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New insights into the structure and mechanism of iodothyronine deiodinases

Title data

Schweizer, Ulrich ; Steegborn, Clemens:
New insights into the structure and mechanism of iodothyronine deiodinases.
In: Journal of Molecular Endocrinology. Vol. 56 (21 September 2015) Issue 2 . - R37-R52.
ISSN 1479-6813
DOI: https://doi.org/10.1530/JME-15-0156

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Abstract in another language

Iodothyronine deiodinases are a family of enzymes that remove specific iodine atoms from one of the two aromatic rings in thyroid hormones. They thereby fine-tune local thyroid hormone concentrations and cellular thyroid hormone signaling. Deiodinases catalyze a remarkable biochemical reaction, i. e. the reductive elimination of a halogenide from an aromatic ring. In metazoans, deiodinases depend on the rare amino acid selenocysteine. The recent solution of the first experimental structure of a deiodinase catalytic domain allowed for a reappraisal of the many mechanistic and mutagenesis data that had been accumulated over more than thirty years. Hence, the structure generates new impetus for efforts directed at understanding catalytic mechanism, substrate specificity, and regulation of deiodinases. This review will focus on structural and mechanistic aspects of iodothyronine deiodinases and briefly compare these enzymes with dehalogenases, which catalyze related reactions. A general mechanism for the selenium-dependent deiodinase reaction will be described, which integrates the mouse deiodinase 3 crystal structure and biochemical studies. We will summarize further, sometimes isoform-specific molecular features of deiodinase catalysis and regulation, and we will shortly discuss available compounds for modulating deiodinase activity for therapeutic purposes.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 26390881
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 26 Oct 2015 07:48
Last Modified: 16 Mar 2016 06:44
URI: https://eref.uni-bayreuth.de/id/eprint/20791