ArticleProceedings of the National Academy of Sciences of the United States of America2014
Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 95 citations in OpenAlex.
- A Crystalline and Thermally Stable Selenocysteine Selenenic Acid.Angewandte Chemie (International ed. in English) · 2026Article
- DIO3 associates with sorting nexins and endosomal trafficking networks in ovarian cancer.Cellular oncology (Dordrecht, Netherlands) · 2026Article
- Beyond Hormone Levels: Thyroid Hormone Signaling from Neurogenesis to Alzheimer's Disease.Cells · 2026Review
- Thyroid Hormone Deiodination-Mechanisms and Small Molecule Enzyme Mimics.Biomolecules · 2025Review
- Structural Insights into the Iodothyronine Deiodinase 2 Catalytic Core and Deiodinase Catalysis and Dimerization.Biomolecules · 2024Article
- Thyroid Hormone Biomonitoring: A Review on Their Metabolism and Machine-Learning Based Analysis on Effects of Endocrine Disrupting Chemicals.Environment & health (Washington, D.C.) · 2024Review
- Factors and Mechanisms of Thyroid Hormone Activity in the Brain: Possible Role in Recovery and Protection.Biomolecules · 2024Review
- Demonstration of the Formation of a Selenocysteine Selenenic Acid through Hydrolysis of a Selenocysteine Selenenyl Iodide Utilizing a Protective Molecular Cradle.Molecules (Basel, Switzerland) · 2023Article
- Relationships Between Maternal Selected Metals (Cu, Mg, Zn and Fe), Thyroid Function and Blood Glucose Levels During Pregnancy.Biological trace element research · 2023Article
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- Combining In Vitro and In Silico New Approach Methods to Investigate Type 3 Iodothyronine Deiodinase Chemical Inhibition Across Species.Environmental toxicology and chemistry · 2023Article
- Insights into the Mechanism of Human Deiodinase 1.International journal of molecular sciences · 2022Article
- Thyroid hormone-dependent oligodendroglial cell lineage genomic and non-genomic signaling through integrin receptors.Frontiers in pharmacology · 2022Review
- Article
- Deiodinases and the Metabolic Code for Thyroid Hormone Action.Endocrinology · 2021Review
- Cryo-EM: A new dawn in thyroid biology.Molecular and cellular endocrinology · 2021Review
- Xenopus laevis and human type 3 iodothyronine deiodinase enzyme cross-species sensitivity to inhibition by ToxCast chemicals.Toxicology in vitro : an international journal published in association with BIBRA · 2021Article
- Human Type 1 Iodothyronine Deiodinase (Thyroid : official journal of the American Thyroid Association · 2021Article
- Extension of the taxonomic coverage of the family GH126 outside Firmicutes and in silico characterization of its non-catalytic terminal domains.3 Biotech · 2020Article
- Thyroxine binding to type III iodothyronine deiodinase.Scientific reports · 2020Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Local levels of active thyroid hormone (3,3',5-triiodothyronine) are controlled by the action of activating and inactivating iodothyronine deiodinase enzymes. Deiodinases are selenocysteine-dependent membrane proteins catalyzing the reductive elimination of iodide from iodothyronines through a poorly understood mechanism. We solved the crystal structure of the catalytic domain of mouse deiodinase 3 (Dio3), which reveals a close structural similarity to atypical 2-Cys peroxiredoxin(s) (Prx). The structure suggests a route for proton transfer to the substrate during deiodination and a Prx-related mechanism for subsequent recycling of the transiently oxidized enzyme. The proposed mechanism is supported by biochemical experiments and is consistent with the effects of mutations of conserved amino acids on Dio3 activity. Thioredoxin and glutaredoxin reduce the oxidized Dio3 at physiological concentrations, and dimerization appears to activate the enzyme by displacing an autoinhibitory loop from the iodothyronine binding site. Deiodinases apparently evolved from the ubiquitous Prx scaffold, and their structure and catalytic mechanism reconcile a plethora of partly conflicting data reported for these enzymes.
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