Comparative kinetic characterization of rat thyroid iodotyrosine dehalogenase and iodothyronine deiodinase type 1
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The initial characterization of a thyroid iodotyrosine dehalogenase (tDh), which deiodinates mono-iodotyrosine and di-iodotyrosine, was made almost 50 years ago, but little is known about its catalytic and kinetic properties. A distinct group of dehalogenases, the so-called iodothyronine deiodinases (IDs), that specifically remove iodine atoms from iodothyronines were subsequently discovered and have been extensively characterized. Iodothyronine deiodinase type 1 (ID1) is highly expressed in the rat thyroid gland, but the co-expression in this tissue of the two different dehalogenating enzymes has not yet been clearly defined. This work compares and contrasts the kinetic properties of tDh and ID1 in the rat thyroid gland. Differential affinities for substrates, cofactors and inhibitors distinguish the two activities, and a reaction mechanism for tDh is proposed. The results reported here support the view that the rat thyroid gland has a distinctive set of dehalogenases specialized in iodine metabolism.
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MIT and DIT can be deiodinated by iodotyrosine dehalogenase (DEHAL), and the iodide released is recycled as a sustained source of intrathyroidal iodide for TH synthesis.
“These MIT and DIT can be deiodinated by iodotyrosine dehalogenase (DEHAL), and the iodide released is recycled as a sustained source of intrathyroidal iodide for TH synthesis (98, 99).”
From Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion (2022) · cites this paper as [99]
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Type 2 iodothyronine deiodinase is highly expressed in human thyroid.
Salvatore, D., Tu, H., Harney, J. W., & Larsen, P. R. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118880 · Cited by 196 · see citing works
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Galton, V. A., Schneider, M. J., Clark, A. S., & St. Germain, D. L. (2009) · Endocrinology · doi:10.1210/en.2008-1572 · Cited by 181 · see citing works
Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion
Jing, L., & Zhang, Q. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.992883 · Cited by 61 · see citing works
- Authors
- Solis-S, J., Villalobos, P., Orozco, A., & Valverde-R, C.
- Affiliations
- Autonomous University of Queretaro (MX)
- Venue
- Journal of Endocrinology
- Publisher
- Bioscientifica
- Published
- 2004-06-01
- Volume
- 181
- Issue
- 3
- Pages
- 385-392
- ISSN
- 0022-0795 (ISSN-L)
- 1479-6805
- OpenAlex
- W2107892821
- Cited by
- 22
- References
- 2
- Citations by year
- 2022: 3 · 2020: 2 · 2018: 1 · 2017: 2 · 2016: 1 · 2013: 1
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Consejo Nacional de Ciencia y Tecnología
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Chemical Analysis and Environmental Impact
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Cancer Diagnosis and Treatment
- Keywords
- thyroid gland, enzyme kinetics, substrate affinity, cofactors, enzyme inhibitors, reaction mechanism, iodine metabolism, thyroid hormone synthesis, rats
- MeSH terms
- Animals, Enzyme Activation, Female, Hydrolases, Iodide Peroxidase, Iodine Radioisotopes, Male, NADP, Oxidation-Reduction, Thyroid Gland, Rats, Sprague-Dawley, Rats, Wistar, Rats
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