Kmal
Lysine malonylation (Kmal, maK), protein malonylation or malonylation, is a reversible post-translational modification (PTM) in eukaryotic and prokaryotic cells, in which a malonyl group (–CO–CH2–COOH) is added to a lysine (K) residue of a protein. It was first identified in 2011 by Peng et al. as an evolutionarily conserved modification and belongs to the acidic acyl modifications such as succinylation and glutarylation. As a dynamically regulated modification, it responds to conditions such as stress responses, metabolic processes, and mutations, thereby influencing the charge, structure, and function of proteins. This involves, among other things, the metabolic pathways of glucose and fatty acids as well as histone-mediated gene regulation, and is increasingly associated with immune regulation, angiogenesis, osteoarthritis, cancer and metabolic diseases such as obesity and type 2 diabetes. Its biological significance is increasingly recognized, but many aspects of its regulation and function remain unresolved, so that its therapeutic potential is still unexplored.
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