{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Meng Y"],"funding":["South Carolina Experiment Station","NIH","NIH HHS","NIGMS NIH HHS"],"pagination":["1643"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10455477"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(8)"],"pubmed_abstract":["Short- and medium-chain acyl-CoA synthetases catalyze similar two-step reactions in which acyl substrate and ATP bind to form an enzyme-bound acyl-adenylate, then CoA binds for formation of the acyl-CoA product. We investigated the roles of active site residues in CoA binding in acetyl-CoA synthetase (Acs) and a medium-chain acyl-CoA synthetase (Macs) that uses 2-methylbutyryl-CoA. Three highly conserved residues, Arg<sup>193</sup>, Arg<sup>528</sup>, and Arg<sup>586</sup> of <i>Methanothermobacter thermautotrophicus</i> Acs (Acs<sub>Mt</sub>), are predicted to form important interactions with the 5'- and 3'-phosphate groups of CoA. Kinetic characterization of Acs<sub>Mt</sub> variants altered at each of these positions indicates these Arg residues play a critical role in CoA binding and c"],"journal":["Life (Basel, Switzerland)"],"pubmed_title":["The Roles of Coenzyme A Binding Pocket Residues in Short and Medium Chain Acyl-CoA Synthetases."],"pmcid":["PMC10455477"],"funding_grant_id":["R15 GM069374","SC-1700198","GM69374-01A1"],"pubmed_authors":["Ahmed O","Meng Y","Smith K","Ingram-Smith C"],"additional_accession":[]},"is_claimable":false,"name":"The Roles of Coenzyme A Binding Pocket Residues in Short and Medium Chain Acyl-CoA Synthetases.","description":"Short- and medium-chain acyl-CoA synthetases catalyze similar two-step reactions in which acyl substrate and ATP bind to form an enzyme-bound acyl-adenylate, then CoA binds for formation of the acyl-CoA product. We investigated the roles of active site residues in CoA binding in acetyl-CoA synthetase (Acs) and a medium-chain acyl-CoA synthetase (Macs) that uses 2-methylbutyryl-CoA. Three highly conserved residues, Arg<sup>193</sup>, Arg<sup>528</sup>, and Arg<sup>586</sup> of <i>Methanothermobacter thermautotrophicus</i> Acs (Acs<sub>Mt</sub>), are predicted to form important interactions with the 5'- and 3'-phosphate groups of CoA. Kinetic characterization of Acs<sub>Mt</sub> variants altered at each of these positions indicates these Arg residues play a critical role in CoA binding and c","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jul","modification":"2026-04-08T13:40:23.4Z","creation":"2025-04-06T16:25:02.57Z"},"accession":"S-EPMC10455477","cross_references":{"pubmed":["37629500"],"doi":["10.3390/life13081643"]}}