{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Muroski JM"],"funding":["NIGMS NIH HHS"],"pagination":["100215"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8942843"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(4)"],"pubmed_abstract":["Syntrophus aciditrophicus is a model syntrophic bacterium that degrades fatty and aromatic acids into acetate, CO<sub>2</sub>, formate, and H<sub>2</sub> that are utilized by methanogens and other hydrogen-consuming microbes. S. aciditrophicus benzoate degradation proceeds by a multistep pathway with many intermediate reactive acyl-coenzyme A species (RACS) that can potentially N<sup>ε</sup>-acylate lysine residues. Herein, we describe the identification and characterization of acyl-lysine modifications that correspond to RACS in the benzoate degradation pathway. The amounts of modified peptides are sufficient to analyze the post-translational modifications without antibody enrichment, enabling a range of acylations located, presumably, on the most extensively acylated proteins throughout "],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation."],"pmcid":["PMC8942843"],"funding_grant_id":["R01 GM104610","R01 GM085402","T32 GM007185"],"pubmed_authors":["Fu JY","Nguyen HH","McInerney MJ","Loo JA","Gunsalus RP","Wofford NQ","James KL","Ogorzalek Loo RR","Mouttaki H","Muroski JM"],"additional_accession":[]},"is_claimable":false,"name":"The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation.","description":"Syntrophus aciditrophicus is a model syntrophic bacterium that degrades fatty and aromatic acids into acetate, CO<sub>2</sub>, formate, and H<sub>2</sub> that are utilized by methanogens and other hydrogen-consuming microbes. S. aciditrophicus benzoate degradation proceeds by a multistep pathway with many intermediate reactive acyl-coenzyme A species (RACS) that can potentially N<sup>ε</sup>-acylate lysine residues. Herein, we describe the identification and characterization of acyl-lysine modifications that correspond to RACS in the benzoate degradation pathway. The amounts of modified peptides are sufficient to analyze the post-translational modifications without antibody enrichment, enabling a range of acylations located, presumably, on the most extensively acylated proteins throughout ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-30T20:58:48.334Z","creation":"2025-04-04T10:01:37.566Z"},"accession":"S-EPMC8942843","cross_references":{"pubmed":["35189333"],"doi":["10.1016/j.mcpro.2022.100215"]}}