The discovery of various lysine acylations raises a question as to whether they are subject to dynamic regulation and, if so, by which enzymes. Since acyltransferases play a crucial role in the succinylation process (acyltransferases are responsible for coupling acyl-CoA to non-protein substrates, possibly aiding lysine acylation as a side reaction). Using immunoprecipitation (IP) and liquid chromatographytandem mass spectrometry (LC-MS/MS), we found the succinyltransferase DLST interacts with PDHA1 and had a succinylation effect.