Information on EC 1.14.16.1 - phenylalanine 4-monooxygenase

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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
-
-
phenylalanine metabolism
-
-
Phenylalanine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Folate biosynthesis
-
-
Metabolic pathways
-
-
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
a psychrophilic bacterium
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
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-5,6,7,8-tetrahydropterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
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
5-hydroxytryptophan + 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
5,6-dimethyl-3-(4-methyl-2-pyridinyl)-2-thioxo-2,3-dihydrothieno[2,3-d]pyrimidin-4(1H)-one
-
weak competitive inhibitor
-
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
panobinostat
-
competitive inhibition
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
(S)-2-amino-3-phenyl-1-propanol
-
6.5fold activation at 10 mM
-
3-Phenylpropionate
-
1.8fold activation at 50 mM
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
-
D-phenylalanine
-
7.1fold activation at 10 mM
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-4-aminophenylalanine
-
3.2fold activation at 10 mM
L-isoleucine
-
1.5fold activation at 50 mM
L-leucine
-
2.2fold activation at 50 mM
L-methionine
-
5.8fold activation at 50 mM
L-norleucine
-
6.6fold activation at 50 mM
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 37°C
20.3
(S)-methyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C
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 - 0.262
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, 25°C, 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 - 500
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 37°C
32.1
N-acetyl-(S)-methyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C
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
-
-
0.9 - 1.4
6,7-dimethyltetrahydropterin
0.031 - 7.85
6-methyl-tetrahydrobiopterin
1.6
6-methyltetrahydropterin
-
wild type enzyme, at 25°C 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
-
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
0.8 - 130
6,7-dimethyl-5,6,7,8-tetrahydropterin
0.59 - 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
-
-