KDAC8 substrate specificity quantified by a biologically relevant, label-free deacetylation assay.

ABSTRACT: Analysis of the human proteome has identified thousands of unique protein sequences that contain acetylated lysine residues in vivo. These modifications regulate a variety of biological processes and are reversed by the lysine deacetylase (KDAC) family of enzymes. Despite the known prevalence and importance of acetylation, the details of KDAC substrate recognition are not well understood. While several methods have been developed to monitor protein deacetylation, none are particularly suited for identifying enzyme-substrate pairs of label-free substrates across the entire family of lysine deacetylases. Here, we present a fluorescamine-based assay which is more biologically relevant than existing methods and amenable to probing substrate specificity. Using this assay, we evaluated the activ

SUBMITTER: Toro TB 

PROVIDER: S-EPMC4815229 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature