Abstract:
: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).
journal_name
Sci Repjournal_title
Scientific reportsauthors
Schuster S,Roessler C,Meleshin M,Zimmermann P,Simic Z,Kambach C,Schiene-Fischer C,Steegborn C,Hottiger MO,Schutkowski Mdoi
10.1038/srep22643subject
Has Abstractpub_date
2016-03-04 00:00:00pages
22643issn
2045-2322pii
srep22643journal_volume
6pub_type
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