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pubmed:abstractText |
In a study of the mureins of coryneform bacteria (Arthrobacter, Brevibacterium, Cellulomonas, Corynebacterium, Erysipelothrix), 21 threonine-containing strains were found. In several of the strains the amino acid and amino sugar composition of the murein was muramic acid (Mur), glucosamine (GlcNH(2)), d-Glu, l-Lys, l-Thr, and Ala in a molar ratio of 1:1:1:1:1:4 or 5, and in several other strains it was Mur, GlcNH(2), d-Glu, l-Lys, l-Thr, Ala, and l-Ser in a molar ratio of 1:1:1:1:1:3:1. The amino acid sequence of the mureins was determined by analyzing the oligopeptides derived from partial acid hydrolysates. It was shown that there were five different murein types. The peptide subunits attached to the muramic acid are the same, namely l-Ala-d-GluNH(2)-l-Lys-d-Ala. In one strain, the alpha-carboxyl group of d-Glu is substituted by d-alanine amide. The interpeptide bridges of the different types consist of the peptides l-Ala-l-Thr-l-Ala, l-Ala-l-Thr, l-Ala-l-Ala-l-Thr, l-Ala-l-Ala-l-Ala-l-Thr, or l-Ala-l-Thr-l-Ser which are bound through their C-termini (l-Ala, l-Thr, l-Ser) to the epsilon-amino group of l-Lys of one peptide subunit and by their N-termini (l-Ala) to the C-terminal d-Ala of an adjacent peptide subunit. Determination of the N- and C-terminal groups in the mureins showed that about 15 to 30% of the interpeptide bridges are not cross-linked.
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