ArticleBiochemistry2009
Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.Nature communications · 2022Article
- Modulation of Human Phenylalanine Hydroxylase by 3-Hydroxyquinolin-2(1H)-One Derivatives.Biomolecules · 2021Article
- Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity.Scientific reports · 2016Article
- The regulatory domain of human tryptophan hydroxylase 1 forms a stable dimer.Biochemical and biophysical research communications · 2016Article
- Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme.Scientific reports · 2016Article
- Structural insights into the regulation of aromatic amino acid hydroxylation.Current opinion in structural biology · 2015Review
- The solution structure of the regulatory domain of tyrosine hydroxylase.Journal of molecular biology · 2014Article
- The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes.Journal of molecular biology · 2014Article
- Article
- Allosteric regulation of phenylalanine hydroxylase.Archives of biochemistry and biophysics · 2012Review
- Monitoring allostery in D2O: a necessary control in studies using hydrogen/deuterium exchange to characterize allosteric regulation.Analytical and bioanalytical chemistry · 2011Article
- Tyrosine hydroxylase and regulation of dopamine synthesis.Archives of biochemistry and biophysics · 2011Review
- Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain.Biochemistry · 2011Article
- Regulation of phenylalanine hydroxylase: conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometry.Biochemistry · 2010Article
- Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The activity of tyrosine hydroxylase is regulated by reversible phosphorylation of serine residues in an N-terminal regulatory domain and catecholamine inhibition at the active site. Catecholamines such as dopamine bind very tightly to the resting enzyme; phosphorylation of Ser40 decreases the affinity for catecholamines by 3 orders of magnitude. The effects of dopamine binding and phosphorylation of Ser40 on the kinetics of deuterium incorporation into peptide bonds were examined by mass spectrometry. When dopamine is bound, three peptic peptides show significantly slower deuterium incorporation, 35-41 and 42-71 in the regulatory domain and 295-299 in the catalytic domain. In the phosphorylated enzyme, peptide 295-299 shows more rapid incorporation of deuterium, while 35-41 and 42-71 can not be detected. These results are consistent with tyrosine hydroxylase existing in two different conformations. In the closed conformation, the regulatory domain lies across the active site loop containing residues 295-298; this is stabilized when dopamine is bound in the active site. In the open conformation, the regulatory domain has moved out of the active site, allowing substrate access; this conformation is favored by phosphorylation of Ser40.
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