Tyrosine hydroxylase and regulation of dopamine synthesis

Daubner, S. Colette; Le, Tiffany; Wang, Shanzhi

doi:10.1016/j.abb.2010.12.017

Cited by 1,092Neurotransmitter Receptor Influence on BehaviorMetabolism and Genetic DisordersParkinson's Disease Mechanisms and Treatments

Tyrosine hydroxylase and regulation of dopamine synthesis

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Daubner, S. Colette, Le, Tiffany, Wang, Shanzhi·2011·Archives of Biochemistry and Biophysics

DOI 10.1016/j.abb.2010.12.017PMC PMC3065393

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Abstract

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 four different serine residues, and dephosphorylation by two 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.

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When TH is reduced to a certain threshold, it causes the motor symptoms of PD.
“when it is reduced to a certain threshold, it will cause the motor symptoms of PD [24]”
From Neuroprotective Effect of Ceftriaxone on MPTP‐Induced Parkinson’s Disease Mouse Model by Regulating Inflammation and Intestinal Microbiota (2021) · cites this paper as [24]
TH is the rate-limiting enzyme that participates in dopamine synthesis.
“TH is the rate-limiting enzyme that participates in dopamine synthesis”
From Neuroprotective Effect of Ceftriaxone on MPTP‐Induced Parkinson’s Disease Mouse Model by Regulating Inflammation and Intestinal Microbiota (2021) · cites this paper as [24]

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[25]Dunkley PR Bobrovskaya L Graham ME von Nagy-Felsobuki EI Dickson PW 2004 Tyrosine hydroxylase phosphorylation: Regulation and consequences J Neurochem 91 1025 1043 15569247
[83]Kuhn D 2003 Tetrahydrobiopterin prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide Molecular Pharmacology 64 946 14500751

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Authors: Daubner, S. C., Le, T., & Wang, S.
Affiliations: St. Mary's University, Texas (US)
Texas A&M University (US)
Corresponding author: Daubner, S. Colette
ORCID: Wang, Shanzhi
Venue: Archives of Biochemistry and Biophysics
Publisher: Elsevier BV
Published: 2011-04
Volume: 508
Issue: 1
Pages: 1-12
ISSN: 0003-9861 (ISSN-L)
DOI: 10.1016/j.abb.2010.12.017
PMC: PMC3065393
OpenAlex: W2103493168
Cited by: 1,092
References: 89
Citations by year: 2026: 120 · 2025: 125 · 2024: 99 · 2023: 116 · 2022: 98 · 2021: 100 · 2020: 87 · 2019: 70 · 2018: 71 · 2017: 57 · 2016: 37 · 2015: 27 · 2014: 31 · 2013: 29 · 2012: 22
FWCI: 1.56
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Archives of Biochemistry and Biophysics (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R01GM047291)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurotransmitter Receptor Influence on Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Keywords: tyrosine hydroxylase, dopamine synthesis, catecholamine synthesis, tetrahydrobiopterin, DOPA, R domain, phosphorylation, product inhibition, dopamine, protein-protein interaction, molecular chaperones, oxidative stress, nitration, glutathionylation, nitric oxide, protein kinase A, phosphatase
MeSH terms: Amino Acid Sequence, Animals, Dopamine, Humans, Molecular Sequence Data, Nitrates, Sulfhydryl Compounds, Tyrosine 3-Monooxygenase, Protein Structure, Tertiary

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Tyrosine hydroxylase and regulation of dopamine synthesis

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