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

Titelangaben

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. Bd. 128 (7 November 2020) Heft 6/7 . - S. 375-378.
ISSN 1439-3646
DOI: https://doi.org/10.1055/a-1022-9916

Abstract

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.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie > Lehrstuhl Biochemie I - Proteinbiochemie der Signaltransduktion - Univ.-Prof. Dr. Clemens Steegborn
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 540 Chemie
500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 27 Nov 2019 08:11
Letzte Änderung: 18 Mär 2022 13:45
URI: https://eref.uni-bayreuth.de/id/eprint/53415