{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Voukia F"],"funding":["European Research Council","Lundbeck Foundation"],"pagination":["477"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12899889"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(3)"],"pubmed_abstract":["Histone lysine acetylation is a widespread posttranslational modification, essential for vital functions in eukaryotic organisms. Histone lysine acetyltransferases (KATs) employ acetyl-coenzyme A as a universal acetyl donor for acetylation of lysine residues in histone and non-histone proteins. Despite the biomedicinal importance of modulation of the KAT activity, application of the acetyl-coenzyme A cosubstrate structure for the design of potent and selective inhibitors has been underexplored. Here, we developed functionalized coenzyme A analogs as inhibitors against human histone lysine acetyltransferases GCN5, KAT8, and HAT1. In contrast to the unmodified coenzyme A, which was found to be a poor inhibitor of GCN5 and KAT8 (IC<sub>50</sub> > 150 μM), we showed that a ketone-substituted c"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Inhibition of Histone Lysine Acetyltransferases by Coenzyme A Analogs."],"pmcid":["PMC12899889"],"funding_grant_id":["715691","R344-2020-1051"],"pubmed_authors":["Andersen SB","Bilgin N","Mecinovic J","Voukia F"],"additional_accession":[]},"is_claimable":false,"name":"Inhibition of Histone Lysine Acetyltransferases by Coenzyme A Analogs.","description":"Histone lysine acetylation is a widespread posttranslational modification, essential for vital functions in eukaryotic organisms. Histone lysine acetyltransferases (KATs) employ acetyl-coenzyme A as a universal acetyl donor for acetylation of lysine residues in histone and non-histone proteins. Despite the biomedicinal importance of modulation of the KAT activity, application of the acetyl-coenzyme A cosubstrate structure for the design of potent and selective inhibitors has been underexplored. Here, we developed functionalized coenzyme A analogs as inhibitors against human histone lysine acetyltransferases GCN5, KAT8, and HAT1. In contrast to the unmodified coenzyme A, which was found to be a poor inhibitor of GCN5 and KAT8 (IC<sub>50</sub> > 150 μM), we showed that a ketone-substituted c","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-09T13:12:22.99Z","creation":"2026-07-09T13:09:13.589Z"},"accession":"S-EPMC12899889","cross_references":{"pubmed":["41683453"],"doi":["10.3390/molecules31030477"]}}