K
the mutant has about 400fold lower activity than the wild type enzyme
Y536A
inactive
Y536A
mutant enzyme shows no activity
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
Y536F
the mutant has about 17fold lower activity than the wild type enzyme
R143A
-
inactive
-
R143A
-
mutant enzyme shows no activity
-
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
-
R143K
-
the mutant has about 400fold lower activity than the wild type enzyme
-
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60
-
10 min, no loss of activity
80
-
10 min, 46% loss of activity
85
-
10 min, 90% loss of activity
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-20°C, 1 mM or 10 mM potassium phosphate buffer, pH 7.0, stable for at least 6 months
-
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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
-
recombinant enzyme using His-tag
-
-
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) as His-tag fusion protein
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)
-
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analysis
-
a simple and rapid enzymic determination of L-Phe with L-phenylalanine oxidase (deaminating and decarboxylating)
analysis
-
a simple and rapid enzymic determination of L-Phe with L-phenylalanine oxidase (deaminating and decarboxylating)
-
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Koyama, H.
A simple and rapid enzymatic determination of L-phenylalanine with a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
Clin. Chim. Acta
136
131-136
1984
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Koyama, H.
Purification and characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
J. Biochem.
92
1235-1240
1982
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Koyama, H.
Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
J. Biochem.
93
1313-1319
1983
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Koyama, H.
Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
J. Biochem.
96
421-427
1984
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Koyama, H.; Suzuki, H.
Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating)
J. Biochem.
100
859-866
1986
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Suzuki, H.; Koyama, H.; Nishina, Y.; Sato, K.; Shiga, K.
A resonance Raman study on a reaction intermediate of Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating)
J. Biochem.
110
169-172
1991
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Suzuki, H.; Higashi, Y.; Asano, M.; Suguro, M.; Kigawa, M.; Maeda, M.; Katayama, S.; Mukouyama, E.B.; Uchiyama, K.
Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme
J. Biochem.
136
617-627
2004
Pseudomonas sp. (Q5W9R9), Pseudomonas sp., Pseudomonas sp. P-501 (Q5W9R9)
brenda
Ohta, Y.; Mukouyama, E.B.; Suzuki, H.
Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501
J. Biochem.
139
551-555
2006
Pseudomonas sp., Pseudomonas sp. P-501
brenda
Ida, K.; Kurabayashi, M.; Suguro, M.; Hiruma, Y.; Hikima, T.; Yamomoto, M.; Suzuki, H.
Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501
J. Biol. Chem.
283
16584-16590
2008
Pseudomonas sp., Pseudomonas sp. P-501
brenda
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
J. Biochem.
150
659-669
2011
Pseudomonas sp. (Q5W9R9), Pseudomonas sp., Pseudomonas sp. P-501 (Q5W9R9)
brenda
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