1.14.16.1: phenylalanine 4-monooxygenase
This is an abbreviated version!
For detailed information about phenylalanine 4-monooxygenase, go to the full flat file.
Word Map on EC 1.14.16.1
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1.14.16.1
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phenylketonuria
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hyperphenylalaninemia
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bh4
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error
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pterins
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inborn
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children
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hydroxylases
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neurotransmitter
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province
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tetrahydropterins
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counsel
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intellectual
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dopamine
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l-tyrosine
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genotype-phenotype
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prenatal
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serotonin
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dihydropteridine
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caucasian
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catecholamine
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hepatocytes
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sepiapterin
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genotype-based
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quinonoid
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non-heme
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chromobacterium
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neopterin
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ligation-dependent
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dihydrochloride
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neuropsychological
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lysolecithin
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lifelong
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phenylpyruvate
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dopa
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cyclohydrolase
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molecular biology
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rflps
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p-chlorophenylalanine
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dihydrobiopterin
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hypopigmentation
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s-oxidation
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pteridine
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violaceum
- 1.14.16.1
- phenylketonuria
- hyperphenylalaninemia
- bh4
- error
- pterins
-
inborn
- children
- hydroxylases
-
neurotransmitter
-
province
- tetrahydropterins
-
counsel
-
intellectual
- dopamine
- l-tyrosine
-
genotype-phenotype
-
prenatal
- serotonin
- dihydropteridine
-
caucasian
- catecholamine
- hepatocytes
- sepiapterin
-
genotype-based
-
quinonoid
-
non-heme
-
chromobacterium
- neopterin
-
ligation-dependent
- dihydrochloride
-
neuropsychological
- lysolecithin
-
lifelong
- phenylpyruvate
- dopa
-
cyclohydrolase
- molecular biology
-
rflps
- p-chlorophenylalanine
- dihydrobiopterin
-
hypopigmentation
-
s-oxidation
- pteridine
- violaceum
Reaction
Synonyms
cePAH, DicPAH, EC 1.14.3.1, EC 1.99.1.2, HPAH, L-phenylalanine 4-hydroxylase, oxygenase, phenylalanine 4-mono-, P4H, PAH, PheH, phenylalaninase, phenylalanine 4-hydroxylase, phenylalanine hydroxylase, phenylalanine monooxygenase, PheOH, phhA
ECTree
1.14.16.1 phenylalanine 4-monooxygenaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(7R)-5,6,7,8-tetrahydropterin
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0.001 mM, 50% inhibition at 0.5 mM phenylalanine, 0.004 mM, 50% inhibition at 0.1 mM phenylalanine, recombinant enzyme
(7R)-tetrahydrobiopterin
slight inhibition, synthetic pathway, overview, conformational structure by NMR
(7S)-tetrahydrobiopterin
strong, competitive inhibition, synthetic pathway, overview, conformational structure by NMR
2,2'-dipyridyl
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99.0% inhibition at 1.0 mM using L-phenylalanine as substrate, 99.0% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
2,3-dihydroxynaphthalene
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binds to Fe3+ on enzyme that is oxidized during catalysis
3,4-Dihydroxystyrene
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0.0005-0.005 mM, 50% inhibition, noncompetitive vs. 6,7-dimethyltetrahydropterin and L-phenylalanine
3-iodotyrosine
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3.0% inhibition at 1.0 mM using L-phenylalanine as substrate, 5.2% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
5,6-dimethyl-3-(4-methyl-2-pyridinyl)-2-thioxo-2,3-dihydrothieno[2,3-d]pyrimidin-4(1H)-one
weak competitive inhibitor
6-Fluorotryptophan
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2.5% inhibition at 1.0 mM using L-phenylalanine as substrate, 4.5% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
Acetohydroxamate
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competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron
bathophenanthroline
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competitive vs. 6-methyl-5,6,7,8-tetrahydropterin and tetrahydrobiopterin, most probably due to chelation of enzyme's iron
benzohydroxamate
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competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron
tetrahydrobiopterin
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excessive dosages of BH4 inhibit PAH under normal phenylalanine conditions in vivo and activate PAH under conditions of high phenylalanine, overview
(6R)-L-erythro-tetrahydrobiopterin
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inhibits phenylalanine and lysolecithin activation
4-Chlorophenylalanine
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specific PAH inhibitor, 97.2% inhibition at 1.0 mM using L-phenylalanine as substrate, 99.2% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
dithiothreitol
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2 mM, 94% inhibition, dithiothreitol induces the dissociation of iron from the enzyme, catalase and phenylalanine partially protect from inhibition
EDTA
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in the absence of added iron in the assay, the EDTA-treated PheH exhibits 3.5% of the L-phenylalanine hydroxylation activity of the metal-containing enzyme
L-phenylalanine
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competitive inhibition of the S-oxidation of S-carboxymethyl-L-cysteine, 92.8% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
S-carboxy-methyl-L-cysteine
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competitive inhibitor of the C-oxidation of L-phenylalanine
S-carboxy-methyl-L-cysteine
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competitive inhibitor of the C-oxidation of L-phenylalanine
S-carboxymethyl-L-cysteine
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competitive inhibitor of the aromatic C-oxidation of L-phenylalanine, 25.2% inhibition at 5.0 mM using L-phenylalanine as substrate
S-carboxymethyl-L-cysteine
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competitive to L-phenylalanine, 5 mM, 74% residual activity with substrate L-phenylalanine
S-methyl-ergothionine
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competitive inhibitor of the C-oxidation of L-phenylalanine
S-methyl-ergothionine
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competitive inhibitor of the C-oxidation of L-phenylalanine
S-methyl-L-cysteine
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competitive inhibitor of the C-oxidation of L-phenylalanine
S-methyl-L-cysteine
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competitive to L-phenylalanine, 5 mM, 89% residual activity with substrate L-phenylalanine
S-methyl-L-cysteine
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competitive inhibitor of the C-oxidation of L-phenylalanine
additional information
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the treatment with EDTA leads to the fully reversible release of iron from the active site without irreversibly inactivating the enzyme
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additional information
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not inhibited by the nitric oxide synthase inhibitors N(G)-monomethyl-D-arginine, 7-nitroindazole, L-thiocitrulline, N(G)-monomethyl-L-arginine, (S)-methy-L-thiocitrulline, and L-N5-(1-iminoethyl)ornithine; PH8, the large aromatic amino acid hydroxylase monoclonal antibody, inhibits the production of both L-tyrosine and S-carboxymethyl-L-cysteine S-oxide to 99.0% and 99.3% at 0.2 mg/ml concentration
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