Acyllysines

Acyllysines are a class of post-translational modifications (PTMs) of proteins where the epsilon-amino group of lysine residues is acylated. This modification involves the covalent attachment of an acyl group, such as acetyl, succinyl, propionyl, or butyryl groups, to the side chain of lysine. Acylation of lysine is a reversible process, with deacylating enzymes known as deacetylases and acylases playing crucial roles in its regulation. This dynamic modification is widespread across all domains of life and affects a vast number of proteins, including histones, transcription factors, and metabolic enzymes.

The functional consequences of lysine acylation are diverse and context-dependent. It can significantly alter the physicochemical properties of the modified protein, impacting its charge, structure, and interactions with other molecules. For instance, the acetylation of histones, a well-studied form of lysine acylation, plays a critical role in epigenetic regulation by modulating chromatin structure and gene expression. Beyond histones, lysine acylation has been implicated in regulating protein stability, localization, activity, and the formation of protein complexes. The study of acyllysines has expanded significantly with advancements in proteomic techniques, allowing for the identification of thousands of acylated lysine sites across the proteome. Understanding the enzymes involved in installing and removing acyl groups, as well as the specific roles of different acylation marks, remains an active area of research.