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Literature summary for 1.14.16.1 extracted from

  • Abita, J.P.; Blandin-Savoja, F.; Rey, F.
    Phenylalanine 4-monooxygenase from human liver (1987), Methods Enzymol., 142, 27-35.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cAMP-dependent protein kinase
-
Homo sapiens
cAMP-dependent protein kinase
-
Rattus norvegicus
lysolecithin
-
Homo sapiens
lysolecithin
-
Rattus norvegicus
additional information relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis Homo sapiens
additional information relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis Rattus norvegicus
additional information enzyme activity is not stimulated by phosphorylation Homo sapiens
Phospholipids activate Homo sapiens
Phospholipids activate Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0026
-
tetrahydrobiopterin
-
Homo sapiens
0.033
-
6,7-dimethyltetrahydropterin
-
Homo sapiens
0.05
-
phenylalanine cofactor tetrahydrobiopterin Homo sapiens
0.55
-
phenylalanine cofactor dimethyltetrahydropterin Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
2 * 54000, fetal liver enzyme, SDS-PAGE Homo sapiens
107000
-
fetal liver enzyme, sucrose density gradient centrifugation Homo sapiens
165000
-
gel filtration Homo sapiens
275000
-
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification
-
Homo sapiens
side-chain modification enzyme contains 0.3 mol of phosphate per mol of enzyme subunit Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
Phenyl-Sepharose, DEAE-Sepharose Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-
liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.106
-
-
Homo sapiens

Storage Stability

Storage Stability Organism
-80°C, enzyme concentration 1 mg/ml, several months, no loss of activity Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 6,7-dimethyltetrahydrobiopterin
-
Homo sapiens L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
-
r
L-phenylalanine + tetrahydrobiopterin + O2 relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis Homo sapiens L-tyrosine + dihydrobiopterin + H2O
-
?
L-phenylalanine + tetrahydrobiopterin + O2 relatively low activity with tetrahydrobiopterin can be selectively increased by limited proteolysis Rattus norvegicus L-tyrosine + dihydrobiopterin + H2O
-
?
L-phenylalanine + tetrahydrobiopterin + O2 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 Homo sapiens L-tyrosine + dihydrobiopterin + H2O
-
?
L-phenylalanine + tetrahydrobiopterin + O2 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 Rattus norvegicus L-tyrosine + dihydrobiopterin + H2O
-
?

Subunits

Subunits Comment Organism
dimer
-
Rattus norvegicus
dimer 2 * 54000, fetal liver enzyme, SDS-PAGE Homo sapiens

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin
-
Homo sapiens
tetrahydrobiopterin
-
Rattus norvegicus