AcylScan™ - Acylation Proteomics

Profiling lysine acylation in liver peptides from wild type and Sirt5 knockout mice: Venn diagram showing the degree of overlap of sites identified using the four indicated acylation-specific antibodies. See full dataset here.

Lysine residues are subject to a wide range of post-translational modifications due to the positively charged ε-amino group side chain. Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize the positive charge of lysine and confer structural alterations affecting substrate protein function. Cellular functions regulated by acylation include cell cycle regulation, mitochondrial metabolism, cytoskeletal regulation, protein-protein interactions and others.