The nucleotide precursors of cell-wall mucopeptide were prepared by vancomycin inhibition of Corynebacterium insidiosum and Corynebacterium poinsettiae. The amino acid in the third position in the former peptide was shown by optical rotatory dispersion of the bisdinitrophenyl derivative to be l-diaminobutyric acid. Homoserine in the nucleotide from C. poinsettiae was catalytically oxidized to aspartic acid, which was then shown to be the l-isomer by optical rotatory dispersion of the trinitrophenyl compound. The sequence for C. insidiosum was UDP-N-acetylmuramyl-glycyl-isoglutamyl- (γ-acetyl)-diaminobutyryl-alanyl-alanine. The cell walls of C. insidiosum and Corynebacterium sepedonicum contained diaminobutyric acid that was optically inactive. It is proposed, therefore, that the primary peptide chain contains the l-isomer with its γ-amino group blocked by acetylation and that cross-linking is achieved by means of the d-isomer, analogous to d-ornithine in C. poinsettiae.

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