{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schum D"],"funding":["National Institutes of Health","NIGMS NIH HHS","NIH HHS"],"pagination":["e0054025"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12172467"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(6)"],"pubmed_abstract":["Pyridoxal 5'-phosphate (PLP) is an essential cofactor for enzymes that catalyze diverse reactions in central metabolism. 2-Aminoacrylate (2AA) is a reactive enamine and an obligate catalytic intermediate in some PLP-mediated reactions. In the absence of the enamine/imine deaminase RidA, <i>Salmonella enterica</i> accumulates 2AA, which causes cellular stress. 2AA can attack PLP in the active site of some enzymes and covalently inactivate them by forming a 2AA-PLP adduct, which has already been characterized for some target enzymes <i>in vivo</i> and <i>in vitro</i>. The mechanism of 2AA attack suggests that a majority of cellular PLP-DEs would be targets of 2AA damage. Herein, a chemical proteomics workflow that uses PL (pyridoxal) probes to enrich PLP-DEs with a click chemistry-based prot"],"journal":["mSystems"],"pubmed_title":["Chemical proteomics enhances the understanding of 2AA stress in &lt;i&gt;Salmonella enterica&lt;/i&gt;."],"pmcid":["PMC12172467"],"funding_grant_id":["RO1GM095837","R35 GM153189","R35GM153189","R01 GM095837"],"pubmed_authors":["Schum D","Sieber SA","Fiedler MK","Shen W","Downs DM"],"additional_accession":[]},"is_claimable":false,"name":"Chemical proteomics enhances the understanding of 2AA stress in &lt;i&gt;Salmonella enterica&lt;/i&gt;.","description":"Pyridoxal 5'-phosphate (PLP) is an essential cofactor for enzymes that catalyze diverse reactions in central metabolism. 2-Aminoacrylate (2AA) is a reactive enamine and an obligate catalytic intermediate in some PLP-mediated reactions. In the absence of the enamine/imine deaminase RidA, <i>Salmonella enterica</i> accumulates 2AA, which causes cellular stress. 2AA can attack PLP in the active site of some enzymes and covalently inactivate them by forming a 2AA-PLP adduct, which has already been characterized for some target enzymes <i>in vivo</i> and <i>in vitro</i>. The mechanism of 2AA attack suggests that a majority of cellular PLP-DEs would be targets of 2AA damage. Herein, a chemical proteomics workflow that uses PL (pyridoxal) probes to enrich PLP-DEs with a click chemistry-based prot","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-03T07:08:42.575Z","creation":"2026-04-25T03:22:19.817Z"},"accession":"S-EPMC12172467","cross_references":{"pubmed":["40439409"],"doi":["10.1128/msystems.00540-25"]}}