Information on EC 1.14.16.1 - phenylalanine 4-monooxygenase

New: Word Map on EC 1.14.16.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.16.1
-
RECOMMENDED NAME
GeneOntology No.
phenylalanine 4-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
oxygenation
-
S-oxygenation
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine degradation I (aerobic)
-
-
L-phenylalanine degradation V
-
-
L-tyrosine biosynthesis IV
-
-
Metabolic pathways
-
-
phenylalanine metabolism
-
-
Phenylalanine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, 6,7-dihydropteridine reductase, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-73-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
field mouse
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Schreber, bank vole
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain NBRC 12614T
SwissProt
Manually annotated by BRENDA team
a psychrophilic bacterium
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-butyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
low activity
-
-
?
(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
(S)-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
-
low activity
-
-
?
(S)-ethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
(S)-ethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
-
-
-
-
?
(S)-ethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
low activity
-
-
?
(S)-methyl-ergothionine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
low activity
-
-
?
(S)-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
(S)-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
-
low activity
-
-
?
(S)-propyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
low activity
-
-
?
2-fluorophenylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
3-(2-thienyl)-L-alanine + 6-methyltetrahydropterin + O2
? + 6-methyldihydropterin + H2O
show the reaction diagram
-
-
-
-
?
3-(2-thienyl)-L-alanine + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
show the reaction diagram
-
-
-
-
?
3-fluorophenylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
3-phenylserine + tetrahydrobiopterin + O2
?
show the reaction diagram
4-chlorophenylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
4-fluorophenylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
4-methyl-L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
show the reaction diagram
beta-2-thienylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
show the reaction diagram
L-methionine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
L-methionine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
lysolecithin activated enzyme
-
-
?
L-norleucine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
lysolecithin activated enzyme
-
-
?
L-norleucine + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
show the reaction diagram
-
5% of the activity with 3-(2-thienyl)-L-alanine
-
-
?
L-Phe + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
show the reaction diagram
-
-
-
-
?
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
show the reaction diagram
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + (6R)-tetrahydrobiopterin + O2
L-tyrosine + (6R)-dihydrobiopterin + H2O
show the reaction diagram
-
in mammals rate-limiting step in complete catabolism of phenylalanine to CO2 and water
-
?
L-phenylalanine + 5,6,7,8-tetrahydro-L-biopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 7,8-dimethyl-6,7-dihydrobiopterin + H2O
show the reaction diagram
-
-
-
-
-
L-phenylalanine + 6,7-dimethyl-tetrahydrobiopterin + O2
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6,7-dimethyltetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyl-tetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyl-tetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
2-amino-4a-hydroxy-7-methyl-5,6,7,8-tetrahydropteridin-4(4aH)-one + H2O + ?
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
?
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-phenylalanine + 6-methyldihydropterin + H2O2
show the reaction diagram
-
copper-depleted enzyme, in the absence of Fe2+, 6-methyltetrahydropterin oxidation can be uncoupled from substrate hydroxylation by the exclusion of iron
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
show the reaction diagram
-
low activity with 6-methyltetrahydropterin
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 6-methyldihydropterin + H2O
show the reaction diagram
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
show the reaction diagram
L-thienylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
L-tryptophan + tetrahydrobiopterin + O2
?
show the reaction diagram
m-tyrosine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
N-acetyl-(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
N-acetyl-(S)-carboxymethyl-L-cysteine S-oxide + ?
show the reaction diagram
-
-
-
-
?
N-acetyl-(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
N-acetyl-(S)-methyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
N-acetyl-(S)-methyl-L-cysteine S-oxide + ?
show the reaction diagram
-
-
-
-
?
N-acetyl-(S)-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
N-acetyl-S-carboxymethyl-L-cysteine + O2
?
show the reaction diagram
N-acetyl-S-methyl-L-cysteine + O2
?
show the reaction diagram
p-methylphenylalanine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
phenylalanine + tetrahydrobiopterin + O2
tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
PAH is a key enzyme in the metabolic pathway of phenylalanine. Deficiency in PAH leads to high and persistent levels of this amino acid in theplasma of phenylketonuria patients, causing permanent neurological damage
-
-
ir
S-carboxy-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
S-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
-
-
-
-
?
S-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
-
-
-
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
conversion to the (S)-sulfoxide
-
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
S-methyl-ergothionine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
S-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
S-methyl-L-cysteine + O2
?
show the reaction diagram
S-methyl-L-cysteine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
lysolecithin activated enzyme
-
-
?
S-methyl-L-cysteine + tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + (6R)-tetrahydrobiopterin + O2
L-tyrosine + (6R)-dihydrobiopterin + H2O
show the reaction diagram
-
in mammals rate-limiting step in complete catabolism of phenylalanine to CO2 and water
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
phenylalanine + tetrahydrobiopterin + O2
tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
PAH is a key enzyme in the metabolic pathway of phenylalanine. Deficiency in PAH leads to high and persistent levels of this amino acid in theplasma of phenylketonuria patients, causing permanent neurological damage
-
-
ir
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(6R)-5,6,7,8-tetrahydro-L-monapterin
-
7% of the activity with tetrahydrobiopterin
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
(7R)-tetrahydrobiopterin
-
8fold lower affinity and activity compared with 6(R)BH4
(7S)-tetrahydrobiopterin
-
8fold lower affinity and activity compared with 6(R)BH4
5,6,7,8-tetrahydro-L-biopterin
5,6,7,8-tetrahydrobiopterin
-
-
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
-
6,7-dimethyltetrahydropterin
-
17% of the activity with tetrahydrobiopterin
6-methyl-tetrahydrobiopterin
6-methyltetrahydrobiopterin
-
-
dihydrobiopterin
-
-
L-threo-neopterin
-
-
tetrahydrobiopterin
tetrahydrofolate
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
substoichiometric amounts after removal of copper with dithiothreitol
Cl-
-
bound by residue S391
Co2+
-
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
copper
additional information
-
enzyme does not contain iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(6R)-L-erythro-tetrahydrobiopterin
(7R)-5,6,7,8-tetrahydrobiopterin
-
-
(7R)-5,6,7,8-tetrahydropterin
-
0.001 mM, 50% inhibition at 0.5 mM phenylalanine, 0.004 mM, 50% inhibition at 0.1 mM phenylalanine, recombinant enzyme
-
(7R)-tetrahydrobiopterin
-
slight inhibition, synthetic pathway, overview, conformational structure by NMR
(7S)-tetrahydrobiopterin
-
strong, competitive inhibition, synthetic pathway, overview, conformational structure by NMR
2,2'-dipyridine
-
-
2,2'-dipyridyl
-
99.0% inhibition at 1.0 mM using L-phenylalanine as substrate, 99.0% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
2,3-dihydroxynaphthalene
-
binds to Fe3+ on enzyme that is oxidized during catalysis
2-mercaptoethanol
-
2 mM, 80% inhibition
3,4-dihydroxyphenylpropane
-
0.0016 mM, 50% inhibition
3,4-Dihydroxyphenylpropionic acid
-
0.24 mM, 50% inhibition
3,4-Dihydroxystyrene
-
0.0005-0.005 mM, 50% inhibition, noncompetitive vs. 6,7-dimethyltetrahydropterin and L-phenylalanine
3-iodotyrosine
-
3.0% inhibition at 1.0 mM using L-phenylalanine as substrate, 5.2% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
4-chloromercuribenzoate
-
1 mM, complete inhibition after 10 min
4-Chlorophenylalanine
4-Fluorophenylalanine
-
above 1 mM
4-hydroxyphenylpyruvic acid
-
above 0.4 mM iron, activation below
6-Fluorotryptophan
-
2.5% inhibition at 1.0 mM using L-phenylalanine as substrate, 4.5% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
7(S)-tetrahydrobiopterin
-
-
8-hydroxyquinoline
-
-
Acetohydroxamate
-
competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron
ascorbate
-
2 mM, 78% inhibition
Bathocuproine
-
-
bathophenanthroline
-
competitive vs. 6-methyl-5,6,7,8-tetrahydropterin and tetrahydrobiopterin, most probably due to chelation of enzyme's iron
bathophenanthroline disulfonate
-
0.025 mM, 50% inhibition
benzohydroxamate
-
competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron
catechol
Co2+
-
replaced Fe2+ at the active site
Copper-chelating agents
-
-
-
D,L-DOPA
-
0.1 mM, approx. 60% inhibition
D,L-m-tyrosine
-
0.4 mM, approx. 80% inhibition
deaza-6-methyltetrahydropterin
-
competitive vs. 6-methyltetrahydropterin
deferoxamine
-
5 mM, 1% residual activity
diethyldithiocarbamate
dithiothreitol
DL-alpha-tocopherol
-
strong inhibition
dopamine
epinephrine
-
-
glycerol
-
-
H2O2
-
inactivates the reduced form of the enzyme
halogenated phenylalanine
-
moderate
-
Iron-chelating agents
-
-
-
L-3,4-dihydroxyphenylalanine
-
-
L-cysteine
-
2 mM, 42% inhibition
L-Dopa
-
0.3 mM, approx. 40% inhibition
L-methionine
L-phenylalanine
L-tryptophan
-
-
norepinephrine
-
-
o-phenanthroline
phenylalanine
-
-
S-carboxy-methyl-L-cysteine
S-carboxymethyl-L-cysteine
S-methyl-ergothionine
S-methyl-L-cysteine
tetrahydrobiopterin
-
excessive dosages of BH4 inhibit PAH under normal phenylalanine conditions in vivo and activate PAH under conditions of high phenylalanine, overview
Thiol-binding reagents
-
-
-
tryptophan
-
recombinant enzyme, 3 mM, approx. 75% inhibition
Tween 80
-
-
tyrosine
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyphenylacetic acid
-
0.4 mM, approx. 30% activation
alpha-chymotrypsin
-
limited proteolysis of purified liver enzyme, 20-30fold increase in activity, cofactor tetrahydrobiopterin
-
cAMP-dependent protein kinase
dithiothreitol
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
L-phenylalanine
liver lysosomal proteases
-
limited proteolysis of liver enzyme
-
lysolecithin
N-ethylmaleimide
-
activation by alkylation of sulfhydryl groups
phenylalanine
Phospholipids
tetrahydrobiopterin
-
excessive dosages of BH4 inhibit PAH under normal phenylalanine conditions in vivo and activate PAH under conditions of high phenylalanine, overview
Trypsin
-
limited proteolysis of purified liver enzyme
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.025
(6R)-5,6,7,8-tetrahydrobiopterin
0.008 - 0.094
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
0.2
(7R)-5,6,7,8-tetrahydrobiopterin
-
recombinant enzyme
8.3
(S)-carboxymethyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37C
20.3
(S)-methyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37C
0.054
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
-
-
1
4-Fluorophenylalanine
-
approx. value
0.001 - 0.155
5,6,7,8-tetrahydrobiopterin
0.044
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
-
0.0344 - 0.0444
6,7-dimethyl-5,6,7,8-tetrahydropterin
0.065 - 0.105
6,7-dimethyltetrahydrobiopterin
0.033 - 0.06
6,7-dimethyltetrahydropterin
0.037 - 0.0455
6-Methyl-5,6,7,8-tetrahydropterin
0.063 - 0.083
6-methyl-tetrahydrobiopterin
0.43 - 6.9
6-methyltetrahydrobiopterin
0.01 - 0.1
6-methyltetrahydropterin
0.22
7(R,S)-tetrahydrobiopterin
-
pH 7.0, 25C, recombinant enzyme
0.008 - 0.028
Abz-VAA
0.0024
L-cyclohexylalanine
-
-
3.1 - 7.75
L-methionine
0.1 - 6.9
L-Phe
0.022 - 7.14
L-phenylalanine
1 - 8.5
L-tryptophan
29.8
N-acetyl-(S)-carboxymethyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37C
32.1
N-acetyl-(S)-methyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37C
55.97 - 63.8
N-acetyl-S-carboxymethyl-L-cysteine
58.92 - 68.25
N-acetyl-S-methyl-L-cysteine
0.043 - 1.3
phenylalanine
4.6 - 14.73
S-carboxy-methyl-L-cysteine
0.0728 - 25.24
S-carboxymethyl-L-cysteine
0.3 - 0.45
S-methyl-ergothionine
18.32 - 51.6
S-methyl-L-cysteine
0.002 - 0.5
tetrahydrobiopterin
0.47 - 1.7
thienylalanine
0.024 - 0.096
tryptophan
additional information
L-phenylalanine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.6
5,6,7,8-tetrahydrobiopterin
3 - 6
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
Chromobacterium violaceum
-
-
0.9 - 1.4
6,7-dimethyltetrahydropterin
0.031 - 7.85
6-methyl-tetrahydrobiopterin
1.6
6-methyltetrahydropterin
Chromobacterium violaceum
-
wild type enzyme, at 25C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
0.04 - 21.5
L-phenylalanine
0.4 - 2.08
L-tryptophan
0.0183 - 16
phenylalanine
additional information
additional information
Homo sapiens
-
wild-type PAH kinetic analyses using a new assay reveal cooperativity of activated PAH toward (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.6 - 48
L-phenylalanine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
(7R)-5,6,7,8-tetrahydrobiopterin
-
-
0.00027 - 0.0032
3,4-Dihydroxystyrene
1.1
4-Chlorophenylalanine
-
-
0.0023 - 0.0049
7(S)-tetrahydrobiopterin
-
pH 7.0, 25C, recombinant enzyme, versus (6R)-tetrahydrobiopterin
1.7
Acetohydroxamate
-
-
0.0000015 - 0.0000018
bathophenanthroline
0.07
benzohydroxymate
-
-
-
0.01
catechol
-
-
0.026
deaza-6-methyltetrahydropterin
-
-
3.5 - 8.11
L-methionine
0.3
L-tryptophan
-
competitive vs. iron
0.11
phenylalanine
-
competitive vs. iron
5.01 - 13.14
S-carboxy-methyl-L-cysteine
17.23
S-carboxymethyl-L-cysteine
-
in pooled hepatic cytosolic enzyme fraction, at 37C
0.41 - 0.5
S-methyl-ergothionine
17.32 - 41.53
S-methyl-L-cysteine
0.3
tyrosine
-
competitive vs. iron
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00009
-
activity in liver of males living in an area with high emissions of SO2 and nitrogen oxides, cofactor tetrahydrobiopterin
0.00033
-
activity in liver of males, cofactor tetrahydrobiopterin
0.0009
-
mutant enzyme V388M, using S-carboxymethyl-L-cysteine as substrate
0.00097
-
activity in liver of males, cofactor tetrahydrobiopterin
0.0014
-
mutant enzyme I65T, using S-carboxymethyl-L-cysteine as substrate; mutant enzyme R68S, using S-carboxymethyl-L-cysteine as substrate
0.0015
-
mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as substrate
0.0016
-
mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as substrate
0.0049
-
L-phenylalanine-activated mutant enzyme S231F, at 25C
0.0052
-
non-L-phenylalanine-activated mutant enzyme S231F, at 25C
0.006
-
activity in liver of males, cofactor 6,7-dimethyltetrahydropterin
0.055
-
I65T mutant enzyme, cofactor 6-methyltetrahydropterin
0.073
-
wild type enzyme, using S-carboxymethyl-L-cysteine as substrate
0.09
-
cofactor 6,7-dimethyltetrahydropterin
0.099
-
R270K mutant enzyme, expression in the absence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
0.105
-
activity in liver of males living in an area with high emissions of SO2 and nitrogen oxides, cofactor 6,7-dimethyltetrahydropterin
0.106
-
-
0.17
-
cofactor 6-methyltetrahydropterin
0.225
-
liver enzyme
0.247
-
activity in liver of males, cofactor 6,7-dimethyltetrahydropterin
0.307
mutant enzyme W180F, at 30C, using L-phenylalanine as substrate
0.342
mutant enzyme W180F, at 30C, using 5,6,7,8-tetrahydrobiopterin as substrate
0.347
wild type enzyme, at 30C, using 5,6,7,8-tetrahydrobiopterin as substrate
0.408
-
V388M mutant enzyme, cofactor tetrahydrobiopterin
0.4169
-
non-L-phenylalanine-activated wild type enzyme, at 25C
0.424
-
maltose-binding-protein phenylalanine hydroxylase fusion protein, dimeric form
0.44
-
liver enzyme
0.505
-
mutant enzyme V388M, using L-phenylalanine as substrate
0.536
-
R261Q mutant enzyme, cofactor tetrahydrobiopterin
0.69
wild type enzyme, at 30C, using L-tryptophan as substrate
0.7418
-
L-phenylalanine-activated wild type enzyme, at 25C
0.745
-
V388M mutant enzyme, cofactor 6-methyltetrahydropterin
0.75
-
mutant enzyme R408W, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25C
0.77
-
mutant R68V, preincubation with L-phenylalanine
0.78
-
R261Q mutant enzyme, cofactor 6-methyltetrahydropterin
0.893
mutant enzyme W180F, at 30C, using L-tryptophan as substrate
1
mutant enzyme L101Y, at 30C, using 5,6,7,8-tetrahydrobiopterin as substrate; mutant enzyme L101Y/W180F, at 30C, using L-phenylalanine as substrate
1.05
mutant enzyme L101Y/W180F, at 30C, using 5,6,7,8-tetrahydrobiopterin as substrate
1.08
-
mutant C237R
1.1
-
wild-type, preincubation with L-phenylalanine
1.13
-
mutant C237R, preincubation with L-phenylalanine
1.2
-
mutant enzyme Y414C, using L-phenylalanine as substrate
1.283
-
maltose-binding-protein phenylalanine hydroxylase fusion protein, tetrameric form
1.32
-
mutant enzyme R155H, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25C
1.46
-
; enzyme form II
1.49
-
mutant enzyme R261Q, using L-phenylalanine as substrate
1.6
-
fetal liver enzyme
1.64
-
mutant enzyme D143G, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25C
1.7
-
pH 7.0, 25C, wild-type, dimer
1.725
-
mutant enzyme R68S, using L-phenylalanine as substrate
1.742
-
recombinant wild-type enzyme, cofactor tetrahydrobiopterin
1.76
-
adult liver enzyme
1.77
mutant enzyme L101Y, at 30C, using L-tryptophan as substrate
1.773
-
V388M mutant enzyme, expression in the absence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
1.8
-
enzyme form I
1.9
-
wild type enzyme, using L-phenylalanine as substrate
1.98
-
substrate L-phenylalanine, mutant N223D
2.1
-
micromol L-Tyr/min/mg, wild-type, pH 7.0, 25C, without L-Phe preincubated enzyme
2.14
-
mutant R68V
2.2
-
mutant R68A, preincubation with L-phenylalanine
2.25
-
mutant enzyme I65T, using L-phenylalanine as substrate
2.34
-
substrate tetrahydrobiopterin, mutant N223D
2.49
-
recombinant wild-type enzyme, cofactor 6-methyltetrahydropterin
2.76
-
mutant enzyme L348V, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25C
2.84
-
substrate tetrahydrobiopterin, mutant T427P
2.91
-
V388M mutant enzyme, expression in the presence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
2.94
-
mutant R68A
2.97
-
mutant C237A
2.98
-
wild type enzyme, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25C
3.17
-
substrate L-phenylalanine, mutant T427P
3.25
-
wild-type
3.32
-
mutant enzyme P416Q, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25C
3.37
wild type enzyme, at 30C, using L-phenylalanine as substrate
3.48
-
substrate L-phenylalanine, wild-type
3.62
mutant enzyme L101Y/W180F, at 30C, using L-tryptophan as substrate
3.67
-
substrate L-phenylalanine, mutant N426D
3.74
-
substrate L-phenylalanine, mutant N32D
3.81
-
mutant C237D
4.19
-
mutant C237D, preincubation with L-phenylalanine
4.37
-
substrate L-phenylalanine, mutant G33A
4.39
-
substrate tetrahydrobiopterin, mutant N426D
4.73
-
substrate tetrahydrobiopterin, mutant G33A; substrate tetrahydrobiopterin, mutant N32D
4.95
-
pH 7.0, 25C, wild-type, tetramer
5
-
phosphorylated recombinant wild-type enzyme, S16N and S16D mutant enzyme
5.1
-
S16A and S16K mutant enzymes
5.16
-
substrate L-phenylalanine, mutant G33V
5.2
-
S16E and S16Q mutant enzyme
5.32
-
substrate tetrahydrobiopterin, wild-type
6.19
-
substrate L-phenylalanine, mutant K113P
6.41
-
substrate tetrahydrobiopterin, mutant G33V
6.48
-
pH 7.0, 25C, N-terminal deletion mutant
6.5
-
micromol L-Tyr/min/mg, mutant Q215K/N216Y, pH 7.0, 25C, with L-Phe preincubated enzyme
6.8
-
recombinant enzyme
8.32
-
pH 7.0, 25C, N-terminal plus C-terminal deletion mutant
8.56
-
substrate tetrahydrobiopterin, mutant K113P
10.16
mutant enzyme L101Y, at 30C, using L-phenylalanine as substrate
10.2
-
in 100 mM Na-HEPES, pH 7.0 at 37C
12.5 - 13
-
-
14
-
truncated enzyme containing C-terminal 334 amino acids
290
-
mutant Y325A, 25C, pH 7.0
300
-
mutant Y325A, preincubation with L-phenylalanine, 25C, pH 7.0
1150
-
mutant Y325F, 25C, pH 7.0
1230
-
wild-type, 25C, pH 7.0
1310
-
mutant Y325L, 25C, pH 7.0
1500
-
mutant Y325L, preincubation with L-phenylalanine, 25C, pH 7.0
3630
-
mutant Y325F, preincubation with L-phenylalanine, 25C, pH 7.0
3640
-
wild-type, preincubation with L-phenylalanine, 25C, pH 7.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7.3
-
assay at
7.5
-
assay at
7.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide