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本文引用的文献

1
The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family.孤儿蛋白双γ-谷氨酰半胱氨酸还原酶加入吡啶核苷酸二硫化物还原酶家族。
Biochemistry. 2013 Apr 30;52(17):2905-13. doi: 10.1021/bi4003343. Epub 2013 Apr 19.
2
Active site residues critical for flavin binding and 5,6-dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB.黄素破坏酶 BluB 中与黄素结合和 5,6-二甲基苯并咪唑生物合成相关的活性位点残基至关重要。
Protein Sci. 2012 Jun;21(6):839-49. doi: 10.1002/pro.2068. Epub 2012 Apr 23.
3
Expression of a soluble form of iodotyrosine deiodinase for active site characterization by engineering the native membrane protein from Mus musculus.通过对来自 Mus musculus 的天然膜蛋白进行工程改造,表达一种可溶性形式的碘酪氨酸脱碘酶,用于活性位点表征。
Protein Sci. 2012 Mar;21(3):351-61. doi: 10.1002/pro.2020.
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Comparing thyroid and insect hormone signaling.比较甲状腺激素和昆虫激素信号转导。
Integr Comp Biol. 2006 Dec;46(6):777-94. doi: 10.1093/icb/icl034. Epub 2006 Sep 7.
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Evolutionary roots of iodine and thyroid hormones in cell-cell signaling.碘和甲状腺激素在细胞间信号传递中的进化根源。
Integr Comp Biol. 2009 Aug;49(2):155-66. doi: 10.1093/icb/icp053. Epub 2009 Jun 23.
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Flavogenomics--a genomic and structural view of flavin-dependent proteins. flavogenomics——黄素依赖蛋白的基因组学和结构学研究
FEBS J. 2011 Aug;278(15):2625-34. doi: 10.1111/j.1742-4658.2011.08202.x. Epub 2011 Jul 5.
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Reductive dehalogenation mediated initiation of aerobic degradation of 2-chloro-4-nitrophenol (2C4NP) by Burkholderia sp. strain SJ98.伯克霍尔德氏菌 SJ98 介导的还原脱卤作用启动 2-氯-4-硝基苯酚(2C4NP)的好氧降解。
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Iodide accumulation by aerobic bacteria isolated from subsurface sediments of a 129I-contaminated aquifer at the Savannah River site, South Carolina.从南卡罗来纳州萨凡纳河场址 129I 污染含水层的地下沉积物中分离出的好氧菌对碘的积累。
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Biocontrol of biomass bulking caused by Haliscomenobacter hydrossis using a newly isolated lytic bacteriophage.利用新分离的溶菌噬菌体控制水发鞘氨醇单胞菌引起的生物量膨胀。
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碘酪氨酸脱碘酶:一种存在于多种门类生物中的独特黄素蛋白。

Iodotyrosine deiodinase: a unique flavoprotein present in organisms of diverse phyla.

作者信息

Phatarphekar Abhishek, Buss Jennifer M, Rokita Steven E

机构信息

Department of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.

出版信息

Mol Biosyst. 2014 Jan;10(1):86-92. doi: 10.1039/c3mb70398c.

DOI:10.1039/c3mb70398c
PMID:24153409
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3858845/
Abstract

Iodide is required for thyroid hormone synthesis in mammals and other vertebrates. The role of both iodide and iodinated tyrosine derivatives is currently unknown in lower organisms, yet the presence of a key enzyme in iodide conservation, iodotyrosine deiodinase (IYD), is suggested by genomic data from a wide range of multicellular organisms as well as some bacteria. A representative set of these genes has now been expressed, and the resulting enzymes all catalyze reductive deiodination of diiodotyrosine with kcat/Km values within a single order of magnitude. This implies a physiological presence of iodotyrosines (or related halotyrosines) and a physiological role for their turnover. At least for Metazoa, IYD should provide a new marker for tracing the evolutionary development of iodinated amino acids as regulatory signals through the tree of life.

摘要

碘化物是哺乳动物和其他脊椎动物甲状腺激素合成所必需的。碘化物和碘化酪氨酸衍生物在低等生物中的作用目前尚不清楚,但来自多种多细胞生物以及一些细菌的基因组数据表明,存在一种碘化物保存关键酶——碘酪氨酸脱碘酶(IYD)。现在已经表达了一组具有代表性的这些基因,所产生的酶都催化二碘酪氨酸的还原脱碘反应,其催化常数与米氏常数之比(kcat/Km)值在一个数量级内。这意味着碘酪氨酸(或相关卤代酪氨酸)在生理上的存在以及它们周转的生理作用。至少对于后生动物来说,IYD应该为追踪碘化氨基酸作为调节信号在生命之树中的进化发展提供一个新的标记。