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Information on EC 1.13.12.9 - phenylalanine 2-monooxygenase
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1.13.12.9 phenylalanine 2-monooxygenaseIUBMB 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.
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Word Map
- 1.13.12.9
- fad
- l-methionine
- proenzyme
- l-tyrosine
-
purple
- ammonia
- flavin
-
l-amino
-
noncatalytic
- l-met
-
prosequence
-
charge-transfer
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
propao, paopt, l-phenylalanine oxidase (deaminating and decarboxylating), l-phe oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-Phe oxidase
L-phenylalanine oxidase
L-phenylalanine oxidase (deaminating and decarboxylating)
oxidase, phenylalanine (deaminating, decarboxylating)
-
-
-
-
PAOpt
proPAO
L-phenylalanine oxidase (deaminating and decarboxylating)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
decarboxylation
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
190396-37-3
-
69403-11-8
-
84012-76-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
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
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
-
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-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
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme also catalyzes the oxidative deamination of L-methionine
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Phe + O2
2-phenylacetamide + CO2 + H2O
highly specific for L-phenylalanine
-
-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
highly specific for L-phenylalanine
-
-
?
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
-
-
?
additional information
?
-
the enzyme also catalyzes the oxidative deamination of L-methionine
-
-
?
additional information
?
-
-
the enzyme also catalyzes the oxidative deamination of L-methionine
-
-
?
additional information
?
-
the enzyme also catalyzes the oxidative deamination of L-methionine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.052
beta-2-thienyl-DL-Ala
-
calculation from oxygen consumption due to oxidation and/or oxygenation
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
0.012
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
0.0159
L-phenylalanine
-
active enzyme comparable to native enzyme, 20 mM Tris-HCl, 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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
115
L-phenylalanine
-
active enzyme comparable to native enzyme, 20 mM Tris-HCl, pH 8.0, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.8 - 11.8
-
50% of maximal activity at pH 9.8 and 11.8, formation of beta-phenylpyruvate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 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
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M142A
-
kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased
R143A
R143K
Y536A
Y536F
M142A
-
kcat is 1/10 of the wild-type enzyme, Km is elevated, affinity for oxygen seems decreased
-
R143A
R143K
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
-
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
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
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mM or 10 mM potassium phosphate buffer, pH 7.0, stable for at least 6 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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