{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qin C"],"funding":["Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)"],"pagination":["6002"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11255334"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["The AMP-forming acetyl-CoA synthetase is regulated by lysine acetylation both in bacteria and eukaryotes. However, the underlying mechanism is poorly understood. The Bacillus subtilis acetyltransferase AcuA and the AMP-forming acetyl-CoA synthetase AcsA form an AcuA•AcsA complex, dissociating upon lysine acetylation of AcsA by AcuA. Crystal structures of AcsA from Chloroflexota bacterium in the apo form and in complex with acetyl-adenosine-5'-monophosphate (acetyl-AMP) support the flexible C-terminal domain adopting different conformations. AlphaFold2 predictions suggest binding of AcuA stabilizes AcsA in an undescribed conformation. We show the AcuA•AcsA complex dissociates upon acetyl-coenzyme A (acetyl-CoA) dependent acetylation of AcsA by AcuA. We discover an intrinsic phosphotransacet"],"journal":["Nature communications"],"pubmed_title":["Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule."],"pmcid":["PMC11255334"],"funding_grant_id":["LA2984-6/1"],"pubmed_authors":["Specht R","Girbardt B","Graf LG","Geist N","Palm GJ","Striska K","Dorre B","Doerr M","Lammers M","Delcea M","Schulze S","Berndt L","Janetzky M","Kemnitz S","Bornscheuer UT","Qin C"],"additional_accession":[]},"is_claimable":false,"name":"Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.","description":"The AMP-forming acetyl-CoA synthetase is regulated by lysine acetylation both in bacteria and eukaryotes. However, the underlying mechanism is poorly understood. The Bacillus subtilis acetyltransferase AcuA and the AMP-forming acetyl-CoA synthetase AcsA form an AcuA•AcsA complex, dissociating upon lysine acetylation of AcsA by AcuA. Crystal structures of AcsA from Chloroflexota bacterium in the apo form and in complex with acetyl-adenosine-5'-monophosphate (acetyl-AMP) support the flexible C-terminal domain adopting different conformations. AlphaFold2 predictions suggest binding of AcuA stabilizes AcsA in an undescribed conformation. We show the AcuA•AcsA complex dissociates upon acetyl-coenzyme A (acetyl-CoA) dependent acetylation of AcsA by AcuA. We discover an intrinsic phosphotransacet","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T07:37:52.118Z","creation":"2025-04-06T17:10:59.714Z"},"accession":"S-EPMC11255334","cross_references":{"pubmed":["39019872"],"doi":["10.1038/s41467-024-49952-0"]}}