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Literature summary for 1.14.16.2 extracted from

  • Neira, J.L.; Hornos, F.; Bacarizo, J.; Camara-Artigas, A.; Gomez, J.
    The monomeric species of the regulatory domain of tyrosine hydroxylase has a low conformational stability (2016), Biochemistry, 55, 3418-3431 .
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34700
-
catalytic domain, gel filtration Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tyrosine + tetrahydrobiopterin + O2 Homo sapiens
-
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + tetrahydrobiopterin + O2
-
Homo sapiens L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 17044, catalytic domain, calculated from amino acid sequence Homo sapiens

Synonyms

Synonyms Comment Organism
TyrH
-
Homo sapiens
tyrosine hydroxylase
-
Homo sapiens