Abstract
The amino acid sequence of the peptide moiety of the mureins of Lactobacillus coryniformis and Lactobacillus cellobiosus cell walls was determined. This was accomplished by the identification of peptides obtained after partial hydrolysis of purified cell walls and by the identification of UDP-activated murein precursors accumulated by ᴅ-cycloserine inhibition. The amino acid sequence proved to be : ʟ-ala-ᴅ-glu-ʟ-lys-ᴅ-ala for L. coryniformis and L-ala-D-glu-L-orn-D-ala for L. cellobio-. D-asp D-asp sus. Aspartic acid is involved in the cross-linking of the mureins by forming a peptide bond with the C-terminal D-alanine of an adjacent muropeptide. Glutamic acid as well as aspartic acid are present as amides.