ArticleProtein science : a publication of the Protein Society2016
Functional analysis of iodotyrosine deiodinase from drosophila melanogaster.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- Polar Interactions between Substrate and Flavin Control Iodotyrosine Deiodinase Function.Biochemistry · 2024Article
- Misregulation of bromotyrosine compromises fertility in maleProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The 2'-hydroxy group of flavin mononucleotide influences the catalytic function and promiscuity of the flavoprotein iodotyrosine dehalogenase.RSC chemical biology · 2023Article
- Substrate Electronics Dominate the Rate of Reductive Dehalogenation Promoted by the Flavin-Dependent Iodotyrosine Deiodinase.Biochemistry · 2023Article
- Sequence Conservation Does Not Always Signify a Functional Imperative as Observed in the Nitroreductase Superfamily.Biochemistry · 2022Article
- The minimal structure for iodotyrosine deiodinase function is defined by an outlier protein from the thermophilic bacterium Thermotoga neapolitana.The Journal of biological chemistry · 2021Article
- Redox control of iodotyrosine deiodinase.Protein science : a publication of the Protein Society · 2019Article
- The importance of a halotyrosine dehalogenase forThe Journal of biological chemistry · 2018Article
- Insect ArylalkylamineFrontiers in molecular biosciences · 2018Review
- The distribution and mechanism of iodotyrosine deiodinase defied expectations.Archives of biochemistry and biophysics · 2017Review
- Active Site Binding Is Not Sufficient for Reductive Deiodination by Iodotyrosine Deiodinase.Biochemistry · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The flavoprotein iodotyrosine deiodinase (IYD) was first discovered in mammals through its ability to salvage iodide from mono- and diiodotyrosine, the by-products of thyroid hormone synthesis. Genomic information indicates that invertebrates contain homologous enzymes although their iodide requirements are unknown. The catalytic domain of IYD from Drosophila melanogaster has now been cloned, expressed and characterized to determine the scope of its potential catalytic function as a model for organisms that are not associated with thyroid hormone production. Little discrimination between iodo-, bromo-, and chlorotyrosine was detected. Their affinity for IYD ranges from 0.46 to 0.62 μM (K
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.