Iodotyrosine deiodinase, also known as iodotyrosine dehalogenase 1, is a type of deiodinase enzyme that scavenges iodide by removing it from iodinated tyrosine residues in the thyroid gland.[5] These iodinated tyrosines are produced during thyroid hormone biosynthesis.[6] The iodide that is scavenged by iodotyrosine deiodinase is necessary to again synthesize the thyroid hormones.[7] After synthesis, the thyroid hormones circulate through the body to regulate metabolic rate, protein expression, and body temperature.[8] Iodotyrosine deiodinase is thus necessary to keep levels of both iodide and thyroid hormones in balance.
Dehalogenation in aerobic organisms is usually done through oxidation and hydrolysis;[9] however, iodotyrosine deiodinase uses reductive dehalogenation. Iodotyrosine deiodinase and iodothyronine deiodinase have been determined as the only two known enzymes to catalyze reductive dehalogenation in mammals.[8] Although these two enzymes perform similar functions, they are structurally and mechanistically different. Iodothyronine deiodinase (not the enzyme that is the topic of this article) uses a selenocysteine active site for catalysis, is a member of the thioredoxin superfamily, and removes iodide only when the substrate is in a double-tyrosine form.[10] By contrast, iodotyrosine deiodinase (the topic enzyme) does not require selenocysteine or cysteine for catalysis,[11] is part of the NADH oxidase/flavin reductase superfamily,[12][13] and removes iodide when the substrate is a single amino acid.[14] Research on iodotyrosine deiodinase has historically been variable and slow due to its lack of stability and arduous purification.[15] Only recently has this enzyme been studied more deeply.[8]
^ abcGRCh38: Ensembl release 89: ENSG00000009765 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000019762 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Cite error: The named reference Moreno_2010 was invoked but never defined (see the help page).
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^ abcCite error: The named reference Rokita_2010 was invoked but never defined (see the help page).
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and 12 Related for: Iodotyrosine deiodinase information
Iodotyrosinedeiodinase, also known as iodotyrosine dehalogenase 1, is a type of deiodinase enzyme that scavenges iodide by removing it from iodinated...
similar to Prx, followed by a reductive recycling of the enzyme. Iodotyrosinedeiodinase contributes to breakdown of thyroid hormones. It releases iodine...
confused with the iodotyrosinedeiodinases that are also deiodinases, but not members of the iodothyronine family. The iodotyrosinedeiodinases (unlike the...
subfamily of deiodinase enzymes that use selenium as the otherwise rare amino acid selenocysteine. (Only the deiodinaseiodotyrosinedeiodinase, which works...
deiodinase activity of iodized single tyrosine molecules within the thyroid follicular cells. For information on that enzyme family, see Iodotyrosine...
detoxification of these classes of contaminants. For example, Iodotyrosinedeiodinase is a mammalian enzyme with the unusual function of aerobic reductive...
iodine atom is added in similar manner to the reaction intermediate 3-iodotyrosine. Inorganic iodine enters the body primarily as iodide, I−. After entering...
class is lithium, which inhibits thyroid hormone secretion by inhibiting iodotyrosine coupling, thyroidal iodide uptake, and alteration in structure of thyroglobulin...
triiodothyronine (T3) and thyroxine (T4), thereby blocking uptake of iodotyrosines from the colloid. They also block iodine release from peripheral hormone...
Plants, insects, zooplankton and algae store iodine as mono-iodotyrosine (MIT), di-iodotyrosine (DIT), iodocarbons, or iodoproteins. Many plants use thyroid...
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