Engaging with benzoyllysine through a π-π-π mechanism.

Epigenetic modifications have been gaining in prominence as fundamental components of the chromatin regulatory machinery. In this review, we summarize the molecular and structural mechanisms of reading, writing, and erasing of lysine benzoylation, a recently discovered posttranslational modification (PTM) in histones. We highlight a unique nature of the conjugated π system of benzoyllysine that may aid in the development of benzoyllysine-specific effectors indifferent to the saturated acyllysine modifications. We also discuss transcriptional and metabolic functions associated with benzoylation of histones and implications of ingesting of sodium benzoate for human health.