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Literature summary for 1.14.16.2 extracted from

  • Nakashima, A.; Hayashi, N.; Kaneko, Y.S.; Mori, K.; Sabban, E.L.; Nagatsu, T.; Ota, A.
    Role of N-terminus of tyrosine hydroxylase in the biosynthesis of catecholamines (2009), J. Neural Transm., 116, 1355-1362.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in monkey striatum using harmless adeno-associated virus vectors and in PC-12 cells and AtT-20 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information the deletion mutation of N-terminal 38-amino acids increases the binding capacity of 5,6,7,8,-tetrahydrobiopterin to tyrosine hydroxylase molecule to increase the activity and possibly to increase the stability Homo sapiens
R37E/R38E the point mutation increases the binding capacity of 5,6,7,8,-tetrahydrobiopterin to tyrosine hydroxylase molecule to increase the activity and possibly to increase the stability Homo sapiens

General Stability

General Stability Organism
the 14-3-3eta protein regulates tyrosine hydroxylase type 1 stability against degradation by acting on the N-terminus Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
adrenaline
-
Homo sapiens
dopamine
-
Homo sapiens
noradrenaline
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein Ser31 and Ser40 are readily phosphorylated to activate tyrosine hydroxylase type 1 in vitro. Although phosphorylation of Ser19 does not directly activate tyrosine hydroxylase, chaperone 14-3-3 protein binds and activates tyrosine hydroxylase at Ser19 phosphorylated by Ca2+/calmodulin-dependent protein kinase II. Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
-
Homo sapiens 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
?

Synonyms

Synonyms Comment Organism
TH1 isoform Homo sapiens
tyrosine hydroxylase
-
Homo sapiens
tyrosine hydroxylase type 1 isoform Homo sapiens

Cofactor

Cofactor Comment Organism Structure
5,6,7,8-tetrahydro-L-biopterin
-
Homo sapiens