Lysine acylation comprises a group of post-translational modifications which involve the transfer of an acyl group to $ε$-amino group of a lysine residue. Most studied acylation modification is acetylation, however recently, a number of new acylation modifications have been discovered. These include formylation, propionylation, butyrylation, malonylation, succinylation, glutarylation and crotonylation. In this chapter, we review the discovery of various acylation modifications and the current insight into their function, regulation and dynamics.
Pougovkina, O., & de Boer, V. C. J. (2016). Protein Lysine Acylation: Abundance, Dynamics and Function. In Sirtuins (pp. 41–69). Springer Netherlands. https://doi.org/10.1007/978-94-024-0962-8_3