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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
?
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 2-amino-4a-hydroxy-7-methyl-5,6,7,8-tetrahydropteridin-4(4aH)-one
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
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 + 4a-hydroxy-6-methyltetrahydropterin
-
-
in the presence of FeSO4 and dithiothreitol
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
-
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
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
-
low activity with 6-methyltetrahydropterin
-
-
?
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
-
-
?
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
?
-
-
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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0.00009
-
activity in liver of males living in an area with high emissions of SO2 and nitrogen oxides, cofactor tetrahydrobiopterin
0.00033
-
activity in liver of males, cofactor tetrahydrobiopterin
0.0009
mutant enzyme V388M, using S-carboxymethyl-L-cysteine as substrate
0.00097
-
activity in liver of males, cofactor tetrahydrobiopterin
0.0015
mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as substrate
0.0016
mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as substrate
0.0049
L-phenylalanine-activated mutant enzyme S231F, at 25°C
0.0052
non-L-phenylalanine-activated mutant enzyme S231F, at 25°C
0.006
-
activity in liver of males, cofactor 6,7-dimethyltetrahydropterin
0.055
-
I65T mutant enzyme, cofactor 6-methyltetrahydropterin
0.073
wild type enzyme, using S-carboxymethyl-L-cysteine as substrate
0.09
-
cofactor 6,7-dimethyltetrahydropterin
0.099
R270K mutant enzyme, expression in the absence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
0.105
-
activity in liver of males living in an area with high emissions of SO2 and nitrogen oxides, cofactor 6,7-dimethyltetrahydropterin
0.17
-
cofactor 6-methyltetrahydropterin
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
0.408
-
V388M mutant enzyme, cofactor tetrahydrobiopterin
0.4169
non-L-phenylalanine-activated wild type enzyme, at 25°C
0.424
-
maltose-binding-protein phenylalanine hydroxylase fusion protein, dimeric form
0.505
mutant enzyme V388M, using L-phenylalanine as substrate
0.536
-
R261Q mutant enzyme, cofactor tetrahydrobiopterin
0.69
wild type enzyme, at 30°C, using L-tryptophan as substrate
0.7418
L-phenylalanine-activated wild type enzyme, at 25°C
0.745
-
V388M mutant enzyme, cofactor 6-methyltetrahydropterin
0.75
mutant enzyme R408W, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
0.77
-
mutant R68V, preincubation with L-phenylalanine
0.78
-
R261Q mutant enzyme, cofactor 6-methyltetrahydropterin
0.893
mutant enzyme W180F, at 30°C, using L-tryptophan as substrate
1.05
mutant enzyme L101Y/W180F, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
1.1
-
wild-type, preincubation with L-phenylalanine
1.13
-
mutant C237R, preincubation with L-phenylalanine
1.2
mutant enzyme Y414C, using L-phenylalanine as substrate
1.283
-
maltose-binding-protein phenylalanine hydroxylase fusion protein, tetrameric form
1.32
mutant enzyme R155H, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
1.49
mutant enzyme R261Q, using L-phenylalanine as substrate
1.64
mutant enzyme D143G, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
1.7
-
pH 7.0, 25°C, wild-type, dimer
1.725
mutant enzyme R68S, using L-phenylalanine as substrate
1.742
-
recombinant wild-type enzyme, cofactor tetrahydrobiopterin
1.76
-
adult liver enzyme
1.77
mutant enzyme L101Y, at 30°C, using L-tryptophan as substrate
1.773
V388M mutant enzyme, expression in the absence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
1.9
wild type enzyme, using L-phenylalanine as substrate
1.98
substrate L-phenylalanine, mutant N223D
10.16
mutant enzyme L101Y, at 30°C, using L-phenylalanine as substrate
10.2
-
in 100 mM Na-HEPES, pH 7.0 at 37°C
1150
-
mutant Y325F, 25°C, pH 7.0
1230
-
wild-type, 25°C, pH 7.0
1310
-
mutant Y325L, 25°C, pH 7.0
14
-
truncated enzyme containing C-terminal 334 amino acids
1500
-
mutant Y325L, preincubation with L-phenylalanine, 25°C, pH 7.0
2.1
-
micromol L-Tyr/min/mg, wild-type, pH 7.0, 25°C, without L-Phe preincubated enzyme
2.2
-
mutant R68A, preincubation with L-phenylalanine
2.25
mutant enzyme I65T, using L-phenylalanine as substrate
2.34
substrate tetrahydrobiopterin, mutant N223D
2.49
-
recombinant wild-type enzyme, cofactor 6-methyltetrahydropterin
2.76
mutant enzyme L348V, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
2.84
substrate tetrahydrobiopterin, mutant T427P
2.91
V388M mutant enzyme, expression in the presence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
2.98
wild type enzyme, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
290
-
mutant Y325A, 25°C, pH 7.0
3.17
substrate L-phenylalanine, mutant T427P
3.32
mutant enzyme P416Q, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C
3.37
wild type enzyme, at 30°C, using L-phenylalanine as substrate
3.48
substrate L-phenylalanine, wild-type
3.62
mutant enzyme L101Y/W180F, at 30°C, using L-tryptophan as substrate
3.67
substrate L-phenylalanine, mutant N426D
3.74
substrate L-phenylalanine, mutant N32D
300
-
mutant Y325A, preincubation with L-phenylalanine, 25°C, pH 7.0
3630
-
mutant Y325F, preincubation with L-phenylalanine, 25°C, pH 7.0
3640
-
wild-type, preincubation with L-phenylalanine, 25°C, pH 7.0
4.19
-
mutant C237D, preincubation with L-phenylalanine
4.37
substrate L-phenylalanine, mutant G33A
4.39
substrate tetrahydrobiopterin, mutant N426D
4.95
-
pH 7.0, 25°C, wild-type, tetramer
5
-
phosphorylated recombinant wild-type enzyme, S16N and S16D mutant enzyme
5.1
-
S16A and S16K mutant enzymes
5.16
substrate L-phenylalanine, mutant G33V
5.2
-
S16E and S16Q mutant enzyme
5.32
substrate tetrahydrobiopterin, wild-type
6.19
substrate L-phenylalanine, mutant K113P
6.41
substrate tetrahydrobiopterin, mutant G33V
6.48
-
pH 7.0, 25°C, N-terminal deletion mutant
6.5
-
micromol L-Tyr/min/mg, mutant Q215K/N216Y, pH 7.0, 25°C, with L-Phe preincubated enzyme
8.32
-
pH 7.0, 25°C, N-terminal plus C-terminal deletion mutant
8.56
substrate tetrahydrobiopterin, mutant K113P
0.0014
mutant enzyme I65T, using S-carboxymethyl-L-cysteine as substrate
0.0014
mutant enzyme R68S, using S-carboxymethyl-L-cysteine as substrate
0.23
-
cofactor tetrahydrobiopterin
0.23
R270K mutant enzyme, expression in the presence of glycerol in the growth medium, cofactor 6-methyltetrahydropterin
1
mutant enzyme L101Y, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
1
mutant enzyme L101Y/W180F, at 30°C, using L-phenylalanine as substrate
1.46
-
-
2.22
-
mutant C237A, preincubation with L-phenylalanine
2.22
-
pH 7.0, 25°C, C-terminal deletion mutant
2.6
-
micromol L-Tyr/min/mg, wild-type, pH 7.0, 25°C, with L-Phe preincubated enzyme
4.73
substrate tetrahydrobiopterin, mutant G33A
4.73
substrate tetrahydrobiopterin, mutant N32D
4.9
-
micromol L-Tyr/min/mg, mutant Q215K/N216Y, pH 7.0, 25°C, with L-Phe preincubated enzyme
4.9
-
recombinant wild-type enzyme
additional information
-
Hill coefficient of wild-type tetramer, substrate L-phenylalanine, 1.9, for wild-type dimer, 0.8, for N-terminal deletion mutant, 1.1, for C-terminal deletion mutant, 1.1
additional information
-
phenlyalanine level determination by the phenylalanine breath test, overview
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Q215K/N216Y
-
humanized mutant Q215K/N216Y of cePAH binds 1.4 L-Phe/subunit. This mutant also displays high catalytic activity and certain positive cooperativity for L-Phe. Km for cofactor tetrahydrobiopterin higher compared to wild-type, [S]0.5 (L-Phe) lower compared to wild-type, Vmax (L-Phe) higher compared to wild-type
D139A
the catalytic efficiency for L-phenylalanine is 81fold lower than that of the wild type enzyme
D139E
the catalytic efficiency for L-phenylalanine is 7fold lower than that of the wild type enzyme
D139N
the catalytic efficiency for L-phenylalanine is 17fold lower than that of the wild type enzyme
F258A
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
G221A
the half-life of the mutant at 50°C is 16.8 min, which is increased by 0.9-times compared to the wild type enzyme
I234D
-
mutant shows decreased kcat value for 6,7-dimethyltetrahydropterin compared to the wild type enzyme
K94R
the half-life of the mutant at 50°C is 26.2 min, which is increased by 1.9-times compared to the wild type enzyme
K94R/G221A
the residual activity of the mutant is improved to 65.6% after keeping at 50°C for 1 h, which is 6.6 time higher than the wild type enzyme
L101A
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101C
the mutant shows 47% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101D
the mutant shows 5% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101E
the mutant shows 9% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101F
the mutant shows 133% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101G
the mutant shows 20% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101H
the mutant shows 16% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101I
the mutant shows 51% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101K
the mutant shows 29% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101M
the mutant shows 102% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101N
the mutant shows 15% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101P
the mutant shows 9% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101Q
the mutant shows 30% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101R
the mutant shows 29% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101S
the mutant shows 28% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101T
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101V
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101W
the mutant shows 55% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101Y
the mutant shows 153% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101Y/W180F
the double mutant displays higher L-tryptophan hydroxylation activity than the wild type enzyme with a 5.2fold increase in kcat
S230P
the mutant shows strongly decreased activity and a marked decrease in the affinity for L-phenylalanine
T254A
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
W180A
the mutant shows 66% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180C
the mutant shows 119% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180D
the mutant shows 3% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180E
the mutant shows 6% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180F
the mutant shows 204% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180G
the mutant shows 8% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180H
the mutant shows 73% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180I
the mutant shows 113% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180K
the mutant shows 4% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180L
the mutant shows 174% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180M
the mutant shows 166% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180N
the mutant shows 49% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180P
the mutant shows 15% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180Q
the mutant shows 17% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180R
the mutant shows 85% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180S
the mutant shows 46% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180T
the mutant shows 44% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180V
the mutant shows 155% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180Y
the mutant shows 115% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
Y155A
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
Y179A
-
stability and metal binding comparable to wild-type, kcat-value one order of magnitude lower than wild-type, KM-value of L-phenylalanine increases by 10-fold
Y179F
-
stability and metal binding comparable to wild-type, kcat-value one order of magnitude lower than wild-type
F258A
-
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
-
S230P
-
the mutant shows strongly decreased activity and a marked decrease in the affinity for L-phenylalanine
-
T254A
-
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
-
Y155A
-
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
-
L101A
-
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
-
L101F
-
the mutant shows 133% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
-
L101I
-
the mutant shows 51% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
-
L101W
-
the mutant shows 55% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
-
L101Y
-
the mutant shows 153% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
-
A202T
the mutation is associated with phenylketonuria
A259V
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
A309V
-
the mutant shows 70% of wild type activity
A322G
-
the mutant shows 75% of wild type activity
A395G
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
A434D
-
the mutation is associated with phenylketonuria
C237A
-
increase of basal activity and affinity for substrate L-phenylalanine
C237R
-
reduced activity, elimination of positive cooperativity
C237S
-
approx. 2fold higher activity than wild-type
D143G
mutant with a mild misfolding defect associated with phenylketonuria
D338Y
the mutation is associated with phenylketonuria
D415N
-
naturally occuring missense mutation causing a mild phenylketonuria phenotype
DELTA1-102
-
mutant lacking the first 102 residues corresponding to the N-terminal regulatory domain. 96% of the truncated mutant exist as a tetramer. On coexpression of wild-type-hPAH and the N-terminally truncated form DELTA1-102 (~95% tetramer), heterotetramers, as a result of an assembly of two different homodimers, are isolated. The recovered (wild-type)/(DELTA1-102 mutant)-hPAH heterotetramers reveal a catalytic activity deviating significantly from that calculated by averaging the respective recombinant homotetrameric forms. The heterotetramer assembly also results in conformational changes in the WT-hPAH protomer, as detected by trypsin limited proteolysis
DELTA1-102/DELTAC24
-
mutant lacking the first 102 residues corresponding to the N-terminal regulatory domain and the last 24 residues at the C-terminal end corresponding to the tetramerisation motif. 81% of the truncated mutant exist as a dimer and 17% as an aggregated form. On co-expression of wild-type-hPAH (50% tetramer, 10% dimer) and the N- and C-terminally truncated form DELTA1-102/DELTAC24 (80% dimer) no heterodimers is recovered
DELTA103-427
-
dimeric double-truncated form: the dimeric variant 103-427 shows a Vmax (1980 nmol Tyr/min/mg protein) comparable with that of the non-activated wild-type PAH, which does not change markedly upon L-Phe preincubation (2421 nmol Tyr/min/mg protein)
E178G/Q232E
the mutant shows 55% activity compared to the wild type enzyme
E221G
the mutation is associated with phenylketonuria
E280G
-
the mutation is associated with phenylketonuria
E390G/R261Q
the mutant shows 63% activity compared to the wild type enzyme
E76A
the mutation is associated with phenylketonuria
F331S
the mutant shows residual enzymatic activity in vitro compared to the wild type enzyme
F382L
naturally occuring mutation and site-directed mutagenesis, the mutant shows 44% reduced activity compared to the wild-type enzyme, analysis of structural alterations
F39C
the mutant enzyme shows reduced activity compared to the wild type
F39L/F55fsdelT
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and causes an atypical form of phenylketonuria
F39L/P281L
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and causes the classical form of phenylketonuria
F39L/R408W
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and causes the classical form of phenylketonuria
G103S
-
site-directed mutagenesis, the mutation occurs naturally in phenylketonuria patients from Korea, the mutant shows highly reduced activity compared to the wild-type
G218V
-
the mutant shows wild type activity
G247R
the mutation is associated with phenylketonuria
G332E
the mutation is associated with phenylketonuria
G332V
-
site-directed mutagenesis, the mutation occurs naturally in phenylketonuria patients from Korea, inactive mutant
G33A
increased basal activity, reduced activation by preincubation with substrate
G33V
increased basal activity, reduced activation by preincubation with substrate
G344D
the mutation is associated with phenylketonuria
H271Q
-
naturally occuring knockout missense mutation leading to a severe phenylketonuria phenotype
I174V
-
naturally occuring missense mutation causing a mild phenylketonuria phenotype
I224T
the mutation is associated with phenylketonuria
I306V
the mutation is associated with phenylketonuria
I65T/R261Q
the mutant shows 19.5% activity compared to the wild type enzyme
I65T/R68S
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and causes a mild form of phenylketonuria
I65V
the mutant enzyme shows reduced activity compared to the wild type
I95F
-
naturally occuring missense mutation causing a mild phenylketonuria phenotype
I97L
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and is involved in the disorder hyperphenylalaninemia
K113P
increased basal activity, reduced activation by preincubation with substrate, increase in positive cooperativity
K398K
naturally occuring mutation
K398N
naturally occuring mutation and site-directed mutagenesis, the mutant shows 45% reduced activity compared to the wild-type enzyme, analysis of structural alterations
K42I
-
the mutant shows 12% of wild type activity
L197F
-
naturally occuring knockout missense mutation leading to a severe phenylketonuria phenotype
L213P
the mutation is associated with phenylketonuria
L255V
-
the mutant shows 13% of wild type activity
L293M
-
site-directed mutagenesis, the mutation occurs naturally in phenylketonuria patients from Korea, the mutant shows reduced activity and no response to tetrahydrobiopterin compared to the wild-type
L358F
the mutant shows residual enzymatic activity in vitro compared to the wild type enzyme
L41F
-
the mutant shows 10% of wild type activity
L48S/R261Q
the mutant shows 35% activity compared to the wild type enzyme
N223D
low basal activity, little activation by preincubation with substrate, increase in positive cooperativity
N223Y
naturally occuring mutation and site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme, analysis of structural alterations
N32D
low basal activity, close to normal activation by preincubation with substrate
N426D
low basal activity, close to normal activation by preincubation with substrate
P122Q
-
the mutant with wild type activity exhibits less than 50% of wild type protein level
P244L
-
the mutant shows 68% of wild type activity
P281S
the mutation is associated with phenylketonuria
P366H
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
P384S
the mutant shows 76% activity compared to the wild type enzyme
P384S/R408W
the mutant shows 56.1% activity compared to the wild type enzyme
P416Q
the mutant retains significant catalytic activity yet is observed in classic and moderate phenylketonuria patients
P69S
-
site-directed mutagenesis, the mutation occurs naturally in phenylketonuria patients from Korea, the mutant shows reduced activity compared to the wild-type
Q232E
the mutant shows 42% activity compared to the wild type enzyme
Q232X
-
the mutation is associated with phenylketonuria
Q419R
naturally occuring mutation and site-directed mutagenesis, the mutant shows 29% reduced activity compared to the wild-type enzyme, analysis of structural alterations
R157N
-
the mutant with wild type activity exhibits less than 50% of wild type protein level
R158Q/R261Q
the mutant shows 23% activity compared to the wild type enzyme
R241H
the mutation is associated with phenylketonuria
R243X
exon 6 C727T mutation naturally occuring in phenylketonuria patients from the Cukurova region in Turkey, sequence determination and analysis
R252G
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
R252Q
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
R270S
-
the mutant shows 3% of wild type activity
R297C
naturally occuring mutation
R297H
naturally occuring mutation
R297L
naturally occuring mutation and site-directed mutagenesis, the mutant shows 58% reduced activity compared to the wild-type enzyme, analysis of structural alterations
R313P
-
the mutation is associated with phenylketonuria
R408W/A300S
the mutant shows 18% activity compared to the wild type enzyme
R408W/I283F
the mutant shows 2% residual activity compared to the wild type enzyme
R408W/I306V
the mutant shows 18% residual activity compared to the wild type enzyme
R408W/pA403V
the mutant shows 20% residual activity compared to the wild type enzyme
R408W/R261Q
the mutant shows 18% activity compared to the wild type enzyme
R408W/R297H
the mutant shows 15% residual activity compared to the wild type enzyme
R408W/Y414C
the mutant shows 40% activity compared to the wild type enzyme
R53H
-
site-directed mutagenesis, the mutation occurs naturally in humans altering the tetrahydrobiopterin responsiveness, the mutant shows reduced activity and dimer stability compared to the wild-type
R68A
-
increase of basal activity and affinity for substrate L-phenylalanine
R68G
-
the mutant shows wild type activity
R68S/R408W
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and causes an atypical form of phenylketonuria
R68V
-
little decrease in activity
R71C
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and is involved in the disorder hyperphenylalaninemia
R86S
-
for the variants R68S and V106A, a Vmax comparable with the activated wild-type PAH is found without L-Phe preincubation, and no further increase is measured when the substrate is present. R68S and V106A without L-Phe preincubation show lower cofactor affinities than the non-activated wild-type PAH. Values are at the same level as determined for the L-Phe preincubated wild-type PAH
S196Y
the mutant shows about 20% activity compared to the wild type enzyme
S231F
the missense phenylalanine hydroxylase gene mutation causes complete loss of enzymatic activity in vitro (residual enzyme activity in vitro is about 1%) as it drastically reduces stability and activity of the PAH enzyme, the mutant enzyme is not activated by pre-incubation with L-phenylalanine substrate
S310F
the mutation is associated with phenylketonuria
S348L
instable enzyme forming aggregates after expression in Escherichia coli in the presence of GroESL
S349A
the mutation is associated with phenylketonuria
S391I
-
site-directed mutagenesis, the mutation occurs naturally in phenylketonuria patients from Korea, inactive mutant
T278I
the mutation is associated with phenylketonuria
T380M
the mutant shows about 25% activity compared to the wild type enzyme
T63P
the mutation is associated with phenylketonuria
V106A
-
for the variants R68S and V106A, a Vmax comparable with the activated wild-type PAH is found without L-Phe preincubation, and no further increase is measured when the substrate is present. R68S and V106A without L-Phe preincubation show lower cofactor affinities than the non-activated wild-type PAH. Values are at the same level as determined for the L-Phe preincubated wild-type PAH
V245A
the mutant shows 50% activity compared to the wild type enzyme
V245A/R261Q
the mutant shows 55% activity compared to the wild type enzyme
V379D/H264Q
the mutant shows significant activity at tyrosine hydroxylation and a 3000fold decrease in preference for phenylalanine over tyrosine as the substrate
W187X
the mutation is associated with phenylketonuria
Y138A
the mutant shows reduced catalytic efficiency (about 38%) compared to the wild type enzyme
Y138E
the mutant shows reduced catalytic efficiency (about 15%) compared to the wild type enzyme
Y138F
the mutant shows reduced catalytic efficiency (about 55%) compared to the wild type enzyme
Y138K
the mutant shows severely reduced catalytic efficiency (about 5%) compared to the wild type enzyme
Y166X
-
the mutation is associated with phenylketonuria
Y168H
the mutation is associated with phenylketonuria
Y325L
-
stable, similar yields and oligomeric distribution as wild-type, reduced specific activity, decreased coupling efficiency and decreased iron content, no positive cooperativity for L-phenylalanine
Y325S
-
aggregation after purification, not suitable for characterization
Y386C
exon 11 A1157G mutation naturally occuring in phenylketonuria patient from the Cukurova region in Turkey, sequence determination and analysis
Y387H
the mutation is associated with phenylketonuria
Y414C/R261Q
the mutant shows 64% activity compared to the wild type enzyme
A322S/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
A47G
the mutation decreases the affinity of the catalytic domain for L-phenylalanine compared to the wild type
DELTA1-117
mutant lacking the first 117 amino acids containing only the catalytic and tetramerization domains: the effects of phenylalanine on the hydrogen/deuterium exchange kinetics are limited to peptides surrounding the binding site for the amino acid substrate
E280A
-
site-directed mutagenesis of catalytic core mutant DELTA117PheH, 70% reduced activity but unaltered isotopic effects of isotope substrates
E330H
-
site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme
E330Q
-
site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme
E44Q
the mutation decreases the affinity of the catalytic domain for L-phenylalanine compared to the wild type and leads to loss of activity
F263A
-
site-directed mutagenesis of catalytic core mutant DELTA117PheH, 85% reduced activity but unaltered isotopic effects of isotope substrates
H264Q
-
mutant of full length enzyme, no tyrosine hydroxylation activity
H285E
-
site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme
H285Q
-
site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows 80% reduced activity compared to the wild-type enzyme
H290E
-
site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme
H290Q
-
site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme
H64N
the mutation decreases the affinity of the catalytic domain for L-phenylalanine compared to the wild type
L293M
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
L48V
the mutation decreases the affinity of the catalytic domain for L-phenylalanine compared to the wild type
L62V
the mutation decreases the affinity of the catalytic domain for L-phenylalanine compared to the wild type and leads to loss of activity
S16A
-
similar Km for tetrahydrobiopterin and activity as wild-type
S16D
-
similar Km for tetrahydrobiopterin and activity as wild-type
S16E
-
slightly higher Km for tetrahydrobiopterin than wild-type, approx. 3fold higher Vmax with phenylalanine
S16K
-
similar Km for tetrahydrobiopterin and activity as wild-type
S16N
-
slightly higher Km for tetrahydrobiopterin than wild-type, approx. 3fold higher Vmax with phenylalanine
S16Q
-
slightly higher Km for tetrahydrobiopterin than wild-type, similar Vmax with phenylalanine
S251A
-
truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity
S251A/H264Q
-
truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity
S251A/H264Q/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
S251A/H264Q/Y277H
-
truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity
S251A/H264Q/Y277H/A322S
-
truncated enzyme containing the catalytic domain, no tyrosine hydroxylation activity
S251A/H264Q/Y277H/A322S/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
S251A/H264Q/Y277H/A322S/V379D/Y356H
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
S251A/H264Q/Y277H/A322S/V379D/Y356H/L293M
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
S251A/H264Q/Y277H/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
S251A/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
Y277H
-
mutant of full length enzyme, no tyrosine hydroxylation activity
Y277H/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
W179/L98Y
-
the mutant shows 46% activity with L-phenylalanine and 1207% activity with L-tryptophan compared to the wild type enzyme
W179F
-
the mutant shows 80% activity with L-phenylalanine and 1739% activity with L-tryptophan compared to the wild type enzyme
W179F/L98Y/Y231C
-
the mutant shows 17% activity with L-phenylalanine and 570% activity with L-tryptophan compared to the wild type enzyme
W179F/Y231C
-
the mutant shows 52% activity with L-phenylalanine and 952% activity with L-tryptophan compared to the wild type enzyme
A104D
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and is involved in the disorder hyperphenylalaninemia
A104D
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to mild phenyletonuria
A259T
the mutation is associated with phenylketonuria
A259T
-
the mutant with wild type activity exhibits less than 50% of wild type protein level
A300S
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
A300S
-
the mutation is associated with phenylketonuria
A300S
the mutation is associated with phenylketonuria
A300S
the mutant shows 31% activity compared to the wild type enzyme
A313T
the mutant displays 20-30% lower catalytic activity than the wild type enzyme
A313T
the mutation leads to thermodynamic stability change upon folding
A403V
-
frequent naturally occuring mutation involved in enzyme deficiency and BH4-responsive hyperphenylalaninemia and/or phenylketonuria
A403V
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
A403V
the mutation is associated with phenylketonuria
A403V
-
the mutant shows wild type activity
A403V
-
the mutation leads to mild phenyletonuria
A447P
-
site-directed mutagenesis, the mutation occurs naturally in phenylketonuria patients from Korea, the mutant shows highly reduced activity compared to the wild-type
A447P
the mutation is associated with phenylketonuria
C237D
-
approx. 3fold higher activity than wild-type
C237D
-
increase of basal activity and affinity for substrate L-phenylalanine
E178G
exon 6 A533G mutation naturally occuring in phenylketonuria patients from the Cukurova region in Turkey, sequence determination and analysis
E178G
the mutant shows 39% activity compared to the wild type enzyme
E280K
-
inactive
E280K
-
the mutation is associated with phenylketonuria
E280K
the mutation is associated with phenylketonuria
E280K
-
the mutant shows 2% of wild type activity
E390G
the mutation is associated with phenylketonuria
E390G
the mutant shows 62% activity compared to the wild type enzyme
E76G
-
the mutant shows 85% of wild type activity
E76G
-
the mutant shows 65% of wild type activity
F161S
-
the mutation is associated with phenylketonuria
F161S
-
the mutant with wild type activity exhibits less than 50% of wild type protein level
F39L
the mutant enzyme shows reduced activity compared to the wild type
F39L
-
the mutant has approximately 3fold higher specific activity than the wild type enzyme and leads to moderate phenyletonuria
G247V
-
the mutation is associated with phenylketonuria
G247V
-
the mutant shows 4% of wild type activity
G46S
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and is involved in the disorder hyperphenylalaninemia
G46S
the mutation is associated with phenylketonuria
G46S
the mutant enzyme shows reduced activity compared to the wild type
G46S
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
G46S
the mutant shows lower allosteric Phe-binding ability compared to the wild type enzyme
G46S
the mutation causes phenylketonuria
I174T
the mutation results in the classical phenylketonuria phenotype expressing 0.2-1.8% of the wild type PAH activity when using L-phenylalanine as substrate, and has less 0.1% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as the substrate
I174T
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine or L-Phe) compared to wild-type
I65S
the mutation is associated with phenylketonuria
I65S
the mutant enzyme shows reduced activity compared to the wild type
I65T
-
22% of wild-type phenylalanine hydroxylase activity
I65T
naturally occuring mutation involved in hyperphenylalaninemia of heterozygous patients, sequence analysis, the heterologous mutant shows reduced activity compared to the wild-type enzyme
I65T
-
frequent naturally occuring mutation involved in enzyme deficiency and BH4-responsive hyperphenylalaninemia and/or phenylketonuria
I65T
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but the mutant can be rescued by co-expression of chaperones GroEL and GroES
I65T
the mutant shows increased specific activity using L-phenylalanine as substrate and decreased specific activity using S-carboxymethyl-L-cysteine compared to the wild type enzyme
I65T
-
the mutation is associated with phenylketonuria
I65T
the mutation is associated with phenylketonuria
I65T
the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate
I65T
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine) no difference in Km (L-Phe) compared to wild-type
I65T
the mutant enzyme shows reduced activity compared to the wild type
I65T
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to moderate phenyletonuria
I65T
the mutant shows 33% activity compared to the wild type enzyme
I65T/R408W
-
naturally occuring mutation in the regulatory domain, that affects enzyme activity and causes the classical form of phenylketonuria
I65T/R408W
naturally occuring mutation involved in phenylketonuria
I65T/R408W
the mutant shows 15% activity compared to the wild type enzyme
L212P
naturally occuring mutation involved in phenylketonuria
L212P
the mutant shows about 20% activity compared to the wild type enzyme
L249F
the mutation is associated with phenylketonuria
L249F
the mutant shows about 55% activity compared to the wild type enzyme
L249P
the mutation is associated with phenylketonuria
L249P
the mutant shows about 5% activity compared to the wild type enzyme
L255S
-
the mutation is associated with phenylketonuria
L255S
-
the mutant shows 3% of wild type activity
L311P
the mutation is associated with phenylketonuria
L311P
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
L348V
25% activity after expression in Escherichia coli in the absence of GroESL, 55% in the presence of GroESL, 77% activity after expression in COS cells at 27°C
L348V
the mutant retains significant catalytic activity yet is observed in classic and moderate phenylketonuria patients
L348V
-
the mutation is associated with phenylketonuria
L348V
the mutation is associated with phenylketonuria
L348V
-
the mutant shows 38% of wild type activity
L48S
-
frequent naturally occuring mutation involved in enzyme deficiency and BH4-responsive hyperphenylalaninemia and/or phenylketonuria
L48S
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
L48S
the mutation is associated with phenylketonuria
L48S
-
the mutant has approximately 3fold higher specific activity than the wild type enzyme and leads to moderate phenyletonuria
L48S
the mutant shows 39% activity compared to the wild type enzyme
P225T
-
naturally occuring knockout missense mutation leading to a severe phenylketonuria phenotype
P225T
the mutation is associated with phenylketonuria
P281L
-
inactive
P281L
exon 7 C842T mutation naturally occuring in phenylketonuria patient from the Cukurova region in Turkey, sequence determination and analysis
P281L
-
naturally occuring missense mutation causing a severe phenylketonuria phenotype
P281L
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
P281L
-
the mutation is associated with phenylketonuria
P281L
the mutation is associated with phenylketonuria
R111X
-
the mutation is associated with phenylketonuria
R111X
the mutation is associated with phenylketonuria
R155H
the mutant displays low PAH activity and decreased apparent affinity for L-Phe yet is observed in mild hyperphenylalaninaemia, mutant does not display kinetic instability, as it is stabilized by (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin similarly to wild type enzyme
R155H
-
the mutation is associated with phenylketonuria
R158Q
-
naturally occuring missense mutation causing a severe phenylketonuria phenotype
R158Q
-
the mutation is associated with phenylketonuria
R158Q
the mutation is associated with phenylketonuria
R158Q
the mutation results in the classical phenylketonuria phenotype expressing 0.2-1.8% of the wild type PAH activity when using L-phenylalanine as substrate, and has less 0.1% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as the substrate
R158Q
the mutant shows 10% activity compared to the wild type enzyme
R158Q
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine or L-Phe) compared to wild-type
R158Q
-
the mutation leads to mild phenyletonuria
R158W
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
R158W
the mutation is associated with phenylketonuria
R176X
-
the mutation is associated with phenylketonuria
R176X
the mutation is associated with phenylketonuria
R241C
-
site-directed mutagenesis, the mutation occurs naturally in humans altering the tetrahydrobiopterin responsiveness, the mutant shows reduced activity and dimer stability compared to the wild-type
R241C
the mutation is associated with phenylketonuria
R243Q
exon 7 G728A mutation naturally occuring in phenylketonuria patient from the Cukurova region in Turkey, sequence determination and analysis
R243Q
-
site-directed mutagenesis, the common mutation occurs naturally in phenylketonuria patients from east asia, the mutant shows reduced activity compared to the wild-type, the mutation affects hydrogen binding between the amide nitrogen of R243 and the carbonyl oxygen of Asp129
R243Q
-
the mutation is associated with phenylketonuria
R243Q
the mutation is associated with phenylketonuria
R243Q
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
R252W
-
naturally occuring missense mutation causing a severe phenylketonuria phenotype
R252W
the mutation is associated with phenylketonuria
R252W
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
R261P
-
naturally occuring missense mutation causing a mild phenylketonuria phenotype
R261P
the mutant shows about 14% activity compared to the wild type enzyme
R261Q
-
31% of wild-type phenylalanine hydroxylase activity
R261Q
exon 7 G728A mutation naturally occuring in phenylketonuria patients from the Cukurova region in Turkey, sequence determination and analysis, second most found mutation within 23 patients
R261Q
naturally occuring mutation involved in hyperphenylalaninemia of heterozygous patients, sequence analysis, the heterologous mutant shows reduced activity compared to the wild-type enzyme
R261Q
-
frequent naturally occuring mutation involved in enzyme deficiency and BH4-responsive hyperphenylalaninemia and/or phenylketonuria
R261Q
-
naturally occuring missense mutation causing a severe phenylketonuria phenotype
R261Q
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
R261Q
naturally occuring mutation involved in phenylketonuria
R261Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but the mutant can be rescued by co-expression of chaperones GroEL and GroES
R261Q
the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme
R261Q
-
the mutation is associated with phenylketonuria
R261Q
the mutation is associated with phenylketonuria
R261Q
the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate
R261Q
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine) no difference in Km (L-Phe) compared to wild-type
R261Q
-
the mutation leads to 29% of wild type activity and moderate phenyletonuria
R261Q
the mutant shows 44% activity compared to the wild type enzyme
R270K
expression in the presence of the chemical chaperone glycerol enhances activity after purification
R270K
naturally occuring mutation involved in hyperphenylalaninemia of heterozygous patients, sequence analysis, the heterologous mutant shows reduced activity compared to the wild-type enzyme
R270K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but the mutant can be rescued by co-expression of chaperones GroEL and GroES
R270K
the mutation is associated with phenylketonuria
R270K
the mutant shows about 15% activity compared to the wild type enzyme
R408Q
-
site-directed mutagenesis, the mutation occurs naturally in humans altering the tetrahydrobiopterin responsiveness, the mutant shows reduced activity and dimer stability compared to the wild-type
R408Q
the mutation is associated with phenylketonuria
R408Q
the mutant shows 46% activity compared to the wild type enzyme
R408Q
-
the mutant shows 84% of wild type activity
R408W
exon 12 C1222T mutation naturally occuring in phenylketonuria patient from the Cukurova region in Turkey, sequence determination and analysis
R408W
-
naturally occuring mutation involved in hyperphenylalaninemia and/or in phenylketonuria, overview
R408W
naturally occuring mutation involved in phenylketonuria
R408W
the mutant is dysfunctional in nearly all biochemical parameters, as evidenced by disease severity in homozygous and hemizygous patients
R408W
-
the mutation is associated with phenylketonuria
R408W
the mutation is associated with phenylketonuria
R408W
the mutation results in the classical phenylketonuria phenotype expressing 0.2-1.8% of the wild type PAH activity when using L-phenylalanine as substrate, and has less 0.1% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as the substrate
R408W
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine or L-Phe) compared to wild-type
R408W
the mutant shows 2% activity compared to the wild type enzyme
R408W
-
the mutant with wild type activity exhibits less than 50% of wild type protein level and leads to classic phenyletonuria
R408W/R158Q
the mutant shows 5% residual activity compared to the wild type enzyme
R408W/R158Q
the mutant shows 4% activity compared to the wild type enzyme
R413P
-
site-directed mutagenesis, the common mutation occurs naturally in phenylketonuria patients from east asia, the mutant shows reduced activity compared to the wild-type
R413P
the mutation is associated with phenylketonuria
R413P
-
the mutant shows 3% of wild type activity
R68S
the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme
R68S
the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate
R68S
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine) no difference in Km (L-Phe) compared to wild-type
R68S
-
the mutant shows 98% of wild type activity
S349P
-
inactive
S349P
-
naturally occuring missense mutation causing a severe phenylketonuria phenotype
S349P
the mutation is associated with phenylketonuria
S349P
-
the mutant shows 1% of wild type activity
T427P
-
increase in the amount of oligomeric forms higher than tetramers after preincubation of a mixture of dimeric and tetrameric forms with phenylalanine, tetrameric form exhibits approx. 50% of wild-type tetramer phenylalanine hydroxylase activity
T427P
low basal activity, little activation by preincubation with substrate, no kinetic cooperativity
V388M
40% activity after expression in Escherichia coli in the absence of GroESL, 82% in the presence of GroESL, 78% activity after expression in COS cells at 27°C
V388M
expression in the presence of the chemical chaperone glycerol enhances activity after purification
V388M
-
30% of wild-type phenylalanine hydroxylase activity
V388M
naturally occuring mutation involved in hyperphenylalaninemia of heterozygous patients, sequence analysis, the heterologous mutant shows reduced activity compared to the wild-type enzyme
V388M
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but the mutant can be rescued by co-expression of chaperones GroEL and GroES
V388M
the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme
V388M
the mutation is associated with phenylketonuria
V388M
the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate
V388M
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine or L-Phe) compared to wild-type
Y204C
the mutation is associated with phenylketonuria
Y204C
the mutant shows wild type activity
Y325A
-
high degree of aggregation, but suffivcient tetrameric form for characterization
Y325A
-
no enzymic activity, aggregation of protein
Y325F
-
kinetics, thermal stability, oligomerization profile similar to wild-type
Y325F
-
stable, similar yields and oligomeric distribution as wild-type, posttranslational hydroxylation
Y356X
-
the mutation is associated with phenylketonuria
Y356X
the mutation is associated with phenylketonuria
Y414C
-
frequent naturally occuring mutation involved in enzyme deficiency and BH4-responsive hyperphenylalaninemia and/or phenylketonuria
Y414C
the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme
Y414C
the mutation is associated with phenylketonuria
Y414C
the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate
Y414C
-
heteromeric hPAH (wild-type + mutant) shows: significantly decreased Vmax values compared to wild-type, significantly increased Km values (substrate: S-carboxymethyl-L-cysteine or L-Phe) compared to wild-type
Y414C
-
the mutation leads to 1% of wild type activity and classic phenyletonuria
Y414C
the mutant shows 57% activity compared to the wild type enzyme
H264Q/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
H264Q/V379D
-
double mutant of full length enzyme, shows significant tyrosine hydroxylation activity
H264Q/Y277H/V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
H264Q/Y277H/V379D
-
triple mutant of full length enzyme, shows significant tyrosine hydroxylation activity
R270K
active-site mutation
R270K
-
the mutation effectively abolishes binding of L-phenylalanine in the active site and leads to strongly reduced kcat/Km value (10000 down) compared to the wild type enzyme
V379D
-
truncated enzyme containing the catalytic domain, mutant shows tyrosine hydroxylation activity
V379D
-
site-directed mutagenesis of catalytic core mutant DELTA117PheH, the isotopic effects of substrates [4-2H]-, [3,5-2H2]-, and 2H5-phenylalanine are altered compared to the wild-type enzyme, overview
additional information
gene knockdown by doublestranded RNA, significant reduction of melanization, enzyme is required for fully functional melanotic encapsulation response
additional information
-
gene knockdown by doublestranded RNA, significant reduction of melanization, enzyme is required for fully functional melanotic encapsulation response
additional information
gene knockdown by doublestranded RNA, significant reduction of melanization, enzyme is required for fully functional melanotic encapsulation response
additional information
-
gene knockdown by doublestranded RNA, significant reduction of melanization, enzyme is required for fully functional melanotic encapsulation response
additional information
Q9XYQ5
gene pah-1 knockout mutant worms do not show an altered phenotype, but in combination with a second mutation of cuticle synthesis, the mutant worms lack a yellow pigment in the cuticle, and show stimulatory effect on superoxide dismutase, and severe cuticle defects, overview
additional information
-
gene pah-1 knockout mutant worms do not show an altered phenotype, but in combination with a second mutation of cuticle synthesis, the mutant worms lack a yellow pigment in the cuticle, and show stimulatory effect on superoxide dismutase, and severe cuticle defects, overview
additional information
-
mutant p.R68S, reduced apparent and equilibrium binding affinity for tetrahydrobiopterin, increased affinity and non-cooperative response for L-phenylalanine, strong substrate inhibition
additional information
-
N-terminal deletion of amino acid residues 1-102, reduction of Hill coefficient, square-wave pattern of surface plasmon resonance response. N-terminal deletion of amino acid residues 1-102 plus C-terminal deletion of amino acid residues 428-452, reduction of Hill coefficient, square-wave pattern of surface plasmon resonance response. C-terminal deletion of amino acid residues 428-452, surface plasmon resonance signal similar to wild-type
additional information
-
N-terminal deletion of amino acid residues 1-116, kinetics, thermal stability, oligomerization profile similar to wild-type. N-terminal deletion of amino acid residues 1-116 plus mutation Y325F, 3fold reduction in kcat-value
additional information
arginine mutations are important for the evolutionary structure and function of the phenylalanine hydroxylase gene, phenylketonuria patients from the Cukurova region in Turkey show in 50% of investigated alleles the IvsVS10-11g splicing mutation, overview
additional information
-
arginine mutations are important for the evolutionary structure and function of the phenylalanine hydroxylase gene, phenylketonuria patients from the Cukurova region in Turkey show in 50% of investigated alleles the IvsVS10-11g splicing mutation, overview
additional information
identification of mutations, that alter the interaction of subunits, which could be a source of phenotypic variation in genetic diseases involving multimeric proteins, e.g. in hypephenylalaninemia, overview
additional information
-
identification of mutations, that alter the interaction of subunits, which could be a source of phenotypic variation in genetic diseases involving multimeric proteins, e.g. in hypephenylalaninemia, overview
additional information
-
identification of naturally occuring missense mutations of the PHA gene involved in phenylketonuria, an autosomal recessive metabolic disease caused by PHA deficiency, the mutants show residual or no catalytic activity
additional information
calculation and computational modeling of the probability that a mutation or an amino acid change in certain positions lead to phenylketonuria to improve clinical monitoring, diagnosis, prognosis and treatment, overview
additional information
-
determination of mutations in gene pah in patients with phenylketonuria in different Israelian populations, genotyping, genotype-phenotype correlation, overview
additional information
-
determination of mutations in gene pah in patients with phenylketonuria, screening and genotyping, genotype-phenotype correlation in the different ethnic groups of Israel, responsiveness of mutants to tetrahydrobiopterin treatment, overview
additional information
-
enzyme mutation can lead to tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. BH4 responsiveness in hyperphenylalaninaemia depends on the patient's genotype and residual PAH activity, of patients with moderate and classic forms of phenylketonuria, only a few are classified as responders and the clinical significance of the effect size may be small, molecular mechanism, phenotypes and clinical treatment, overview
additional information
hyperphenylalaninemia is a group of autosomal recessive disorders caused by a wide range of PAH gene variants, identification of 5 human variants in a Southern Italian population, genotyping, overview
additional information
-
hyperphenylalaninemia is a group of autosomal recessive disorders caused by a wide range of PAH gene variants, identification of 5 human variants in a Southern Italian population, genotyping, overview
additional information
-
identification of 57 mutations in a wide range genotyping, the mutants show substantial residual PAH activity, average 47%, presumed to be associated with BH4-responsiveness, genotyping, genotype-phenotype correlation, overview
additional information
-
identification of mutations involved in hyperphenylalaninemia and/or in phenylketonuria, genotyping of a Southern Italian population, overview
additional information
-
mutations in the pah gene can lead to phenylketonuria, patients respond to treatment with tetrahydrobiopterin, the extent depends on the type of disorder, phenotypes, overview
additional information
-
phenylketonuria results from a mutation in the liver enzyme phenylalanine hydroxylase, the disease is correlated with high and persistent levels of Phe in the plasma plasma of PKU patients causing permanent neurological damage. Construction of PAH-based fusion proteins with delivery moieties based on the HIV-transactivator of transcription peptide, and fragments of human hepatocyte growth factor, i.e. N-terminal and first, second, and third kringle domains, respectively, of HGF, aiming to specifically target PAH to the liver, which retain PAH activity after being internalized into liver cells, effects of the transgenic construct in HuH7, HepG2, and Colo205 cells
additional information
phenylketonuria, PKU, results from mutations in the pah gene and is characterized by elevated phenylalanine levels in the plasma, the specific category of PKU since classical PKU requires a stringent diet while milder categories may not require diet and a very important BH4-responsive category may be treated with the PAH cofactor 6R-tetrahydrobiopterin, there is a close genotype-phenotype correlation in PKU, so genotyping is very important for diagnosis and therapy, overview
additional information
-
phenylketonuria, PKU, results from mutations in the pah gene and is characterized by elevated phenylalanine levels in the plasma, the specific category of PKU since classical PKU requires a stringent diet while milder categories may not require diet and a very important BH4-responsive category may be treated with the PAH cofactor 6R-tetrahydrobiopterin, there is a close genotype-phenotype correlation in PKU, so genotyping is very important for diagnosis and therapy, overview
additional information
-
construction and catalytic properties of deletion mutant DELTA117PheH, consisting of the catalytic core of the enzyme, the isotopic effects of substrates [4-2H]-, [3,5-2H2]-, and 2H5-phenylalanine are unaltered compared to the wild-type enzyme, overview
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