Product description |
Malonylation of lysine is a newly identified reversible modification controlling protein activity. Sirt5, a regulatory enzyme for lysine malonylation, can catalyze lysine demalonylation reactions in vivo and in vitro. With integrated proteomic approaches and biochemistry analysis, lysine malonylation is widely distributed in wide ranges of histones and non-histone substrates. Lysine malonylation may provide a new paradigm in the cellular regulation, such as energy metabolism in diverse organisms. |
Background |
Histones, fundamental proteins involved in chromatin structure and gene regulation, are subject to a wide array of enzyme-catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitination, and numerous others. Histone L-lactylation, a recently discovered post-translational modification induced by lactate has emerged as a significant addition to this repertoire. The extent and dynamics of this modification are highly reliant on lactate levels within the cellular microenvironment and can be modulated through the introduction of extracellular lactate in cultured cells or the stimulation of intracellular glycolysis. The introduction of lysine L-lactylation is mediated by the acetyltransferase p300, while the removal of lactylation marks from histones has been attributed to Class I histone deacetylases (HDAC 1-3). Histone lactylation has been implicated in various biological processes, including inflammation, fibrosis, differentiation, and cancer progression. |