Chemical proteomics enhances the understanding of 2AA stress in <i>Salmonella enterica</i>.

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, Salmonella enterica 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 in vivo and in vitro. 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

SUBMITTER: Schum D 

PROVIDER: S-EPMC12172467 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature