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Literature summary for 1.14.16.2 extracted from

  • Skjevik, A.A.; Mileni, M.; Baumann, A.; Halskau, O.; Teigen, K.; Stevens, R.C.; Martinez, A.
    The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes (2014), J. Mol. Biol., 426, 150-168.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
complex of 14-3-3gamma protein and phosphorylated tyrosine hydroxylase(1-43), sitting drop vapor diffusion method, using 30% (w/v) polyethylene glycol 2000 monomethyl ether as precipitant 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
-
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P07101
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein
-
Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
tyrosine hydroxylase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin
-
Homo sapiens