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Literature summary for 1.14.16.1 extracted from

  • Kaufman, S.
    Aromatic amino acid hydroxylases (1987), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 18, 217-282.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
cAMP-dependent protein kinase
-
Homo sapiens
cAMP-dependent protein kinase 2-4fold increase in activity in the presence of tetrahydrobiopterin 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 relatively low activity with tetrahydrobiopterin can be selectively increased by phosphorylation Rattus norvegicus
additional information non activated enzyme has much greater activity with 6-methyltetrahydropterin and dimethyltetrahydropterin than with tetrahydrobiopterin Rattus norvegicus
N-ethylmaleimide activation by alkylation of sulfhydryl groups Rattus norvegicus
Phospholipids activate Homo sapiens
Phospholipids activate Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000 110000
-
Rattus norvegicus
200000 210000
-
Rattus norvegicus

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information hepatic enzyme consists of a mixture of phosphorylated and nonphosphorylated forms Rattus norvegicus
side-chain modification liver enzyme in untreated animals is a mixture of phosphorylated and nonphosphorylated forms, enzyme may be phosphorylated in vivo by cAMP-dependent protein kinase Rattus norvegicus
side-chain modification activity of liver enzyme might be regulated by phosphorylation-dephosphorylation Homo sapiens

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 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 Rattus norvegicus L-tyrosine + dihydrobiopterin + H2O
-
?
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 non activated enzyme has much greater activity with 6-methyltetrahydropterin and dimethyltetrahydropterin than with tetrahydrobiopterin 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
More
-
Homo sapiens
More some authors report that the enzyme exists as a mixture of dimers and tetramers, others report that it exists solely as tetramer or as dimer, percentage of dimers increases on frozen storage, preincubation of the enzyme with phenylalanine leads to even higher than 200000 Da molecular weight forms Rattus norvegicus
tetramer tetrameric species accounts for 78% of the total enzyme Rattus norvegicus

Cofactor

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