Titlebar

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

 

A continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions

Title data

Schuster, Sabine ; Roessler, Claudia ; Meleshin, Marat ; Zimmermann, Philipp ; Simic, Zeljko ; Kambach, Christian ; Schiene-Fischer, Cordelia ; Steegborn, Clemens ; Hottiger, Michael O. ; Schutkowski, Mike:
A continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions.
In: Scientific Reports. Vol. 6 (2016) . - p. 22643.
ISSN 2045-2322
DOI: https://doi.org/10.1038/srep22643

Abstract in another language

Sirtuins are NAD(+) dependent lysine deacylases involved in many regulatory processes such as control of metabolic pathways, DNA repair and stress response. Modulators of sirtuin activity are required as tools for uncovering the biological function of these enzymes and as potential therapeutic agents. Systematic discovery of such modulators is hampered by the lack of direct and continuous activity assays. The present study describes a novel continuous assay based on the increase of a fluorescence signal subsequent to sirtuin mediated removal of a fluorescent acyl chain from a modified TNFα-derived peptide. This substrate is well recognized by human sirtuins 1-6 and represents the best sirtuin 2 substrate described so far with a kcat/KM-value of 176 000 M(-1)s(-1). These extraordinary substrate properties allow the first determination of Ki-values for the specific Sirt2 inhibitory peptide S2iL5 (600 nM) and for the quasi-universal sirtuin inhibitor peptide thioxo myristoyl TNFα (80 nM).

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 26940860
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: 14 Mar 2016 11:04
Last Modified: 14 Mar 2016 11:04
URI: https://eref.uni-bayreuth.de/id/eprint/31740