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• W2115315693 abstract "Bacterial peptidoglycan is a mesh-like network comprised of sugars and oligopeptides. Transpeptidases cross-link peptidoglycan oligopeptides to provide vital cell wall rigidity and structural support. It was recently discovered that the same transpeptidases catalyze the metabolic incorporation of exogenous D-amino acids onto bacterial cell surfaces with vast promiscuity for the side-chain identity. It is now shown that this enzymatic promiscuity is not exclusive to side chains, but that C-terminus variations can also be accommodated across a diverse range of bacteria. Atomic force microscopy analysis revealed that the incorporation of C-terminus amidated D-amino acids onto bacterial surfaces substantially reduced the cell wall stiffness. We exploited the promiscuity of bacterial transpeptidases to develop a novel assay for profiling different bacterial species." @default.
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• W2115315693 date "2015-04-01" @default.
• W2115315693 modified "2023-09-30" @default.
• W2115315693 title "Metabolic Profiling of Bacteria by Unnatural C-terminated<scp>D</scp>-Amino Acids" @default.
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• W2115315693 doi "https://doi.org/10.1002/anie.201409927" @default.
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