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(S)-butyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
low activity
-
?
(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)-ethyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
low activity
-
?
(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
low activity
-
?
(S)-propyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
low activity
-
?
2-fluorophenylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
3-(2-thienyl)-L-alanine + 6-methyltetrahydropterin + O2
? + 6-methyldihydropterin + H2O
-
-
-
?
3-(2-thienyl)-L-alanine + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
-
-
?
3-fluorophenylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
3-phenylserine + tetrahydrobiopterin + O2
?
4-chlorophenylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
4-fluorophenylalanine + tetrahydrobiopterin + O2
?
4-methyl-L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
-
-
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
Abz-VAA + tetrahydrobiopterin + O2
?
-
-
-
r
beta-2-thienylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
L-methionine + 5,6,7,8-tetrahydrobiopterin + O2
?
L-methionine + tetrahydrobiopterin + O2
?
-
lysolecithin activated enzyme
-
?
L-norleucine + tetrahydrobiopterin + O2
?
-
lysolecithin activated enzyme
-
?
L-norleucine + tetrahydrobiopterin + O2
? + dihydrobiopterin + H2O
5% of the activity with 3-(2-thienyl)-L-alanine
-
?
L-Phe + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
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
-
-
?
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 + (7R)-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
r
L-phenylalanine + (7R,S)-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
r
L-phenylalanine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
?
-
-
-
r
L-phenylalanine + 5,6,7,8-tetrahydro-L-biopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
?
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
-
-
?
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydropterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
?
L-phenylalanine + 6,7-dimethyl-tetrahydrobiopterin + O2
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
-
-
-
?
L-phenylalanine + 6,7-dimethyltetrahydrobiopterin
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
L-phenylalanine + 6,7-dimethyltetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
-
-
-
?
L-phenylalanine + 6-methyl-tetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4-hydroxy-tetrahydrobiopterin
-
-
-
?
L-phenylalanine + 6-methyl-tetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4a-hydroxy-tetrahydrobiopterin
-
-
?
L-phenylalanine + 6-methyltetrahydrobiopterin + O2
L-tyrosine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
2-amino-4a-hydroxy-7-methyl-5,6,7,8-tetrahydropteridin-4(4aH)-one + H2O + ?
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
?
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-phenylalanine + 6-methyldihydropterin + H2O2
-
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
-
low activity with 6-methyltetrahydropterin
-
?
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-hydroxytetrahydrobiopterin
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
L-thienylalanine + tetrahydrobiopterin + O2
?
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
L-tryptophan + tetrahydrobiopterin + O2
5-hydroxytryptophan + 4a-hydroxytetrahydrobiopterin
L-tryptophan + tetrahydrobiopterin + O2
?
m-tyrosine + tetrahydrobiopterin + O2
?
-
-
-
?
N-acetyl-(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
N-acetyl-(S)-carboxymethyl-L-cysteine S-oxide + ?
-
-
?
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 + ?
-
-
?
N-acetyl-(S)-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
-
?
N-acetyl-S-carboxymethyl-L-cysteine + O2
?
N-acetyl-S-methyl-L-cysteine + O2
?
p-methylphenylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
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
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
-
?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
S-methyl-ergothionine + 5,6,7,8-tetrahydrobiopterin + O2
?
S-methyl-L-cysteine + 5,6,7,8-tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
S-methyl-L-cysteine + O2
?
S-methyl-L-cysteine + tetrahydrobiopterin + O2
?
-
lysolecithin activated enzyme
-
?
S-methyl-L-cysteine + tetrahydrobiopterin + O2
S-methyl-L-cysteine S-oxide + dihydrobiopterin + H2O
thienylalanine + tetrahydrobiopterin
?
-
-
-
r
additional information
?
-
3-phenylserine + tetrahydrobiopterin + O2

?
-
-
-
?
3-phenylserine + tetrahydrobiopterin + O2
?
-
-
-
?
4-fluorophenylalanine + tetrahydrobiopterin + O2

?
-
-
-
?
4-fluorophenylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2

4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
-
-
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
-
-
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
-
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-methionine + 5,6,7,8-tetrahydrobiopterin + O2

?
-
-
-
?
L-methionine + 5,6,7,8-tetrahydrobiopterin + O2
?
low activity
-
?
L-methionine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
-
-
?
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
-
-
?
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
-
-
-
?
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 + 6,7-dimethyltetrahydrobiopterin

L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
-
-
-
r
L-phenylalanine + 6,7-dimethyltetrahydrobiopterin
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
-
-
-
r
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
-
-
?
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
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
Q9XYQ5
-
-
?
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
-
-
?
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
-
-
684389, 684443, 684445, 686957, 688016, 688143, 688178, 689019, 726815, 728775, 745105, 746412 -
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
ir
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
-
-
-
?
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
-
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
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
-
-
-
?
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
-
-
?
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-thienylalanine + tetrahydrobiopterin + O2

?
-
-
-
?
L-thienylalanine + tetrahydrobiopterin + O2
?
-
-
-
?
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
-
?
L-tryptophan + tetrahydrobiopterin + O2
?
-
-
-
?
N-acetyl-S-carboxymethyl-L-cysteine + O2

?
-
-
?
N-acetyl-S-carboxymethyl-L-cysteine + O2
?
-
-
-
?
N-acetyl-S-methyl-L-cysteine + O2

?
-
-
?
N-acetyl-S-methyl-L-cysteine + O2
?
-
-
-
?
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-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
-
-
?
S-methyl-ergothionine + 5,6,7,8-tetrahydrobiopterin + O2

?
-
-
-
?
S-methyl-ergothionine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
-
-
?
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 + O2

?
-
-
?
S-methyl-L-cysteine + O2
?
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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 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
?
-
-
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.
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
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
L-phenylalanine + 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
additional information
?
-
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
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
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
-
-
-
?
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
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additional information
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hyperphenylalaninemia comprises a group of autosomal recessive disorders mainly caused by phenylalanine hydroxylase gene mutations
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additional information
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hyperphenylalaninemia is a group of autosomal recessive disorders caused by a wide range of PAH gene variants
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additional information
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hyperphenylalaninemia is a group of autosomal recessive disorders caused by a wide range of PAH gene variants
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additional information
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the enzyme is important in the metabolism of xenobiotic thioether substrates, overview
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additional information
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the enzyme is important in the metabolism of xenobiotic thioether substrates, overview
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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
0.0024
L-cyclohexylalanine
-
-
0.022 - 500
L-phenylalanine
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
additional information
L-phenylalanine
0.003
(6R)-5,6,7,8-tetrahydrobiopterin

-
recombinant enzyme
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
0.001
5,6,7,8-tetrahydrobiopterin

-
using L-phenylalanine as cosubstrate
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
0.065
6,7-dimethyltetrahydrobiopterin

-
native liver enzyme
0.065
6,7-dimethyltetrahydrobiopterin
-
native enzyme, at pH 6.8 and 25°C
0.105
6,7-dimethyltetrahydrobiopterin
-
chymotrypsin activated liver enzyme
0.105
6,7-dimethyltetrahydrobiopterin
-
chymotrypsin-activated enzyme, at pH 6.8 and 25°C
0.033
6,7-dimethyltetrahydropterin

-
-
0.05 - 0.06
6,7-dimethyltetrahydropterin
-
-
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, wild-type enzyme
0.43
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant E330H
0.43
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant H285E
1.2
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant H290Q
1.6
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant E330Q
3.4
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant H290E
6.9
6-methyltetrahydrobiopterin
-
pH 7.0, 25°C, mutant H285Q
0.01 - 0.015
6-methyltetrahydropterin

-
-
0.043
6-methyltetrahydropterin
-
using L-phenylalanine as cosubstrate
0.045
6-methyltetrahydropterin
-
-
0.045
6-methyltetrahydropterin
-
recombinant enzyme
0.045
6-methyltetrahydropterin
-
substrate phenylalanine
0.045
6-methyltetrahydropterin
-
native liver enzyme
0.061
6-methyltetrahydropterin
-
recombinant enzyme
0.073
6-methyltetrahydropterin
-
maltose-binding-protein phenylalanine fusion protein
0.085
6-methyltetrahydropterin
-
truncated enzyme containing C-terminal 334 amino acids
0.087
6-methyltetrahydropterin
-
chymotrypsin activated liver enzyme
0.088
6-methyltetrahydropterin
-
recombinant enzyme
0.09
6-methyltetrahydropterin
-
-
0.1
6-methyltetrahydropterin
-
recombinant enzyme
0.008
Abz-VAA

-
mutant Y325L, 25°C, pH 7.0
0.008
Abz-VAA
-
mutant enzyme Y325L, 25°C, pH 7.0
0.027
Abz-VAA
-
mutant Y325F, 25°C, pH 7.0
0.027
Abz-VAA
-
mutant enzyme Y325F, 25°C, pH 7.0
0.028
Abz-VAA
-
wild-type, 25°C, pH 7.0
0.028
Abz-VAA
-
wild type enzyme, 25°C, pH 7.0
3.1
L-methionine

-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
7.75
L-methionine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
0.1
L-Phe

-
allelic combination wild-type/mutant I65T, Vmax: 1 micromol/min/mg, pH 6.8, 37°C
0.1
L-Phe
-
allelic combination wild-type/mutant R68S, Vmax: 1 micromol/min/mg, pH 6.8, 37°C
0.1
L-Phe
-
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
0.43
L-Phe
-
pH 7.0, 25°C, wild-type enzyme
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
1
L-Phe
-
allelic combination wild-type/mutant R261Q, Vmax: 0.9 micromol/min/mg, pH 6.8, 37°C
1.2
L-Phe
-
pH 7.0, 25°C, mutant H290Q
1.6
L-Phe
-
pH 7.0, 25°C, mutant E330Q
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
3.4
L-Phe
-
pH 7.0, 25°C, mutant H290E
6.9
L-Phe
-
pH 7.0, 25°C, mutant H285Q
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
-
using 5,6,7,8-tetrahydrobiopterin as cofactor
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
0.05 - 0.075
L-phenylalanine
-
recombinant enzyme, cofactor tetrahydrobiopterin
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
0.12
L-phenylalanine
-
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
0.137
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
0.138
L-phenylalanine
-
cofactor tetrahydrobiopterin
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
0.14
L-phenylalanine
-
post-translational activation of human cDNA-expressed PAH, activator: L-Phe (4 mM), Vmax: 1.86 nmoles/min/mg, pH 6.8, 37°C
0.145
L-phenylalanine
-
truncated enzyme containing C-terminal 334 amino acids
0.16
L-phenylalanine
-
in pooled hepatic cytosolic enzyme fraction activated with 1 mM lysophosphatidylcholine, at 37°C
0.175
L-phenylalanine
-
cofactor tetrahydrobiopterin, recombinant enzyme
0.194
L-phenylalanine
-
cofactor tetrahydrobiopterin, maltose-binding-protein phenylalanine fusion protein
0.225
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
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
0.244
L-phenylalanine
wild type enzyme, at pH 7.4 and 20°C
0.25
L-phenylalanine
-
using 6-methyltetrahydropterin as cofactor
0.253
L-phenylalanine
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.26
L-phenylalanine
-
pH 6.8, 37°C
0.26
L-phenylalanine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
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
0.316
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
0.318
L-phenylalanine
-
-
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)
0.329
L-phenylalanine
-
recombinant enzyme
0.382
L-phenylalanine
-
cofactor 6-methyltetrahydropterin, recombinant enzyme
0.393
L-phenylalanine
-
cofactor 6-methyltetrahydropterin
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
0.64
L-phenylalanine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
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
0.735
L-phenylalanine
-
in 100 mM Na-HEPES, pH 7.0 at 37°C
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
-
in pooled hepatic cytosolic enzyme fraction, at 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
500
L-phenylalanine
-
mutant enzyme R270K, at pH 7.0 and 25°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)
4.9
L-tryptophan
-
cofactor 2-amino-4-hydroxy-6-methyltetrahydropteridine
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
58.92
N-acetyl-S-methyl-L-cysteine

-
wild type enzyme from hepatic cytosol
60.54
N-acetyl-S-methyl-L-cysteine
wild type enzyme from hepatic cytosol
68.25
N-acetyl-S-methyl-L-cysteine
wild type enzyme from Hep-G2 cell cytosol
0.043
phenylalanine

-
recombinant enzyme, cofactor (6R)-methyltetrahydropterin
0.049
phenylalanine
-
phenylalanine-activated recombinant enzyme, cofactor tetrahydrobiopterin
0.05
phenylalanine
-
cofactor tetrahydrobiopterin
0.05
phenylalanine
-
recombinant enzyme, cofactor tetrahydrobiopterin
0.055
phenylalanine
-
recombinant enzyme, cofactor (7R)-5,6,7,8-tetrahydrobiopterin
0.17
phenylalanine
-
cofactor 6-methyltetrahydropterin, recombinant enzyme
0.18
phenylalanine
-
cofactor 6-methyltetrahydropterin
0.183
phenylalanine
-
S16E mutant enzyme
0.187
phenylalanine
-
phosphorylated recombinant wild-type enzyme
0.2
phenylalanine
-
recombinant wild-type enzyme
0.2
phenylalanine
-
cofactor tetrahydrobiopterin
0.217
phenylalanine
-
S16Q mutant enzyme
0.254
phenylalanine
-
S16K mutant enzyme
0.266
phenylalanine
-
S16D mutant enzyme
0.287
phenylalanine
-
S16N mutant enzyme
0.288
phenylalanine
-
S16A mutant enzyme
0.55
phenylalanine
-
cofactor dimethyltetrahydropterin
1.3
phenylalanine
-
cofactor 6,7-dimethyltetrahydrobiopterin
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
14.73
S-carboxymethyl-L-cysteine
-
pH 6.8, 37°C
14.73
S-carboxymethyl-L-cysteine
-
wild type enzyme from hepatic cytosol
15
S-carboxymethyl-L-cysteine
-
allelic combination wild-type/mutant I65T, Vmax: 18 micromol/min/mg, pH 6.8, 37°C
16.22
S-carboxymethyl-L-cysteine
-
-
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
wild type enzyme from hepatic cytosol
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
16.53
S-carboxymethyl-L-cysteine
-
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
25.24
S-carboxymethyl-L-cysteine
-
-
25.24
S-carboxymethyl-L-cysteine
wild type enzyme from Hep-G2 cell cytosol
0.3
S-methyl-ergothionine

-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
0.45
S-methyl-ergothionine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
18.32
S-methyl-L-cysteine

-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
43.25
S-methyl-L-cysteine
-
pH 6.8, 37°C
43.25
S-methyl-L-cysteine
-
at 37°C, 50 mM potassium phosphate buffer, pH 6.8
43.25
S-methyl-L-cysteine
-
wild type enzyme from hepatic cytosol
44.63
S-methyl-L-cysteine
wild type enzyme from hepatic cytosol
51.6
S-methyl-L-cysteine
wild type enzyme from Hep-G2 cell cytosol
0.002
tetrahydrobiopterin

-
native liver enzyme
0.002 - 0.004
tetrahydrobiopterin
-
-
0.0025
tetrahydrobiopterin
-
S16A mutant enzyme
0.0026
tetrahydrobiopterin
-
-
0.0027
tetrahydrobiopterin
-
S16K mutant enzyme
0.0028
tetrahydrobiopterin
-
S16D mutant enzyme
0.0034
tetrahydrobiopterin
-
S16E mutant enzyme
0.0036
tetrahydrobiopterin
-
S16N mutant enzyme
0.0044
tetrahydrobiopterin
-
S16Q mutant enzyme
0.0046
tetrahydrobiopterin
-
phosphorylated recombinant wild-type enzyme
0.00936
tetrahydrobiopterin
-
pH 6.8, 37°C, cosubstrate L-phenylalanine
0.01 - 0.015
tetrahydrobiopterin
-
substrate phenylalanine
0.012
tetrahydrobiopterin
-
chymotrypsin activated liver enzyme
0.014
tetrahydrobiopterin
-
mutant C237R
0.016
tetrahydrobiopterin
-
recombinant enzyme
0.021
tetrahydrobiopterin
-
recombinant wild-type enzyme, dimeric form
0.022
tetrahydrobiopterin
-
-
0.023
tetrahydrobiopterin
-
native liver enzyme in crude extract
0.025
tetrahydrobiopterin
-
recombinant wild-type enzyme
0.025
tetrahydrobiopterin
-
cleaved maltose-binding-protein phenylalanine fusion protein
0.025
tetrahydrobiopterin
-
recombinant wild-type enzyme, tetrameric form
0.029
tetrahydrobiopterin
-
recombinant enzyme
0.03 - 0.04
tetrahydrobiopterin
-
recombinant wild-type, C237S and C237D mutant enzyme
0.031
tetrahydrobiopterin
-
maltose-binding-protein phenylalanine fusion protein
0.031
tetrahydrobiopterin
-
Gly103-Gln428 deletion mutant, dimeric form
0.032
tetrahydrobiopterin
-
Ser2-Gln428 deletion mutant, dimeric form
0.032
tetrahydrobiopterin
mutant enzyme Y138E, at pH 7.0 and 25°C
0.034
tetrahydrobiopterin
-
Asp112-Lys452 deletion mutant, tetrameric form
0.034
tetrahydrobiopterin
-
mutant C237A
0.034
tetrahydrobiopterin
-
mutant C237D
0.035
tetrahydrobiopterin
Q9XYQ5
-
0.035
tetrahydrobiopterin
-
wild-type
0.035
tetrahydrobiopterin
mutant enzyme Y138F, at pH 7.0 and 25°C
0.037
tetrahydrobiopterin
-
mutant R68A
0.037
tetrahydrobiopterin
-
mutant R68V
0.039
tetrahydrobiopterin
wild type enzyme, at pH 7.0 and 25°C
0.041
tetrahydrobiopterin
-
truncated enzyme containing C-terminal 334 amino acids
0.044
tetrahydrobiopterin
mutant enzyme Y138K, at pH 7.0 and 25°C
0.047
tetrahydrobiopterin
mutant enzyme Y138A, at pH 7.0 and 25°C
0.053
tetrahydrobiopterin
-
recombinant enzyme
0.082
tetrahydrobiopterin
-
V388M mutant enzyme
0.125
tetrahydrobiopterin
-
in 100 mM Na-HEPES, pH 7.0 at 37°C
0.3
tetrahydrobiopterin
-
pH 7.0, 10°C, recombinant enzyme
0.5
tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant enzyme
0.47
thienylalanine

-
native enzyme
0.47
thienylalanine
-
native enzyme, cofactor tetrahydrobiopterin
1.7
thienylalanine
-
cofactor tetrahydrobiopterin, lysolecithin activated enzyme
1.7
thienylalanine
-
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
Q9XYQ5
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
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
thermodynamics, overview
-
additional information
additional information
-
binding constants for Fe2+ of wild-type and mutant enzymes, 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
-
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