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Literature summary extracted from

  • Vermeer, L.M.; Higgins, C.A.; Roman, D.L.; Doorn, J.A.
    Real-time monitoring of tyrosine hydroxylase activity using a plate reader assay (2013), Anal. Biochem., 432, 11-15.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.16.2 expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.16.2 3,4-dihydroxyphenylacetaldehyde potent inhibitor, 0.01 and 0.02 mM cause 66% and 75% inhibition, respectively Homo sapiens
1.14.16.2 3-iodo-L-tyrosine competitive inhibitor Homo sapiens
1.14.16.2 CoCl2 0.1 mM CoCl2 results in more than 80% inhibition Homo sapiens

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 Homo sapiens
-
 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.16.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.16.2 amylose resin column chromatography and HiPrep Q column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2
-
 Homo sapiens 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.16.2 tyrosine hydroxylase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.16.2 tetrahydrobiopterin
-
 Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.14.16.2 0.05
-
 pH and temperature not specified in the publication Homo sapiens 3-iodo-L-tyrosine