Export bibliographic data
Literature by the same author
plus on the publication server
plus at Google Scholar


Structure and Mechanism of Iodothyronine Deiodinases : What We Know, What We Don't Know, and What Would Be Nice to Know

Title data

Steegborn, Clemens ; Schweizer, Ulrich:
Structure and Mechanism of Iodothyronine Deiodinases : What We Know, What We Don't Know, and What Would Be Nice to Know.
In: Experimental and clinical endocrinology & diabetes. (7 November 2019) .
ISSN 1439-3646
DOI: https://doi.org/10.1055/a-1022-9916

Abstract in another language

Deiodinases catalyze the specific removal of iodine atoms from one of the two iodinated phenyl rings in iodothyronines. They thereby fine-regulate local thyroid hormone concentrations in organs or cells. The chemical reaction is unique in the sense that in metazoans the reductive elimination of iodide depends on the rare amino acid selenocysteine in the enzymes' active centers. While there is no prokaryotic homologue of such deiodinases, the solution of the crystal structure of a catalytic domain of mouse deiodinase 3 has revealed that the ancient peroxiredoxin structure has been repurposed, and improved using selenocysteine, as a deiodinase during metazoan evolution. Likewise, many biochemical findings obtained over decades can now be interpreted in light of the molecular structure. Despite this leap in our understanding of deiodinase structure, there are still several open questions that need to be addressed in order to fully understand substrate binding, catalytic mechanism, and regulation of deiodinases. We surmise that these issues as well as differences between the three highly homologous isoenzymes must be understood in order to develop modulators of deiodinases that could be valuable in clinical use.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 27 Nov 2019 08:11
Last Modified: 27 Nov 2019 08:11
URI: https://eref.uni-bayreuth.de/id/eprint/53415