TH (Tyrosine 3-hydroxylase; also tyrosine 3-monooxygenase) is a 60-62 kDa member of the biopterin-dependent aromatic amino acid hydroxylase family of molecules. It is expressed by neurons of the dopamine and autonomic nervous system, plus the neuroendocrine cells of the adrenal medulla. TH is considered the rate limiting enzyme for catecholamine synthesis, and serves to catalyze the hydroxylation of L-tyrosine. It maintains stores of catecholamines following secretion, and its activity is regulated by targeted site phosphorylation. Human TH is 528 amino acids (aa) in length. It contains an N-terminal ACT domain (aa 69-190) that binds small molecules and regulates enzyme activity, and a C-terminal enzymatic region (aa 196-493). There are three significant utilized phosphorylation sites. Two at Ser31 and Ser40 increase enzyme activity, while phosphorylation at Ser19 promotes subsequent Ser40 phosphorylation. TH functions as a 240 kDa noncovalent homotetramer. There are four potential splice variants. One shows a deletion of aa 31-34, a second shows a deletion of aa 31-61, while a third contains a Met substitution for aa 1-34. A fourth isoform variant shows a deletion of aa 35-61. Over aa 278-401, human TH shares 94% aa sequence identity with mouse TH, a molecule that most closely resembles the fourth human isoform variant described above.

Alternate Names

TH, TYH

Entrez Gene IDs

7054 (Human); 21823 (Mouse); 25085 (Rat)

Gene Symbol

UniProt

P07101

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Human/Mouse/Rat Tyrosine Hydroxylase Alexa Fluor® 532-conjugated Antibody

R&D Systems, part of Bio-Techne | Catalog # AF7566X

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Background: Tyrosine Hydroxylase