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Tyrosine hydroxylase activity is increased in the short term by phosphorylation.
Treatment options for severe tyrosine hydroxylase deficiency have been less effective.
It is an inhibitor of the enzyme tyrosine hydroxylase.
The phosphorylation at Ser19 and Ser8 has no direct effect on tyrosine hydroxylase activity.
Tyrosine hydroxylase activity is regulated chronically (days) by protein synthesis.
Dystonia in tyrosine hydroxylase deficiency usually affects the legs.
Tyrosine hydroxylase can also be regulated by inhibition.
Long term regulation of tyrosine hydroxylase can also be mediated by phosphorylation mechanisms.
Increase in tyrosine hydroxylase activity due to phosphorylation can be sustained by nicotine for up to 48 hours.
Tyrosine hydroxylase is activated by phosphorylation dependent binding to 14-3-3 proteins.
Tyrosine hydroxylase can be inhibited by the drug α-methyl-para-tyrosine (metirosine).
Later evidence suggested that it might lie on chromosome 11, near the gene for the enzyme tyrosine hydroxylase.
The severe form of tyrosine hydroxylase deficiency causes symptoms at a very young age (first months of life).
Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines.
Tyrosine hydroxylase is a tetramer of four identical subunits (homotetramer).
Mild and moderate forms of tyrosine hydroxylase deficiency show dramatic improvement when treated with levodopa.
This initial reaction catalyzed by tyrosine hydroxylase has been shown to be the rate limiting step in the production of catecholamines.
Vitamin D increases expression of the tyrosine hydroxylase gene in adrenal medullary cells.
Tyrosine hydroxylase is somewhat stabilized to heat inactivation when the regulatory serines are phosphorylated.
The activity of tyrosine hydroxylase in the brains of patients with Alzheimer's disease has been shown to be significantly reduced compared to healthy individuals.
In the California work, the researchers took skin cells from rats and used a modified virus to insert genes that produce the enzyme tyrosine hydroxylase.
Tyrosine hydroxylase deficiency occurs due to disruptions or changes (mutations) of the TH gene.
As for the tetramerization and catalytic domains their structure was found with rat tyrosine hydroxylase using X-ray crystallography.
Several chemists and toxicologists came upon a paper describing very similar ocular, but not skin, lesions with inhibitors of tyrosine hydroxylase.
Dopamine is a brain chemical that serves as a neurotransmitter and is deficient in children with tyrosine hydroxylase deficiency.