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Literature summary extracted from

  • Gordon, S.L.; Quinsey, N.S.; Dunkley, P.R.; Dickson, P.W.
    Tyrosine hydroxylase activity is regulated by two distinct dopamine-binding sites (2008), J. Neurochem., 106, 1614-1623.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.16.2 additional information phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme, the low-affinity dopamine-binding site is able to regulate tyrosine hydroxylase activity in both the non-phosphorylated and pSer40 forms of the enzyme, with dissociation of dopamine from the site increasing activity 12fold and 9fold respectively Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.16.2 adrenaline
-
 Rattus norvegicus
1.14.16.2 dopamine binding kinetics and regulatory function, overview, phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme. Binding of dopamine to the high-affinity site also decreases Vmax and increases the Km for the cofactor tetrahydrobiopterin, while binding of dopamine to the low affinity site regulates tyrosine hydroxylase activity by increasing the Km for tetrahydrobiopterin Rattus norvegicus
1.14.16.2 noradrenaline
-
 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.16.2 additional information
-
 additional information kinetics analysis, overview Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.16.2 cytosol
-
 Rattus norvegicus 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2 Rattus norvegicus the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of residue Ser40. Phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme, regulation mechanism overview 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.16.2 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.14.16.2 phosphoprotein phosphorylation of Ser40 activtes the enzyme by reversing the inhibition by dopamine binding Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2
-
 Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
 ?
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2 the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of residue Ser40. Phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme, regulation mechanism overview Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.16.2 tyrosine hydroxylase
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.16.2 25 30 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.16.2 7.4
-
 assay at Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.16.2 tetrahydrobiopterin binding of dopamine to the high-affinity site of the enzyme decreases Vmax and increases the Km for the cofactor tetrahydrobiopterin, while binding of dopamine to the low affinity site regulates tyrosine hydroxylase activity by increasing the Km for tetrahydrobiopterin Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.16.2 additional information
-
 additional information inhibition kinetics Rattus norvegicus