Tyrosine Hydroxylase and Regulation of Dopamine Synthesis

By S. C. Daubner, Tiffany Le, Shanzhi Wang. Archives of Biochemistry and Biophysics, 2010

1,017 citations recorded by the source corpus.

Tyrosine hydroxylase is the rate-limiting enzyme of catecholamine biosynthesis; it uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Its amino terminal 150 amino acids comprise a domain whose structure is involved in regulating the enzyme’s activity. Modes of regulation include phosphorylation by multiple kinases at 4 different serine residues, and dephosphorylation by 2 phosphatases. The enzyme is inhibited in feedback fashion by the catecholamine neurotransmitters. Dopamine binds to TyrH competitively with tetrahydrobiopterin, and interacts with the R domain. TyrH activity is modulated by protein-protein interactions with enzymes in the same pathway or the tetrahydrobiopterin pathway, structural proteins considered to be chaperones that mediate the neuron’s oxidative state, and the protein that transfers dopamine into secretory vesicles. TyrH is modified in the presence of NO, resulting in nitration of tyrosine residues and the glutathionylation of cysteine residues.

Subfields: Biochemistry, Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/25bb172a083ea36e95ea2e7dddf9f833abbcbf2a

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Citations in the corpus

• Complexity of dopamine metabolism (2013, background): “Excellent in-depth reports of TH are available and should be consulted for further information [43,44].”