The amino acid sequence of the peptide moiety of the pseudomurein from Methanobacterium thermoautotrophicum

Abstract

The amino acid sequence of the peptide subunits of the peptide moiety of the sacculus polymer (pseudomurein) of Methanobacterium thermoautotrophicum was elucidated by analysing overlapping peptides obtained from partial acid hydrolsates of isolated sacculi. It is suggested that the peptide subunits are attached to glycan strands via one of their glutamyl residues. Another glutamyl residue may crosslink two adjacent peptide subunits to form a dimer. The calculated molar ratios of the amino acids and the percentages of the N- or C-terminal amino acid residues of the supposed dimers are compatible with those actually found in the sacculus polymer.