A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates.

A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates.
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哺乳动物还原性去二世酶具有脱盐酸盐氯化和溴化底物具有广泛的能力。

DOI:
10.1021/ja906642n
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发表时间:
2009-10-14
影响因子:
15
通讯作者:
Rokita, Steven E.
Rokita, Steven E.
中科院分区:
化学1区
文献类型:
--
作者:
McTamney, Patrick M.;Rokita, Steven E.

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碘酪氨酸脱碘酶是碘稳态和正常甲状腺功能所必需的哺乳动物。该酶促进3-碘酪氨酸的净还原脱碘以形成碘化物和酪氨酸。这种还原脱卤在好氧生物中并不常见,其对黄素单核苷酸的需求在催化中更是罕见。现在显示还原当量直接从黄素转移到卤化底物,而不涉及标准酶测定中通常包括的其他组分。此外,已发现脱碘酶作为脱溴酶和脱氯酶。这些新的活性扩展了黄素在生物催化中的可能作用,并为确定这一不寻常过程的机制提供了基础。
Iodotyrosine deiodinase is essential for iodide homeostasis and proper thyroid function in mammals. This enzyme promotes a net reductive deiodination of 3-iodotyrosine to form iodide and tyrosine. Such a reductive dehalogenation is uncommon in aerobic organisms, and its requirement for flavin mononucleotide is even more uncommon in catalysis. Reducing equivalents are now shown to transfer directly from the flavin to the halogenated substrate without involvement of other components typically included in the standard enzymatic assay. Additionally, the deiodinase has been discovered to act as a debrominase and a dechlorinase. These new activities expand the possible roles of flavin in biological catalysis and provide a foundation for determining the mechanism of this unusual process.
DOI: 10.1203/01.pdr.0000050655.25689.ce
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