Molecular weight-determination of biosynthetically modified monomeric and oligomeric muropeptides from Escherichia coli by plasma desorption-mass spectrometry.

The presence of certain D-amino acids in the growth media of Escherichia coli results in the accumulation of 2 major and 3-5 minor new muropeptides in the murein sacculus. Preliminary data suggested that the major muropeptides correspond to a monomer and a cross-linked dimer with one residue of D-amino acid per molecule. We have analyzed several D-amino acid-modified muropeptides by plasma desorption-mass spectrometry. Our results confirmed that the general structures of the major modified muropeptides are: GlucNAc-MurNAc-L-Ala-D-Glu-m-A2pm-D-X, and GlucNAc-MurNAc-L-Ala-D-Glu-m-A2pm-D-Ala; GlucNAc-MurNAc-L-Ala-D-Glu-m-A2pm-D-X, being X a residue of the D-amino acid. These results corroborate the usefulness of this technique for the structural analysis of muropeptides.