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
-
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
- 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 (Activating Compound
Activating Compound on EC 1.14.16.1 - phenylalanine 4-monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
alpha-chymotrypsin
-
limited proteolysis of purified liver enzyme, 20-30fold increase in activity, cofactor tetrahydrobiopterin
-
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
-
2 mM, up to 4fold increase in activity, mixed activation mechanism, oxidation of Trp120 to 5-hydroxy-Trp120
tetrahydrobiopterin
-
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
-
1.6fold increase in activity, cofactor tetrahydrobiopterin
-
cAMP-dependent protein kinase
-
2-4fold increase in activity in the presence of tetrahydrobiopterin
-
dithiothreitol
-
in the absence of dithiothreitol the activity of recently purified PheH is 50% of that achieved when dithiothreitol is present
L-phenylalanine
-
preincubation with L-phenylalanine exhibits 1.3fold stimulatory effect on kcat
L-phenylalanine
-
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
-
2fold activation of recombinant enzyme, cofactor tetrahydrobiopterin
lysolecithin
-
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
phenylalanine
-
recombinant enzyme, 2fold increase in activity, cofactor tetrahydrobiopterin
phenylalanine
-
approx. 4.5fold increase in activity of non-phosphorylated and phosphorylated enzyme, cofactor tetrahydrobiopterin
phenylalanine
-
after activation with phenylalanine the dimer/tetramer equilibrium is shifted towards the tetrameric form
phenylalanine
-
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
-
major regulator of liver enzyme, binds at an effector site converting the inactive to an active enzyme
phenylalanine
-
homotropic allosteric activator of both hepatic and recombinant enzymes
phenylalanine
-
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
-
increase in activity in the presence of tetrahydrobiopterin but not in the presence of synthetic pterin cofactors
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
additional information
-
activity of recombinant enzyme is activated 1.5fold by exposure to pH 8.5-9.0
-
additional information
-
the enzyme is not affected in any direction by preincubation with the substrate L-phenylalanine
-
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by phosphorylation
-
additional information
-
non activated enzyme has much greater activity with 6-methyltetrahydropterin and dimethyltetrahydropterin than with tetrahydrobiopterin
-
additional information
not significantly activated by L-valine, L-alanine, and L-serine
-
