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• W2897022918 abstract "This work shows that the BadL protein of Rhodopseudomonas palustris has N- acetyltransferase activity and that this activity is required for the catabolism of benzoate under photosynthetic conditions in this bacterium. R. palustris occupies lignin-rich habitats, making its benzoate-degrading capability critical for the recycling of this important, energy-rich biopolymer. This work identifies the product of the BadL enzyme as acetamidobenzoates, which were needed to derepress genes encoding benzoate-degrading enzymes and proteins of the photosynthetic apparatus responsible for the generation of the proton motive force under anoxia in the presence of light. In short, acetamidobenzoates potentially coordinate the use of benzoate as a source of reducing power and carbon with the generation of a light-driven proton motive force that fuels ATP synthesis, motility, transport, and many other processes in the metabolically versatile bacterium R. palustris ." @default.
• W2897022918 created "2018-10-26" @default.
• W2897022918 creator A5034511623 @default.
• W2897022918 creator A5056279286 @default.
• W2897022918 date "2018-11-07" @default.
• W2897022918 modified "2023-09-26" @default.
• W2897022918 title "Small-Molecule Acetylation Controls the Degradation of Benzoate and Photosynthesis in Rhodopseudomonas palustris" @default.
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• W2897022918 doi "https://doi.org/10.1128/mbio.01895-18" @default.
• W2897022918 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6191541" @default.
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• W2897022918 hasPublicationYear "2018" @default.
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