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
-
error
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pterins
-
inborn
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children
-
hydroxylases
-
neurotransmitter
-
province
-
tetrahydropterins
-
counsel
-
intellectual
-
dopamine
-
l-tyrosine
-
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
-
pteridine
-
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
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results (Metals Ions
Metals Ions on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
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substoichiometric amounts after removal of copper with dithiothreitol
Co2+
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
copper
Fe2+
Iron
Zn2+
copper
-
electron paramagnetic resonance spectroscopy indicates a type II copper-containing enzyme
copper
-
copper does not support enzyme activity and can be removed by dithiothreitol
Fe2+
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incubation of apo-PAH with 0.5 mM Fe2+ and removal of free Fe2+ provides a holoenzyme which retains almost stoichiometric amounts of Fe2+ bound (0.88 mol Fe2+/mol monomer)
Fe2+
native metal cofactor, determination of binding affinity, binding structure, overview
Fe2+
-
0.1 mM added as ferrous ammonium sulfate, 40-70% activation depending on assay conditions
Fe2+
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nonheme iron is bound on one face by residues His285, His290, and Glu330 forming a a 2-His-1-carboxylate facial triad, the three ligands differ in their sensitivity to mutagenesis, structure, overview
Iron
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copper depleted enzyme can be reconstituted with approx. 1 molecule of iron per enzyme molecule, iron reconstituted enzyme hydroxylates phenylalanine
Iron
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non-heme iron, required, effects of cofactor and substrate on the iron environment, the abilities of nitric oxide to behave as an oxygen mimic and a spectroscopic probe of ferrous iron are used to investigate the geometric and electronic effects of cofactor and substrate binding to cPAH by electron paramagnetic resonance (EPR) and UV-Vis spectroscopies, overview
Iron
conformation and distances to the catalytic iron of both L-phenylalanine and the cofactor analog L-erythro-7,8-dihydrobiopterin simultaneously bound to the recombinant enzyme estimated by 1H-NMR
Iron
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1 iron atom per subunit, fully active enzyme has non-heme high-spin ferric iron coordinated at the active site
Iron
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iron can be removed by treatment with o-phenanthroline, reconstitution of apoenzyme with iron restores 90% of the initial activity
Iron
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kinetic data suggest, that enzyme's iron is solvent-accessible and resides in a hydrophobic pocket of the enzyme
Zn2+
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substoichiometric amounts after removal of copper with dithiothreitol
Zn2+
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
