Lysine Deacetylase Activity Monitored by a Fluorogenic Assay using the CLARIOstar®

Protein acetylation is a universal regulatory mechanism of protein activities. Recent developments in epigenetic drug discovery have caused increasing interest in methods to study lysine deacetylation, including in vitro assays of lysine deacetylases. This application note describes use of the BMG Labtech CLARIOstar^® multimode reader to optimize a commercial peptidase coupled lysine deacetylase assay to establish the enzymatic properties of Escherichia coli CobB. CobB is a sirtuin-type enzyme that participates in the regulation of bacterial transcription, translation, metabolism, and chemotaxis.