<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Muroski JM</submitter><funding>NIGMS NIH HHS</funding><pagination>100215</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8942843</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>21(4)</volume><pubmed_abstract>Syntrophus aciditrophicus is a model syntrophic bacterium that degrades fatty and aromatic acids into acetate, CO&lt;sub>2&lt;/sub>, formate, and H&lt;sub>2&lt;/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&lt;sup>ε&lt;/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 </pubmed_abstract><journal>Molecular &amp; cellular proteomics : MCP</journal><pubmed_title>The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation.</pubmed_title><pmcid>PMC8942843</pmcid><funding_grant_id>R01 GM104610</funding_grant_id><funding_grant_id>R01 GM085402</funding_grant_id><funding_grant_id>T32 GM007185</funding_grant_id><pubmed_authors>Fu JY</pubmed_authors><pubmed_authors>Nguyen HH</pubmed_authors><pubmed_authors>McInerney MJ</pubmed_authors><pubmed_authors>Loo JA</pubmed_authors><pubmed_authors>Gunsalus RP</pubmed_authors><pubmed_authors>Wofford NQ</pubmed_authors><pubmed_authors>James KL</pubmed_authors><pubmed_authors>Ogorzalek Loo RR</pubmed_authors><pubmed_authors>Mouttaki H</pubmed_authors><pubmed_authors>Muroski JM</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation.</name><description>Syntrophus aciditrophicus is a model syntrophic bacterium that degrades fatty and aromatic acids into acetate, CO&lt;sub>2&lt;/sub>, formate, and H&lt;sub>2&lt;/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&lt;sup>ε&lt;/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 </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Apr</publication><modification>2026-05-30T20:58:48.334Z</modification><creation>2025-04-04T10:01:37.566Z</creation></dates><accession>S-EPMC8942843</accession><cross_references><pubmed>35189333</pubmed><doi>10.1016/j.mcpro.2022.100215</doi></cross_references></HashMap>