ArticleThe Journal of biological chemistry2022
2-Aminoacrylate stress damages diverse PLP-dependent enzymes in vivo.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Terminal alkyne formation by a pyridoxal phosphate-dependent enzyme.Nature chemical biology · 2026Article
- The mechanism of thioamide formation by the YcfA-YcfC system in 6-thioguanine biosynthesis.Nature communications · 2025Article
- Isoleucine Binding and Regulation ofBiochemistry · 2025Article
- Article
- Perturbation of the MetJ regulon impacts the consequences of 2-aminoacrylate stress inMicrobiology (Reading, England) · 2025Article
- Site-directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus.Protein science : a publication of the Protein Society · 2024Article
- Discovery and Characterization of Pyridoxal 5'-Phosphate-Dependent Cycloleucine Synthases.Journal of the American Chemical Society · 2024Article
- Tetrahydrofolate levels influence 2-aminoacrylate stress inJournal of bacteriology · 2024Article
- RidA proteins contribute to fitness ofMicrobial cell (Graz, Austria) · 2024Article
- A metabolic map of the DNA damage response identifies PRDX1 in the control of nuclear ROS scavenging and aspartate availability.Molecular systems biology · 2023Article
- Modulators of a robust and efficient metabolism: Perspective and insights from the Rid superfamily of proteins.Advances in microbial physiology · 2023Review
- His-163 is a stereospecific proton donor in the mechanism of d-glucosaminate-6-phosphate ammonia-lyase.FEBS letters · 2022Article
- Article
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3 authors.
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Abstract
Pyridoxal 5'-phosphate (PLP) is an essential cofactor for a class of enzymes that catalyze diverse reactions in central metabolism. The catalytic mechanism of some PLP-dependent enzymes involves the generation of reactive enamine intermediates like 2-aminoacrylate (2AA). 2AA can covalently modify PLP in the active site of some PLP-dependent enzymes and subsequently inactivate the enzyme through the formation of a PLP-pyruvate adduct. In the absence of the enamine/imine deaminase RidA, Salmonella enterica experiences 2AA-mediated metabolic stress. Surprisingly, PLP-dependent enzymes that generate endogenous 2AA appear to be immune to its attack, while other PLP-dependent enzymes accumulate damage in the presence of 2AA stress; however, structural determinants of 2AA sensitivity are unclear. In this study, we refined a molecular method to query proteins from diverse systems for their sensitivity to 2AA in vivo. This method was then used to examine active site residues of Alr, a 2AA-sensitive PLP-dependent enzyme, that affect its sensitivity to 2AA in vivo. Unexpectedly, our data also showed that a low level of 2AA stress can persist even in the presence of a functional RidA. In summary, this study expands our understanding of 2AA metabolism and takes an initial step toward characterizing the structural determinants influencing enzyme susceptibility to damage by free 2AA.
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