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
-
province
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tetrahydropterins
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counsel
-
intellectual
-
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
-
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 (Posttranslational Modification
Posttranslational Modification on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
side-chain modification
additional information
side-chain modification
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recombinant enzyme incorporates 1 mol phosphate per mol of enzyme subunit when phosphorylated in vitro by cyclic AMP-dependent protein kinase, Ser-16 seems to be the phosphorylation site
side-chain modification
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incorporation of 0.6 mol phosphate per enzyme subunit, recombinant enzyme
side-chain modification
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activity of liver enzyme might be regulated by phosphorylation-dephosphorylation
side-chain modification
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liver enzyme in untreated animals is a mixture of phosphorylated and nonphosphorylated forms, enzyme may be phosphorylated in vivo by cAMP-dependent protein kinase
side-chain modification
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recombinant enzyme incorporates 0.97 phosphate per subunit
side-chain modification
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enzyme contains 0.3 mol of phosphate per mol of enzyme subunit
side-chain modification
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enzyme form I contains 0.3 mol phosphate per mol subunit, enzyme form II contains 0.4 mol
side-chain modification
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phosphorylated enzyme shows a 3.3fold increase in Vmax
additional information
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enzyme is phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase
additional information
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self-hydroxylation mechanism at Phe325, dependent on iron at the active site
additional information
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hepatic enzyme consists of a mixture of phosphorylated and nonphosphorylated forms
