1.14.16.1: phenylalanine 4-monooxygenase
This is an abbreviated version!
For detailed information about phenylalanine 4-monooxygenase, go to the full flat file.
Word Map on EC 1.14.16.1
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1.14.16.1
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phenylketonuria
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hyperphenylalaninemia
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bh4
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error
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pterins
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inborn
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children
-
hydroxylases
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neurotransmitter
-
province
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tetrahydropterins
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counsel
-
intellectual
-
dopamine
-
l-tyrosine
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genotype-phenotype
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prenatal
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serotonin
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dihydropteridine
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caucasian
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catecholamine
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hepatocytes
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sepiapterin
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genotype-based
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quinonoid
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non-heme
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chromobacterium
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neopterin
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ligation-dependent
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dihydrochloride
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neuropsychological
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lysolecithin
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lifelong
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phenylpyruvate
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dopa
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cyclohydrolase
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molecular biology
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rflps
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p-chlorophenylalanine
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dihydrobiopterin
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hypopigmentation
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s-oxidation
-
pteridine
-
violaceum
- 1.14.16.1
- phenylketonuria
- hyperphenylalaninemia
- bh4
- error
- pterins
-
inborn
- children
- hydroxylases
-
neurotransmitter
-
province
- tetrahydropterins
-
counsel
-
intellectual
- dopamine
- l-tyrosine
-
genotype-phenotype
-
prenatal
- serotonin
- dihydropteridine
-
caucasian
- catecholamine
- hepatocytes
- sepiapterin
-
genotype-based
-
quinonoid
-
non-heme
-
chromobacterium
- neopterin
-
ligation-dependent
- dihydrochloride
-
neuropsychological
- lysolecithin
-
lifelong
- phenylpyruvate
- dopa
-
cyclohydrolase
- molecular biology
-
rflps
- p-chlorophenylalanine
- dihydrobiopterin
-
hypopigmentation
-
s-oxidation
- pteridine
- violaceum
Reaction
Synonyms
cePAH, DicPAH, EC 1.14.3.1, EC 1.99.1.2, HPAH, L-phenylalanine 4-hydroxylase, oxygenase, phenylalanine 4-mono-, P4H, PAH, PheH, phenylalaninase, phenylalanine 4-hydroxylase, phenylalanine hydroxylase, phenylalanine monooxygenase, PheOH, phhA
ECTree
1.14.16.1 phenylalanine 4-monooxygenaseAdvanced search results
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results (Turnover Number
Turnover Number on EC 1.14.16.1 - phenylalanine 4-monooxygenase
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TURNOVER NUMBER [1/s] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1.6
6-methyltetrahydropterin
-
wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
additional information
additional information
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wild-type PAH kinetic analyses using a new assay reveal cooperativity of activated PAH toward (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
0.2
5,6,7,8-tetrahydrobiopterin
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.2
5,6,7,8-tetrahydrobiopterin
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.57
5,6,7,8-tetrahydrobiopterin
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.6
5,6,7,8-tetrahydrobiopterin
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.9
6,7-dimethyltetrahydropterin
-
mutant enzyme I234D, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
1.4
6,7-dimethyltetrahydropterin
-
wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
0.031 - 0.51
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH
1.12
6-methyl-tetrahydrobiopterin
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pH 7.0, 25°C, recombinant mutant DELTA 117PheH V379D
7.85
6-methyl-tetrahydrobiopterin
-
pH 7.0, 25°C, recombinant mutant DELTA 117PheH
0.04 - 1.97
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH
0.18
L-phenylalanine
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.3
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH V379D
0.57
L-phenylalanine
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
1.93
L-phenylalanine
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
4.9
L-phenylalanine
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
5.83
L-phenylalanine
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
6.62
L-phenylalanine
-
wild type enzyme, without preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C
8.55
L-phenylalanine
-
pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH
8.81
L-phenylalanine
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
8.93
L-phenylalanine
-
wild type enzyme, 5 min preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C
10.9
L-phenylalanine
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
18
L-phenylalanine
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
21.5
L-phenylalanine
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.4
L-tryptophan
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.51
L-tryptophan
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
1.02
L-tryptophan
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
2.08
L-tryptophan
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.135
phenylalanine
-
Ser2-Gln428 deletion mutant, L-phenylalanine activated, dimeric form
0.165
phenylalanine
-
Ser2-Gln428 deletion mutant, lysophosphatidylcholine activated, dimeric form
0.233
phenylalanine
-
Ser2-Gln428 deletion mutant, lysophosphatidylcholine and phenylalanine activated, dimeric form
0.45
phenylalanine
-
Asp112-Lys452 deletion mutant, lysophosphatidylcholine activated, tetrameric form
0.667
phenylalanine
-
Gly103-Gln428 deletion mutant, lysophosphatidylcholine activated, dimeric form
0.877
phenylalanine
-
recombinant enzyme, lysophosphatidylcholine activated, tetrameric form
1.05
phenylalanine
-
Asp112-Lys452 deletion mutant, L-phenylalanine activated, tetrameric form
1.05
phenylalanine
-
Asp112-Lys452 deletion mutant, lysophosphatidylcholine and phenylalanine activated, tetrameric form
1.24
phenylalanine
-
Gly103-Gln428 deletion mutant, lysophosphatidylcholine and phenylalanine activated, dimeric form
1.3
phenylalanine
-
recombinant enzyme, L-phenylalanine activated, tetrameric form
1.33
phenylalanine
-
Gly103-Gln428 deletion mutant, L-phenylalanine activated, dimeric form
1.59
phenylalanine
-
recombinant enzyme, lysophosphatidylcholine and phenylalanine activated, tetrameric form
