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• W2076934723 abstract "The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts containing non-α-lysine substrates of PoxA modified EF-P with a change in mass consistent with addition of β-lysine, a substrate also predicted by genomic analyses. EF-P was efficiently functionally modified with (R)-β-lysine but not (S)-β-lysine or genetically encoded α-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases." @default.
• W2076934723 created "2016-06-24" @default.
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• W2076934723 date "2011-08-14" @default.
• W2076934723 modified "2023-10-14" @default.
• W2076934723 title "The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine" @default.
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• W2076934723 doi "https://doi.org/10.1038/nchembio.632" @default.
• W2076934723 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3177975" @default.
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