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
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Subunits
Subunits on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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dimer
homodimer
homotetramer
monomer
oligomer
wild-type and mutant enzymes show different oligomeric states, from dimer to hexamer, overview
tetramer
additional information
dimer
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2 * 13000 (regulatory domain 1-118), gel filtration. In the presence of phenylalanine, the protein elutes earlier from the column, consistent with a conformational change in the presence of the amino acid
homodimer
2 * 13500, catalytic domain, calculated from amino acid sequence
homodimer
2 * 65000, catalytic domain fused to maltose-binding protein, SDS-PAGE
monomer
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1 * 30300, deduced from gene sequence and crystallization data
additional information
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rat liver enzyme and recombinant human enzyme are in a tetramer/dimer equilibrium
additional information
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the N-terminal regulatory domain is an ACT domain, a small molecule-binding domain characterized by high sequence divergence and evolutionary mobility. The ACT domain displays a ferredoxin-like fold, structure comparison with ACT and ACT-like proteins and analysis, a GAL-IESRP motif is located at the interface between the interacting regulatory and catalytic domains, overview
additional information
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some authors report that the enzyme exists as a mixture of dimers and tetramers, others report that it exists solely as tetramer or as dimer, percentage of dimers increases on frozen storage, preincubation of the enzyme with phenylalanine leads to even higher than 200000 Da molecular weight forms
additional information
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rat liver enzyme and recombinant human enzyme are in a tetramer/dimer equilibrium