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Information on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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1.14.16.1 phenylalanine 4-monooxygenaseIUBMB Comments
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.
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Word Map
- 1.14.16.1
- phenylketonuria
- hyperphenylalaninemia
- bh4
- pterins
-
hydroxylases
-
inborn
- l-tyrosine
-
genotype-phenotype
- tetrahydropterins
-
dehydratase
- catecholamine
- serotonin
- dihydropteridine
- dopamine
-
intellectual
- sepiapterin
-
province
- molecular biology
-
cyclohydrolase
- violaceum
-
rflps
- pteridine
- p-chlorophenylalanine
-
chromobacterium
-
quinonoid
-
genotype-based
- dihydrobiopterin
- dopa
- lysolecithin
- melanin
-
counsel
-
non-heme
- neopterin
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dihydrochloride
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hypopigmentation
-
neuropsychological
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
phenylalanine hydroxylase, pheoh, phenylalanine 4-hydroxylase, phenylalanine monooxygenase, dicpah, cepah, l-phenylalanine 4-hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.14.3.1
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-
formerly
-
EC 1.99.1.2
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-
formerly
-
L-phenylalanine 4-hydroxylase
oxygenase, phenylalanine 4-mono-
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-
-
-
P4H
PAH
PheH
phenylalaninase
-
-
-
-
phenylalanine 4-hydroxylase
phenylalanine hydroxylase
phenylalanine monooxygenase
phhA
PAH
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-
-
-
PAH
-
-
PAH
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phenylalanine 4-hydroxylase
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-
-
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phenylalanine hydroxylase
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-
-
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phenylalanine hydroxylase
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-
phenylalanine hydroxylase
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phenylalanine hydroxylase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
enzyme requires an initial reduction of Cu2+ to Cu+ for activation
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
proposed catalytic cycle
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
mechansim, conformational transition and hysteresis
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
analysis of conformational changes upon substrate binding
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
sequential ter-bi mechansim, L-phenylalanine is the middle substrate in order of binding
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
substrate binding triggers structural changes throughout the entire tetrameric enzyme
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
catalytic mechanism
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
residues S391 and G332 are important for activity
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
kinetics, molecular dynamics simulations, structure-energetics calculations, and molecular interaction fields, structure-function analysis
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
substrate and oxygen binding site, reaction mechanism, structure-function analysis
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
substrate and oxygen binding site, reaction mechanism, structure-function analysis
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
substrate and oxygen binding site, reaction mechanism, structure-function analysis
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
molecular mechanism
Q9XYQ5
L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
structural analysis reveal an additional L-Phe binding site at the regulatory domain of full-length cePAH. This site involves the GA(S)L/ISRP motifs, which are also found in ACT domains of other L-Phe binding proteins
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
1H-15N HSQC NMR spectra are obtained of the 15N-labeled protein alone and in the presence of phenylalanine. Regulatory domain of phenylalanine hydroxylase can bind phenylalanine, consistent with the presence of an allosteric site for the amino acid
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
hydrogen/deuterium exchange monitored by mass spectrometry is used to gain insight into local conformational changes accompanying activation of rat phenylalanine hydroxylase by phenylalanine. Peptides in the regulatory and catalytic domains that lie in the interface between these two domains show large increases in the extent of deuterium incorporation from solvent in the presence of phenylalanine
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L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
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oxidation
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oxidation
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S-oxidation of S-carboxymethyl-L-cysteine, C-oxidation of L-phenylalanine
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9029-73-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
(S)-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
low activity
-
-
?
(S)-ethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
(S)-ethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
(S)-methyl-ergothionine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
low activity
-
-
?
(S)-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
(S)-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
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low activity
-
-
?
3-(2-thienyl)-L-alanine + 6-methyltetrahydropterin + O2
? + 6-methyldihydropterin + H2O
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-
-
-
?
3-(2-thienyl)-L-alanine + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
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-
-
-
?
4-methyl-L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
?
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-
-
-
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
L-methionine + tetrahydrobiopterin + O2
?
-
lysolecithin activated enzyme
-
-
?
L-norleucine + tetrahydrobiopterin + O2
?
-
lysolecithin activated enzyme
-
-
?
L-norleucine + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
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5% of the activity with 3-(2-thienyl)-L-alanine
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-
?
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
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-
-
-
?
L-phenylalanine + (6R)-tetrahydrobiopterin + O2
L-tyrosine + (6R)-dihydrobiopterin + H2O
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in mammals rate-limiting step in complete catabolism of phenylalanine to CO2 and water
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?
L-phenylalanine + 5,6,7,8-tetrahydro-L-biopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
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-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 7,8-dimethyl-6,7-dihydrobiopterin + H2O
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-
-
-
-
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydropterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
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-
-
-
?
L-phenylalanine + 6,7-dimethyl-tetrahydrobiopterin + O2
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
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-
-
-
?
L-phenylalanine + 6,7-dimethyltetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
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-
-
-
?
L-phenylalanine + 6-methyl-tetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4-hydroxy-tetrahydrobiopterin
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-
-
-
?
L-phenylalanine + 6-methyl-tetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4a-hydroxy-tetrahydrobiopterin
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-
-
-
?
L-phenylalanine + 6-methyltetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4a-hydroxytetrahydrobiopterin
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-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
2-amino-4a-hydroxy-7-methyl-5,6,7,8-tetrahydropteridin-4(4aH)-one + H2O + ?
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-
-
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?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-phenylalanine + 6-methyldihydropterin + H2O2
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copper-depleted enzyme, in the absence of Fe2+, 6-methyltetrahydropterin oxidation can be uncoupled from substrate hydroxylation by the exclusion of iron
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?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
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low activity with 6-methyltetrahydropterin
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-
?
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
N-acetyl-(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
N-acetyl-(S)-carboxymethyl-L-cysteine S-oxide + ?
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-
-
-
?
N-acetyl-(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
-
-
-
?
N-acetyl-(S)-methyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
N-acetyl-(S)-methyl-L-cysteine S-oxide + ?
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-
-
-
?
phenylalanine + tetrahydrobiopterin + O2
tyrosine + 4a-hydroxytetrahydrobiopterin
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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
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-
ir
S-carboxy-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
S-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
S-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
?
-
conversion to the (S)-sulfoxide
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-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
S-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
S-methyl-L-cysteine + tetrahydrobiopterin + O2
?
-
lysolecithin activated enzyme
-
-
?
S-methyl-L-cysteine + tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
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74% methyl-hydroxylation, 26% para-hydroxylation, shift of para-substituent by NIH shift mechanism
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
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79% methyl-hydroxylation, 21% para-hydroxylation, shift of para-substituent by NIH shift mechanism
?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
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4times slower reaction than with L-phenylalanine
-
?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
-
50% less active than the enzyme from Chromobacterium violaceum
-
?
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
structure-function relationships
-
-
?
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
an automated fluorescence-based continuous real-time PAH activity assay that is faster and more efficient but as precise and accurate as standard methods is developed. The assay is performed with and without preincubation of the enzyme with 1 mM L-Phe
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
substrate binding by His285, Trp326, Arg270, Ser349, and Trp278
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
specific for the L-isomer, no activity with the D-isomer, effects of isotopic substrates [4-2H]-, [3,5-2H2]-, and 2H5-phenylalanine, overview
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
highest activity
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 6-methyldihydropterin + H2O
-
-
in the presence of FeSO4 and dithiothreitol
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 6-methyldihydropterin + H2O
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
modelling of cellular regulation
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
Q9XYQ5
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
Q9XYQ5
mechanism and regulation of the enzyme, which is involved in synthesis of a melamin compound required for cuticle synthesis, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
although the enzyme is monomeric with a single L-Phe-binding site, the substrate binds cooperatively
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
preferred substrate
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
the enzyme catalyzes the catabolism of L-Phe, mainly in the liver, and is increased in response to L-Phe, determination of dietary requirement for L-phenylalanine, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
ir
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
687979, 689888, 727014, 727648, 728633, 744514, 744845, 744917, 744918, 745024, 745169, 745398, 745400, 745582, 745600, 745782, 746450
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
enzyme mutations can lead to phenylketonuria and BH4-responsive hyperphenylalaninemia in case of enzyme deficiency
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
enzyme mutations can lead to phenylketonuria, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
impact of the enzyme structure on its regulation, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
mutations in the pah gene, e.g. manifestating in the regulatory domain, can lead to phenylketonuria, patients respond to treatment with tetrahydrobiopterin, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
the native regulation system is designed to maintain phenylalanine levels constant in the human body
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
active site structure, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
preferred substrate
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
preferred substrate
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
preferred substrate
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
preferred substrate
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 2-amino-4-hydroxy-6-methyltetrahydropteridine, tetrahydrofolate, and 6-methyl-5-deazatetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 2-amino-4-hydroxy-6-methyltetrahydropteridine, tetrahydrofolate, and 6-methyl-5-deazatetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 2-amino-4-hydroxy-6-methyltetrahydropteridine, tetrahydrofolate, and 6-methyl-5-deazatetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis, alkylation of sulfhydryl groups with N-ethylmaleimide or phosphorylation by cAMP-dependent protein kinase
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
-
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
4-alpha-carbinolamine is the first free pterin product formed
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
specificity is quantitatively altered when the enzyme is activated by lysolecithin
4-alpha-carbinolamine is the first free pterin product formed
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methyltetrahydropterin, 7-methylpterin, and 2,4,5-triamino-6-hydroxypyrimidine
-
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methyltetrahydropterin, 7-methylpterin, and 2,4,5-triamino-6-hydroxypyrimidine
4-alpha-carbinolamine is the first free pterin product formed
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
non activated enzyme has much greater activity with 6-methyltetrahydropterin and dimethyltetrahydropterin than with tetrahydrobiopterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
-
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
low activity with tetrahydrobiopterin can be selectively increased by a wide variety of reversible and irreversible modificators of the enzyme, e.g. interaction with phospholipids
4-alpha-carbinolamine is the first free pterin product formed
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
-
?
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
-
the activity for L-tryptophan is extremely low compared to L-phenylalanine activity levels
-
-
?
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
the activity for L-tryptophan is extremely low compared to L-phenylalanine activity levels
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
?
-
0.4% of activity with L-phenylalanine
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
?
-
truncated enzyme containing C-terminal 334 amino acids
-
-
?
S-carboxy-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
poor substrate
-
-
?
S-carboxy-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
poor substrate
-
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
S-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
poor substrate
-
-
?
S-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
poor substrate
-
-
?
S-methyl-L-cysteine + tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
S-methyl-L-cysteine + tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
-
?
additional information
?
-
-
EPR and UV-Vis studies of enzyme-nitric oxide adducts, increase in NO affinity in the presence of substrate, overview
-
-
-
additional information
?
-
-
no activity against 5-deaza,6-methyltetrahydropterin
-
-
-
additional information
?
-
-
enzyme deletion mutations are involved in development of the autosomal recessive genetic disorder phenylketonuria, overview
-
-
-
additional information
?
-
-
pterin-4a-carbinolamine dehydratase, PCD, is an essential component of the phenylalanine hydroxylase system, catalyzing the regeneration of the essential cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin, i.e. (6R)BH4, PHA is implicated in primapterinuria, a variant form of phenylketonuria, phenylalanine hydroxylase system overview
-
-
-
additional information
?
-
-
hyperphenylalaninemia comprises a group of autosomal recessive disorders mainly caused by phenylalanine hydroxylase gene mutations
-
-
-
additional information
?
-
-
hyperphenylalaninemia is a group of autosomal recessive disorders caused by a wide range of PAH gene variants
-
-
-
additional information
?
-
-
the enzyme is important in the metabolism of xenobiotic thioether substrates, overview
-
-
-
additional information
?
-
-
does not use thiodiglycolic acid as substrate
-
-
-
additional information
?
-
-
the rate of clearance of the substrates via human PAH is L-phenylalanine > L-methionine > S-carboxy-methyl-L-cysteine > S-methyl-L-cysteine
-
-
-
additional information
?
-
-
thiodiglycolic acid is not a substrate for PAH
-
-
-
additional information
?
-
-
thiodiglycolic acid, (S)-pentyl-L-cysteine, (S)-hexyl-L-cysteine, (S)-heptyl-L-cysteine, (S)-octyl-L-cysteine, and (S)-benzyl-L-cysteine are no substrates
-
-
-
additional information
?
-
-
the enzyme is nearly incapable of hydroxylating tyrosine
-
-
-
additional information
?
-
-
phenylalanine monooxygenase is the only enzyme responsible for the sulfur oxygenation of S-carboxymethyl-L-cysteine
-
-
-
additional information
?
-
-
the enzyme is important in the metabolism of xenobiotic thioether substrates, overview
-
-
-
additional information
?
-
-
the rate of clearance of the substrates via rat PAH is L-phenylalanine > L-methionine > S-carboxy-methyl-L-cysteine > S-methyl-L-cysteine
-
-
-
additional information
?
-
-
thiodiglycolic acid is not a substrate for PAH
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
L-phenylalanine + (6R)-tetrahydrobiopterin + O2
L-tyrosine + (6R)-dihydrobiopterin + H2O
-
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
-
-
-
-
?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
phenylalanine + tetrahydrobiopterin + O2
tyrosine + 4a-hydroxytetrahydrobiopterin
-
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
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
modelling of cellular regulation
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
Q9XYQ5
mechanism and regulation of the enzyme, which is involved in synthesis of a melamin compound required for cuticle synthesis, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
P30967
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
Q47XN7
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
the enzyme catalyzes the catabolism of L-Phe, mainly in the liver, and is increased in response to L-Phe, determination of dietary requirement for L-phenylalanine, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
684443, 684445, 688016, 688178, 726815, 728775, 745105, 746412, 689888, 727014, 727648, 728633, 744514, 744845, 744917, 744918, 745024, 745169, 745398, 745400, 745582, 745600, 745782, 746450
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
Q8TEY0
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
enzyme mutations can lead to phenylketonuria and BH4-responsive hyperphenylalaninemia in case of enzyme deficiency
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
enzyme mutations can lead to phenylketonuria, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
impact of the enzyme structure on its regulation, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
mutations in the pah gene, e.g. manifestating in the regulatory domain, can lead to phenylketonuria, patients respond to treatment with tetrahydrobiopterin, overview
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
the native regulation system is designed to maintain phenylalanine levels constant in the human body
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
additional information
?
-
-
enzyme deletion mutations are involved in development of the autosomal recessive genetic disorder phenylketonuria, overview
-
-
-
additional information
?
-
-
pterin-4a-carbinolamine dehydratase, PCD, is an essential component of the phenylalanine hydroxylase system, catalyzing the regeneration of the essential cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin, i.e. (6R)BH4, PHA is implicated in primapterinuria, a variant form of phenylketonuria, phenylalanine hydroxylase system overview
-
-
-
additional information
?
-
-
hyperphenylalaninemia comprises a group of autosomal recessive disorders mainly caused by phenylalanine hydroxylase gene mutations
-
-
-
additional information
?
-
-
hyperphenylalaninemia is a group of autosomal recessive disorders caused by a wide range of PAH gene variants
-
-
-
additional information
?
-
-
the enzyme is important in the metabolism of xenobiotic thioether substrates, overview
-
-
-
additional information
?
-
-
the enzyme is important in the metabolism of xenobiotic thioether substrates, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(6R)-5,6,7,8-tetrahydro-L-monapterin
-
7% of the activity with 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
6,7-dimethyltetrahydropterin
-
17% of the activity with tetrahydrobiopterin
5,6,7,8-tetrahydro-L-biopterin
-
PAH can be activated up to 20times in the presence of its natural cofactor 5,6,7,8-tetrahydro-L-biopterin but cannot be activated in the presence of synthetic cofactors such as 6,7-dimethyltetrahydrobiopterin or 6-methyltetrahydropterin
5,6,7,8-tetrahydro-L-biopterin
-
-
tetrahydrobiopterin
-
required for activity, binding involves Ph254 and Tyr325, structure overview
tetrahydrobiopterin
-
-
438654, 438655, 438714, 438715, 438716, 438721, 438722, 438725, 438726, 438729, 438731, 684717, 688016
tetrahydrobiopterin
-
-
438654, 438716, 438724, 438727, 438734, 672381, 673309, 684389, 684445, 686957, 687588, 687979, 688016, 688143, 688178, 689019, 689888, 745398
tetrahydrofolate
-
10% of activity with 6,7-dimethyltetrahydropterin
tetrahydrofolate
-
20% of the activity with tetrahydrobiopterin
additional information
-
artificial cofactor: 2,4,5-triamino-6-hydroxypyrimidine; artificial cofactors: 6-methyltetrahydropterin, 6,7-dimethyltetrahydropterin; artificial cofactors: 6-methyltetrahydropterin, 7-methylpterin
-
additional information
-
artificial cofactors: 6-methyltetrahydropterin, 6,7-dimethyltetrahydropterin; artificial cofactors: 6-methyltetrahydropterin, 7-methylpterin
-
additional information
-
artificial cofactors: 6-methyltetrahydropterin, 6,7-dimethyltetrahydropterin
-
additional information
-
artificial cofactors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 6-methyl-5-deazatetrahydropterin and 2-amino-4-hydroxy-6-methyltetrahydropteridine can replace tetrahydrobiopterin
-
additional information
-
artificial cofactors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 6-methyl-5-deazatetrahydropterin and 2-amino-4-hydroxy-6-methyltetrahydropteridine can replace tetrahydrobiopterin; artificial cofactors: 6-methyltetrahydropterin, 6,7-dimethyltetrahydropterin
-
additional information
-
artificial cofactors: 6-methyltetrahydropterin, 6,7-dimethyltetrahydropterin
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
substoichiometric amounts after removal of copper with dithiothreitol
Co2+
-
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
copper
Fe2+
Iron
Zn2+
copper
-
1 mol of Cu2+ per mol of enzyme; electron paramagnetic resonance spectroscopy indicates a type II copper-containing enzyme
copper
-
copper does not support enzyme activity and can be removed by dithiothreitol
Fe2+
-
incubation of apo-PAH with 0.5 mM Fe2+ and removal of free Fe2+ provides a holoenzyme which retains almost stoichiometric amounts of Fe2+ bound (0.88 mol Fe2+/mol monomer)
Fe2+
-
native metal cofactor, determination of binding affinity, binding structure, overview
Fe2+
-
0.1 mM added as ferrous ammonium sulfate, 40-70% activation depending on assay conditions
Fe2+
-
nonheme iron is bound on one face by residues His285, His290, and Glu330 forming a a 2-His-1-carboxylate facial triad, the three ligands differ in their sensitivity to mutagenesis, structure, overview
Iron
-
electron paramagnetic resonance spectrum; iron-protein; one-dimensional 1H-NMR spectroscopy of iron
Iron
-
copper depleted enzyme can be reconstituted with approx. 1 molecule of iron per enzyme molecule, iron reconstituted enzyme hydroxylates phenylalanine
Iron
-
non-heme iron, required, effects of cofactor and substrate on the iron environment, the abilities of nitric oxide to behave as an oxygen mimic and a spectroscopic probe of ferrous iron are used to investigate the geometric and electronic effects of cofactor and substrate binding to cPAH by electron paramagnetic resonance (EPR) and UV-Vis spectroscopies, overview
Iron
-
conformation and distances to the catalytic iron of both L-phenylalanine and the cofactor analog L-erythro-7,8-dihydrobiopterin simultaneously bound to the recombinant enzyme estimated by 1H-NMR
Iron
-
electron paramagnetic resonance spectrum; iron-protein; one-dimensional 1H-NMR spectroscopy of iron
Iron
-
1 iron atom per subunit, fully active enzyme has non-heme high-spin ferric iron coordinated at the active site
Iron
-
electron paramagnetic resonance spectrum; iron can be removed by treatment with o-phenanthroline, reconstitution of apoenzyme with iron restores 90% of the initial activity; iron-protein
Iron
-
kinetic data suggest, that enzyme's iron is solvent-accessible and resides in a hydrophobic pocket of the enzyme
Zn2+
-
substoichiometric amounts after removal of copper with dithiothreitol
Zn2+
-
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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'-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
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
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
Acetohydroxamate
-
competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron
bathophenanthroline
-
competitive vs. 6-methyl-5,6,7,8-tetrahydropterin and tetrahydrobiopterin, most probably due to chelation of enzyme's iron
benzohydroxamate
-
competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron
tetrahydrobiopterin
-
excessive dosages of BH4 inhibit PAH under normal phenylalanine conditions in vivo and activate PAH under conditions of high phenylalanine, overview
(6R)-L-erythro-tetrahydrobiopterin
-
inhibits phenylalanine and lysolecithin activation
4-Chlorophenylalanine
-
specific PAH inhibitor, 97.2% inhibition at 1.0 mM using L-phenylalanine as substrate, 99.2% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
dithiothreitol
-
2 mM, 94% inhibition, dithiothreitol induces the dissociation of iron from the enzyme, catalase and phenylalanine partially protect from inhibition
EDTA
-
in the absence of added iron in the assay, the EDTA-treated PheH exhibits 3.5% of the L-phenylalanine hydroxylation activity of the metal-containing enzyme
L-phenylalanine
-
competitive inhibition of the S-oxidation of S-carboxymethyl-L-cysteine, 92.8% inhibition at 1.0 mM using S-carboxymethyl-L-cysteine as substrate
S-carboxy-methyl-L-cysteine
-
competitive inhibitor of the C-oxidation of L-phenylalanine
S-carboxy-methyl-L-cysteine
-
competitive inhibitor of the C-oxidation of L-phenylalanine
S-carboxymethyl-L-cysteine
-
competitive inhibitor of the aromatic C-oxidation of L-phenylalanine, 25.2% inhibition at 5.0 mM using L-phenylalanine as substrate
S-carboxymethyl-L-cysteine
-
competitive to L-phenylalanine, 5 mM, 74% residual activity with substrate L-phenylalanine
S-methyl-ergothionine
-
competitive inhibitor of the C-oxidation of L-phenylalanine
S-methyl-ergothionine
-
competitive inhibitor of the C-oxidation of L-phenylalanine
S-methyl-L-cysteine
-
competitive inhibitor of the C-oxidation of L-phenylalanine
S-methyl-L-cysteine
-
competitive to L-phenylalanine, 5 mM, 89% residual activity with substrate L-phenylalanine
S-methyl-L-cysteine
-
competitive inhibitor of the C-oxidation of L-phenylalanine
additional information
-
the treatment with EDTA leads to the fully reversible release of iron from the active site without irreversibly inactivating the enzyme
-
additional information
-
not inhibited by the nitric oxide synthase inhibitors N(G)-monomethyl-D-arginine, 7-nitroindazole, L-thiocitrulline, N(G)-monomethyl-L-arginine, (S)-methy-L-thiocitrulline, and L-N5-(1-iminoethyl)ornithine; PH8, the large aromatic amino acid hydroxylase monoclonal antibody, inhibits the production of both L-tyrosine and S-carboxymethyl-L-cysteine S-oxide to 99.0% and 99.3% at 0.2 mg/ml concentration
-
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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
-
approx. 4.5fold increase in activity of non-phosphorylated and phosphorylated enzyme, cofactor tetrahydrobiopterin
phenylalanine
-
recombinant enzyme, 2fold increase in activity, cofactor tetrahydrobiopterin
phenylalanine
-
after activation with phenylalanine the dimer/tetramer equilibrium is shifted towards the tetrameric form; 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
-
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
phenylalanine
-
homotropic allosteric activator of both hepatic and recombinant enzymes
Phospholipids
-
activate; 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
-
enzyme activity is not stimulated by phosphorylation; 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
-
non activated enzyme has much greater activity with 6-methyltetrahydropterin and dimethyltetrahydropterin than with tetrahydrobiopterin; relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis; relatively low activity with tetrahydrobiopterin can be selectively increased by phosphorylation
-
additional information
-
relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis
-
additional information
-
not significantly activated by L-valine, L-alanine, and L-serine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
-
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
0.025
(6R)-5,6,7,8-tetrahydrobiopterin
-
recombinant enzyme, phenylalanine-activated
0.008
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
wild-type, pH 7.3, 25°C, measurement by continuous PAH activity assay (direct in-well fluorescence detection): Vmax: 2.277 micromol L-Tyr/min/mg (without L-Phe preincubation)
0.024
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
wild-type, pH 7.3, 25°C, measurement by standard discontinuous PAH activity assay (HPLC and fluorimetric detection): Vmax: 3.425 micromol L-Tyr/min/mg (with L-Phe preincubation)
0.027
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
mutant enzyme R155H, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.029
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
wild-type, pH 7.0, 25°C
0.03
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
mutant enzyme P416Q, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.033
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
wild type enzyme, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.035
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
mutant enzyme R408W, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.04
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
mutant enzyme L348V, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.053
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
mutant enzyme D143G, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.094
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
mutant Q215K/N216Y, pH 7.0, 25°C
0.022
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme Y414C, using L-phenylalanine as cosubstrate
0.0231
5,6,7,8-tetrahydrobiopterin
-
using L-phenylalanine as cosubstrate, in pooled hepatic cytosolic enzyme fraction, at 37°C
0.02333
5,6,7,8-tetrahydrobiopterin
-
using L-phenylalanine as cosubstrate, in pooled hepatic cytosolic enzyme fraction activated with 1 mM lysophosphatidylcholine, at 37°C
0.024
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme V388M, using L-phenylalanine as cosubstrate
0.026
5,6,7,8-tetrahydrobiopterin
-
wild type enzyme, using L-phenylalanine as cosubstrate
0.027
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme R261Q, using L-phenylalanine as cosubstrate
0.032
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme R68S, using L-phenylalanine as cosubstrate
0.035
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.04
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme I65T, using L-phenylalanine as cosubstrate
0.0728
5,6,7,8-tetrahydrobiopterin
-
wild type enzyme, using S-carboxymethyl-L-cysteine as cosubstrate
0.07312
5,6,7,8-tetrahydrobiopterin
-
using S-carboxymethyl-L-cysteine as cosubstrate, in pooled hepatic cytosolic enzyme fraction activated with 1 mM lysophosphatidylcholine, at 37°C
0.07812
5,6,7,8-tetrahydrobiopterin
-
using S-carboxymethyl-L-cysteine as cosubstrate, in pooled hepatic cytosolic enzyme fraction, at 37°C
0.086
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.099
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.14
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme R68S, using S-carboxymethyl-L-cysteine as cosubstrate
0.14
5,6,7,8-tetrahydrobiopterin
-
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.143
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as cosubstrate
0.146
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme V388M, using S-carboxymethyl-L-cysteine as cosubstrate
0.15
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme I65T, using S-carboxymethyl-L-cysteine as cosubstrate
0.155
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as cosubstrate
0.0344
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
enzyme form II, substrate L-phenylalanine
0.0444
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
enzyme form I, substrate L-phenylalanine
0.152
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
wild type enzyme, at pH 7.4 and 20°C
0.236
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
mutant enzyme D139N, at pH 7.4 and 20°C
0.254
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
mutant enzyme D139N, at pH 7.4 and 20°C
0.262
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
mutant enzyme D139N, at pH 7.4 and 20°C
0.105
6,7-dimethyltetrahydrobiopterin
-
chymotrypsin activated liver enzyme
0.037
6-Methyl-5,6,7,8-tetrahydropterin
-
enzyme form I, substrate L-phenylalanine
0.0455
6-Methyl-5,6,7,8-tetrahydropterin
-
enzyme form II, substrate L-phenylalanine
0.063
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH V379D
0.083
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH
0.43
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant E330H; pH 7.0, 25°C, mutant H285E; pH 7.0, 25°C, wild-type enzyme
0.073
6-methyltetrahydropterin
-
maltose-binding-protein phenylalanine fusion protein
0.085
6-methyltetrahydropterin
-
truncated enzyme containing C-terminal 334 amino acids
0.1
L-Phe
-
allelic combination wild-type/mutant I65T, Vmax: 1 micromol/min/mg, pH 6.8, 37°C; allelic combination wild-type/mutant R68S, Vmax: 1 micromol/min/mg, pH 6.8, 37°C; allelic combination wild-type/wild-type, Vmax: 3 micromol/min/mg, pH 6.8, 37°C
0.2
L-Phe
-
allelic combination wild-type/mutant Y414C, Vmax: 1 micromol/min/mg, pH 6.8, 37°C
0.9
L-Phe
-
allelic combination wild-type/mutant V388M, Vmax: 0.9 micromol/min/mg, pH 6.8, 37°C
1
L-Phe
-
allelic combination wild-type/mutant R158Q, Vmax: 0.9 micromol/min/mg, pH 6.8, 37°C; allelic combination wild-type/mutant R261Q, Vmax: 0.9 micromol/min/mg, pH 6.8, 37°C
2
L-Phe
-
allelic combination wild-type/mutant I174T, Vmax: 0.7 micromol/min/mg, pH 6.8, 37°C
3
L-Phe
-
allelic combination wild-type/mutant R408W, Vmax: 0.7 micromol/min/mg, pH 6.8, 37°C
0.022
L-phenylalanine
-
mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.024
L-phenylalanine
-
mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.026
L-phenylalanine
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.027
L-phenylalanine
-
mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.032
L-phenylalanine
-
mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.033
L-phenylalanine
-
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.04
L-phenylalanine
-
mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.05
L-phenylalanine
-
post-translational activation of human cDNA-expressed PAH, activator: NO (nitric oxide) (0.01 mM), Vmax: 33.05 nmoles/min/mg, pH 6.8, 37°C
0.06
L-phenylalanine
-
post-translational activation of human cDNA-expressed PAH, activator: ONOO- (peroxynitrite)(1 mM), Vmax: 32.65 nmoles/min/mg, pH 6.8, 37°C
0.07
L-phenylalanine
-
post-translational activation of human cDNA-expressed PAH, activator: HO (hydroxyl radical) (0.01 mM), Vmax: 32.3 nmoles/min/mg, pH 6.8, 37°C
0.09
L-phenylalanine
-
native liver enzyme in crude extract, cofactor 6-methyltetrahydropterin
0.111
L-phenylalanine
-
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.12
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH
0.12
L-phenylalanine
-
post-translational activation of human cDNA-expressed PAH, activator: lysophosphatidylcholine (5 mM), Vmax: 3.72 nmoles/min/mg, pH 6.8, 37°C; post-translational activation of human cDNA-expressed PAH, activator: N-ethylmaleimide (50 mM), Vmax: 9.3 nmoles/min/mg, pH 6.8, 37°C
0.1365
L-phenylalanine
-
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.14
L-phenylalanine
-
post-translational activation of human cDNA-expressed PAH, activator: H2O2 (0.1 mM), Vmax: 28.4 nmoles/min/mg, pH 6.8, 37°C; post-translational activation of human cDNA-expressed PAH, activator: L-Phe (4 mM), Vmax: 1.86 nmoles/min/mg, pH 6.8, 37°C
0.16
L-phenylalanine
-
in pooled hepatic cytosolic enzyme fraction activated with 1 mM lysophosphatidylcholine, at 37°C
0.194
L-phenylalanine
-
cofactor tetrahydrobiopterin, maltose-binding-protein phenylalanine fusion protein
0.236
L-phenylalanine
-
cofactor tetrahydrobiopterin, cleaved maltose-binding-protein phenylalanine fusion protein
0.244
L-phenylalanine
-
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.253
L-phenylalanine
-
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.287
L-phenylalanine
-
wild type enzyme, 5 min preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C
0.3 - 0.4
L-phenylalanine
-
native and recombinant enzyme, cofactor 6-methyltetrahydropterin
0.318
L-phenylalanine
-
wild-type, pH 7.3, 25°C, measurement by continuous PAH activity assay (direct in-well fluorescence detection): Vmax: 2.53 micromol L-Tyr/min/mg (without L-Phe preincubation), 6.59 micromol L-Tyr/min/mg (with L-Phe preincubation)
0.414
L-phenylalanine
-
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.42
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH V379D
0.454
L-phenylalanine
-
cofactor 6-methyl-5,6,7,8-tetrahydropterin, enzyme form II
0.4675
L-phenylalanine
-
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.478
L-phenylalanine
-
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.504
L-phenylalanine
-
cofactor 6-methyltetrahydropterin, maltose-binding-protein phenylalanine fusion protein
0.637
L-phenylalanine
-
wild type enzyme, without preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C
0.6872
L-phenylalanine
-
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.72
L-phenylalanine
-
cofactor 6-methyl-5,6,7,8-tetrahydropterin, enzyme form I
0.87
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: NO (nitric oxide) (0.01 mM), Vmax: 274.5 nmoles/min/mg, pH 6.8, 37°C
1.1
L-phenylalanine
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C
1.22
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: N-ethylmaleimide (50 mM), Vmax: 224 nmoles/min/mg, pH 6.8, 37°C
1.25
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: ONOO- (peroxynitrite)(1 mM), Vmax: 260.4 nmoles/min/mg, pH 6.8, 37°C
1.43
L-phenylalanine
-
cofactor 6,7-dimethyl-5,6,7,8-tetrahydropterin, enzyme form II
1.5 - 2
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: HO (hydroxyl radical) (0.01 mM), Vmax: 241.6 nmoles/min/mg, pH 6.8, 37°C
1.92
L-phenylalanine
-
cofactor 6,7-dimethyl-5,6,7,8-tetrahydropterin, enzyme form I
2.85
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: lysophosphatidylcholine (5 mM), Vmax: 29.1 nmoles/min/mg, pH 6.8, 37°C
3.01
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: H2O2 (0.1 mM), Vmax: 205 nmoles/min/mg, pH 6.8, 37°C
3.05
L-phenylalanine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: L-Phe (4 mM), Vmax: 14.23 nmoles/min/mg, pH 6.8, 37°C
1
L-tryptophan
-
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
3.44
L-tryptophan
-
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
3.54
L-tryptophan
-
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
4.06
L-tryptophan
-
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
8.5
L-tryptophan
-
cofactor 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, enzyme form I
55.97
N-acetyl-S-carboxymethyl-L-cysteine
-
wild type enzyme from hepatic cytosol
57.15
N-acetyl-S-carboxymethyl-L-cysteine
-
wild type enzyme from hepatic cytosol
63.8
N-acetyl-S-carboxymethyl-L-cysteine
-
wild type enzyme from Hep-G2 cell cytosol
0.049
phenylalanine
-
phenylalanine-activated recombinant enzyme, cofactor tetrahydrobiopterin
0.055
phenylalanine
-
recombinant enzyme, cofactor (7R)-5,6,7,8-tetrahydrobiopterin
4.6
S-carboxy-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
14.73
S-carboxy-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
0.0728
S-carboxymethyl-L-cysteine
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.14
S-carboxymethyl-L-cysteine
-
mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.143
S-carboxymethyl-L-cysteine
-
mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.146
S-carboxymethyl-L-cysteine
-
mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.15
S-carboxymethyl-L-cysteine
-
mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
0.155
S-carboxymethyl-L-cysteine
-
mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C
2 - 3
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant R261Q, Vmax: 15 micromol/min/mg, pH 6.8, 37°C
2.38
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: NO (nitric oxide) (0.01 mM), Vmax: 42.32 nmoles/min/mg, pH 6.8, 37°C
2.75
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: H2O2 (0.1 mM), Vmax: 36.5 nmoles/min/mg, pH 6.8, 37°C
3.2
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: HO (hydroxyl radical) (0.01 mM), Vmax: 36.5 nmoles/min/mg, pH 6.8, 37°C
4.1
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: ONOO- (peroxynitrite)(1 mM), Vmax: 41.27 nmoles/min/mg, pH 6.8, 37°C
4.38
S-carboxymethyl-L-cysteine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: NO (nitric oxide) (0.01 mM), Vmax: 500 nmoles/min/mg, pH 6.8, 37°C
4.62
S-carboxymethyl-L-cysteine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: H2O2 (0.1 mM), Vmax: 430 nmoles/min/mg, pH 6.8, 37°C
5.23
S-carboxymethyl-L-cysteine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: N-ethylmaleimide (50 mM), Vmax: 450 nmoles/min/mg, pH 6.8, 37°C
6.49
S-carboxymethyl-L-cysteine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: HO (hydroxyl radical) (0.01 mM), Vmax: 455 nmoles/min/mg, pH 6.8, 37°C
7.54
S-carboxymethyl-L-cysteine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: ONOO- (peroxynitrite)(1 mM), Vmax: 481 nmoles/min/mg, pH 6.8, 37°C
7.65
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: N-ethylmaleimide (50 mM), Vmax: 5.58 nmoles/min/mg, pH 6.8, 37°C
8
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/wild-type, Vmax: 114 micromol/min/mg, pH 6.8, 37°C
8.1
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: L-Phe (4 mM), Vmax: 0.07 nmoles/min/mg, pH 6.8, 37°C
8.3
S-carboxymethyl-L-cysteine
-
post-translational activation of human cDNA-expressed PAH, activator: lysophosphatidylcholine (5 mM), Vmax: 4.38 nmoles/min/mg, pH 6.8, 37°C
15
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant I65T, Vmax: 18 micromol/min/mg, pH 6.8, 37°C
16.53
S-carboxymethyl-L-cysteine
-
in pooled hepatic cytosolic enzyme fraction activated with 1 mM lysophosphatidylcholine, at 37°C
16.53
S-carboxymethyl-L-cysteine
-
post-translational activation of PAH in human hepatic cytosol fractions, activator: L-Phe (4 mM), Vmax: 0.87 nmoles/min/mg, pH 6.8, 37°C; post-translational activation of PAH in human hepatic cytosol fractions, activator: lysophosphatidylcholine (5 mM), Vmax: 52.31 nmoles/min/mg, pH 6.8, 37°C
18
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant R68S, Vmax: 17 micromol/min/mg, pH 6.8, 37°C
19
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant I174T, Vmax: 2 micromol/min/mg, pH 6.8, 37°C
20
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant R158Q, Vmax: 3 micromol/min/mg, pH 6.8, 37°C
21
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant R408W, Vmax: 2 micromol/min/mg, pH 6.8, 37°C
24
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant Y414C, Vmax: 22 micromol/min/mg, pH 6.8, 37°C
25
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant V388M, Vmax: 12 micromol/min/mg, pH 6.8, 37°C
0.45
S-methyl-ergothionine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
43.25
S-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
0.025
tetrahydrobiopterin
-
cleaved maltose-binding-protein phenylalanine fusion protein
0.03 - 0.04
tetrahydrobiopterin
-
recombinant wild-type, C237S and C237D mutant enzyme
0.031
tetrahydrobiopterin
-
maltose-binding-protein phenylalanine fusion protein
0.041
tetrahydrobiopterin
-
truncated enzyme containing C-terminal 334 amino acids
1.7
thienylalanine
-
cofactor tetrahydrobiopterin, lysolecithin activated enzyme
0.024
tryptophan
-
truncated enzyme containing C-terminal 334 amino acids, pH 8.0
0.096
tryptophan
-
truncated enzyme containing C-terminal 334 amino acids, pH 7.0
additional information
L-phenylalanine
-
wild-type, pH 7.3, 25°C, measurement by standard discontinuous PAH activity assay (HPLC and fluorimetric detection): Vmax: 0.495 micromol L-Tyr/min/mg (without L-Phe preincubation), 1.55 micromol L-Tyr/min/mg (with L-Phe preincubation), S0.5: 0.318 mM (without L-Phe preincubation), S0.5: 0.154 mM (with L-Phe preincubation)
additional information
additional information
-
kinetics, molecular dynamics simulations, structure-energetics calculations, and molecular interaction fields, overview
-
additional information
additional information
-
thermodynamics of iron nitrosyl formation
-
additional information
additional information
-
binding constants for Fe2+ of wild-type and mutant enzymes, overview
-
additional information
additional information
Q9XYQ5
kinetic analysis
-
additional information
additional information
-
thermodynamics, overview
-
additional information
additional information
-
kinetic and molecular modelling of sulfur-containing substrates, overview
-
additional information
additional information
-
kinetic and molecular modelling of sulfur-containing substrates, overview
-
additional information
additional information
-
[S]0.5 (L-phenylalanine): 0.188 mM wild-type,0,109 mM mutant Q215K/N216Y, Vmax (wild-type): 1.9 micromol L-Tyr/min/mg, Vmax (mutant Q215K/N216Y): 6.6 micromol L-Tyr/min/mg, pH 7.0, 25°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
6-methyltetrahydropterin
-
wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
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
-
0.2
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5); wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.57
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.6
5,6,7,8-tetrahydrobiopterin
-
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.9
6,7-dimethyltetrahydropterin
-
mutant enzyme I234D, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
1.4
6,7-dimethyltetrahydropterin
-
wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
0.031 - 0.51
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH
1.12
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH V379D
7.85
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH
0.04 - 1.97
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH
0.18
L-phenylalanine
-
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.3
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH V379D
0.57
L-phenylalanine
-
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
1.93
L-phenylalanine
-
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
4.9
L-phenylalanine
-
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
5.83
L-phenylalanine
-
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
6.62
L-phenylalanine
-
wild type enzyme, without preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C
8.55
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH
8.81
L-phenylalanine
-
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
8.93
L-phenylalanine
-
wild type enzyme, 5 min preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C
10.9
L-phenylalanine
-
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
18
L-phenylalanine
-
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
21.5
L-phenylalanine
-
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.4
L-tryptophan
-
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.51
L-tryptophan
-
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
1.02
L-tryptophan
-
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
2.08
L-tryptophan
-
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.135
phenylalanine
-
Ser2-Gln428 deletion mutant, L-phenylalanine activated, dimeric form
0.165
phenylalanine
-
Ser2-Gln428 deletion mutant, lysophosphatidylcholine activated, dimeric form
0.233
phenylalanine
-
Ser2-Gln428 deletion mutant, lysophosphatidylcholine and phenylalanine activated, dimeric form
0.45
phenylalanine
-
Asp112-Lys452 deletion mutant, lysophosphatidylcholine activated, tetrameric form
0.667
phenylalanine
-
Gly103-Gln428 deletion mutant, lysophosphatidylcholine activated, dimeric form
0.877
phenylalanine
-
recombinant enzyme, lysophosphatidylcholine activated, tetrameric form
1.05
phenylalanine
-
Asp112-Lys452 deletion mutant, L-phenylalanine activated, tetrameric form; Asp112-Lys452 deletion mutant, lysophosphatidylcholine and phenylalanine activated, tetrameric form
1.24
phenylalanine
-
Gly103-Gln428 deletion mutant, lysophosphatidylcholine and phenylalanine activated, dimeric form
1.3
phenylalanine
-
recombinant enzyme, L-phenylalanine activated, tetrameric form
1.33
phenylalanine
-
Gly103-Gln428 deletion mutant, L-phenylalanine activated, dimeric form
1.59
phenylalanine
-
recombinant enzyme, lysophosphatidylcholine and phenylalanine activated, tetrameric form
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
mutant enzyme D139N, at pH 7.4 and 20°C
5.1
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
mutant enzyme D139N, at pH 7.4 and 20°C
9.4
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
mutant enzyme D139N, at pH 7.4 and 20°C
130
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
wild type enzyme, at pH 7.4 and 20°C
5.6
L-phenylalanine
-
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
14
L-phenylalanine
-
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
25
L-phenylalanine
-
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
32
L-phenylalanine
-
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
48
L-phenylalanine
-
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023 - 0.0049
7(S)-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant enzyme, versus (6R)-tetrahydrobiopterin
17.23
S-carboxymethyl-L-cysteine
-
in pooled hepatic cytosolic enzyme fraction, at 37°C
5.01
S-carboxy-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
13.14
S-carboxy-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
0.5
S-methyl-ergothionine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
41.53
S-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00009
-
activity in liver of males living in an area with high emissions of SO2 and nitrogen oxides, cofactor tetrahydrobiopterin
0.0014
-
mutant enzyme I65T, using S-carboxymethyl-L-cysteine as substrate; mutant enzyme R68S, using S-carboxymethyl-L-cysteine as substrate
0.006
-
activity in liver of males, 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
0.23
0.247
-
activity in liver of males, cofactor 6,7-dimethyltetrahydropterin
0.307
-
mutant enzyme W180F, at 30°C, using L-phenylalanine as substrate
0.342
-
mutant enzyme W180F, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
0.347
-
wild type enzyme, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
0.424
-
maltose-binding-protein phenylalanine hydroxylase fusion protein, dimeric form
0.75
-
mutant enzyme R408W, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.893
-
mutant enzyme W180F, at 30°C, using L-tryptophan as substrate
1
-
mutant enzyme L101Y, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate; mutant enzyme L101Y/W180F, at 30°C, using L-phenylalanine as substrate
1.05
-
mutant enzyme L101Y/W180F, at 30°C, using 5,6,7,8-tetrahydrobiopterin 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 25°C