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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Activating Compound
Activating Compound on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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alpha-chymotrypsin
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limited proteolysis of purified liver enzyme, 20-30fold increase in activity, cofactor tetrahydrobiopterin
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glycerol
does no affect the wild-type enzyme activity at 1-5%, but increases the activity of the mutant enzymes about 1-3fold, overview
H2O2
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2 mM, up to 4fold increase in activity, mixed activation mechanism, oxidation of Trp120 to 5-hydroxy-Trp120
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
cAMP-dependent protein kinase
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1.6fold increase in activity, cofactor tetrahydrobiopterin
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cAMP-dependent protein kinase
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2-4fold increase in activity in the presence of tetrahydrobiopterin
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dithiothreitol
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in the absence of dithiothreitol the activity of recently purified PheH is 50% of that achieved when dithiothreitol is present
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preincubation with L-phenylalanine exhibits 1.3fold stimulatory effect on kcat
L-phenylalanine
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hepatic phenylalanine hydroxylase variably increases with in response to L-phenylalanine or a 10% dietary supplement of indispensable amino acids including L-phenylalanine but does not increase in response to indispensable amino acids lacking L-phenylalanine when the amino acids are added to a diet that is marginally adequate in L-phenylalanine
lysolecithin
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2fold activation of recombinant enzyme, cofactor tetrahydrobiopterin
lysolecithin
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1 mM, approx. 7.5fold stimulation of phosphorylated recombinant wild-type enzyme, S16E and S16D mutant enzymes, approx. 24fold stimulation of non-phosphorylated recombinant wild-type enzyme, S16A, S16Q, S16N and S16K mutant enzymes
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recombinant enzyme, 2fold increase in activity, cofactor tetrahydrobiopterin
phenylalanine
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approx. 4.5fold increase in activity of non-phosphorylated and phosphorylated enzyme, cofactor tetrahydrobiopterin
phenylalanine
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after activation with phenylalanine the dimer/tetramer equilibrium is shifted towards the tetrameric form
phenylalanine
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wild-type tetramer reveals a kinetic positive coorperativity of L-phenylalanine binding leading to a 5-6fold activation of wild-type tetramer, dimeric form shows a hyperbolic rate vs. substrate concentration, 1.6fold activation by phenylalanine, tetrameric T427P mutant enzyme shows no cooperativity, dimeric forms of wild-type and T427P mutant have similar kinetic properties
phenylalanine
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major regulator of liver enzyme, binds at an effector site converting the inactive to an active enzyme
phenylalanine
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homotropic allosteric activator of both hepatic and recombinant enzymes
phenylalanine
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binds to activation site distinct from catalytic site with a stoichiometry of 1/enzyme subunit, binding induces a conformation change converting the enzyme tetramer from an inactive to an active form, activation site binds phenylalanine in a cooperative manner, regulation of activation
Phospholipids
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increase in activity in the presence of tetrahydrobiopterin but not in the presence of synthetic pterin cofactors
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relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
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additional information
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relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
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additional information
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activity of recombinant enzyme is activated 1.5fold by exposure to pH 8.5-9.0
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additional information
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the enzyme is not affected in any direction by preincubation with the substrate L-phenylalanine
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additional information
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relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
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additional information
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relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
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additional information
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relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
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additional information
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relatively low activity with tetrahydrobiopterin can be selectively increased by phosphorylation
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additional information
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non activated enzyme has much greater activity with 6-methyltetrahydropterin and dimethyltetrahydropterin than with tetrahydrobiopterin
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additional information
not significantly activated by L-valine, L-alanine, and L-serine
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