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Metabolic Profiling of Bacteria by Unnatural C‐terminated D ‐Amino Acids
Author(s) -
Pidgeon Sean E.,
Fura Jonathan M.,
Leon William,
Birabaharan Morgan,
Vezenov Dmitri,
Pires Marcos M.
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201409927
Subject(s) - peptidoglycan , bacterial cell structure , amino acid , chemistry , cell wall , bacteria , biochemistry , oligopeptide , peptide , stereochemistry , biology , genetics
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.