{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["James AM"],"funding":["Medical Research Council","Wellcome Trust"],"pagination":["2105-2112"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6381604"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(9)"],"pubmed_abstract":["Acetyl coenzyme A (AcCoA), a key intermediate in mitochondrial metabolism, N-acetylates lysine residues, disrupting and, in some cases, regulating protein function. The mitochondrial lysine deacetylase Sirtuin 3 (Sirt3) reverses this modification with benefits reported in diabetes, obesity, and aging. We show that non-enzymatic lysine N-acetylation by AcCoA is greatly enhanced by initial acetylation of a cysteine residue, followed by SN-transfer of the acetyl moiety to a nearby lysine on mitochondrial proteins and synthetic peptides. The frequent occurrence of an S-acetyl intermediate before lysine N-acetylation suggests that proximity to a thioester is a key determinant of lysine susceptibility to acetylation. The thioesterase glyoxalase II (Glo2) can limit protein S-acetylation, thereby "],"journal":["Cell reports"],"pubmed_title":["Non-enzymatic N-acetylation of Lysine Residues by AcetylCoA Often Occurs via a Proximal S-acetylated Thiol Intermediate Sensitive to Glyoxalase II."],"pmcid":["PMC6381604"],"funding_grant_id":["110159/Z/15/Z","110158/Z/15/Z","MC_U105663142"],"pubmed_authors":["Hall AR","Hoogewijs K","Fearnley IM","Ding S","Murphy MP","Logan A","James AM"],"additional_accession":[]},"is_claimable":false,"name":"Non-enzymatic N-acetylation of Lysine Residues by AcetylCoA Often Occurs via a Proximal S-acetylated Thiol Intermediate Sensitive to Glyoxalase II.","description":"Acetyl coenzyme A (AcCoA), a key intermediate in mitochondrial metabolism, N-acetylates lysine residues, disrupting and, in some cases, regulating protein function. The mitochondrial lysine deacetylase Sirtuin 3 (Sirt3) reverses this modification with benefits reported in diabetes, obesity, and aging. We show that non-enzymatic lysine N-acetylation by AcCoA is greatly enhanced by initial acetylation of a cysteine residue, followed by SN-transfer of the acetyl moiety to a nearby lysine on mitochondrial proteins and synthetic peptides. The frequent occurrence of an S-acetyl intermediate before lysine N-acetylation suggests that proximity to a thioester is a key determinant of lysine susceptibility to acetylation. The thioesterase glyoxalase II (Glo2) can limit protein S-acetylation, thereby ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Feb","modification":"2026-05-07T06:06:05.484Z","creation":"2026-04-07T22:39:43.245Z"},"accession":"S-EPMC6381604","cross_references":{"pubmed":["28249157"],"doi":["10.1016/j.celrep.2017.02.018"]}}