Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization.
http://www.nature.com/nrm/journal/v15/n8/full/nrm3841.html
N-Acetylation of imidazole is not favourable, because it leads to a loss of aromaticity of the imidazole ring; the guanidinium group of arginine is too basic and always positively charged and thus cannot participate in nucleophilic substitution at the carbonyl group of acetyl-CoA. Lysine is thus a better nucleophile.
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