1.13.12.9: phenylalanine 2-monooxygenase
This is an abbreviated version!
For detailed information about phenylalanine 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.9
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1.13.12.9
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fad
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l-methionine
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proenzyme
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l-tyrosine
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purple
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ammonia
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flavin
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l-amino
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noncatalytic
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l-met
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prosequence
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charge-transfer
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analysis
- 1.13.12.9
- fad
- l-methionine
- proenzyme
- l-tyrosine
-
purple
- ammonia
- flavin
-
l-amino
-
noncatalytic
- l-met
-
prosequence
-
charge-transfer
- analysis
Reaction
Synonyms
L-Phe oxidase, L-phenylalanine oxidase, L-phenylalanine oxidase (deaminating and decarboxylating), oxidase, phenylalanine (deaminating, decarboxylating), PAOpt, proPAO
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1.13.12.9 phenylalanine 2-monooxygenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.13.12.9 - phenylalanine 2-monooxygenase
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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
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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
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
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-
?
L-Phe + O2
2-phenylacetamide + CO2 + H2O
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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
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
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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
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-
?
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
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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
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oxidative deamination and oxygenative decarboxylation of L-phenylalanine, L-tyrosine, L-tryptophan, and L-methionine
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-
?
additional information
?
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-
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
?
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the enzyme also catalyzes the oxidative deamination of L-methionine
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-
?
additional information
?
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the enzyme also catalyzes the oxidative deamination of L-methionine
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-
?
additional information
?
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-
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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-
?
