Die Wirkung von d-Aminosäuren auf die Struktur und Biosynthese des Peptidoglycans

Translated title of the contribution: Mode of action of d-amino acids on the biosynthesis of peptidoglycan

Bernd Trippen, Walter P. Hammes, Karl Heinz Schleifer, Otto Kandler

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


The mechanism of growth inhibition by d-amino acids was studied. d-Serine at concentrations from 0.02-0.2 M was sufficient to cause partial growth inhibition in seven species of bacteria representing the four most common types of peptidoglycan. The inhibited cells displayed morphological alterations. In the nucleotide-activated peptidoglycan precursors of these cells, d-alanine residues in position 4 and/or 5 of the peptide moiety were partially or even completely replaced by d-serine. The peptidoglycan also contained d-serine instead of d-alanine, but the percentual content of d-serine was significantly lower than that in the precursors. In addition, the modified peptidoglycan was less cross-linked than the normal one. Four other d-amino acids (d-threonine, d-valine, d-leucine, d-methionine) at concentrations of about 0.2 M caused similar effects as did d-serine when applied to Corynebacterium callunae and Bacillus subtilis. Thus the mode of action of d-amino acids on peptidoglycan synthesis can be generally described as follows: in their presence, at growth inhibiting concentrations modified nucleotide-activated peptidoglycan precursors are formed in which d-alanine residues are replaced by the d-amino acids. They are less efficiently incorporated into peptidoglycan. A high percentage of the modified muropeptides remains non-cross-linked, since they are poor substrates for the transpeptidation reaction. In the majority of the organisms, cross-linking was decreased when d-alanine in position 4 of the peptide subunit was replaced, in two organisms (Corynebacterium insidiosum and Staphylococcus aureus) replacement in position 5 was most effective, however. The low extent of crosslinkage is consistent with the morphological aberrations of inhibited cells. In previous studies with glycine, results were described that were in close analogy to those obtained with d-amino acids. However, glycine can replace not only d-alanine residues in position 4 and 5 but also l-alanine in position 1 of the peptide subunit.

Translated title of the contributionMode of action of d-amino acids on the biosynthesis of peptidoglycan
Original languageGerman
Pages (from-to)247-261
Number of pages15
JournalArchives of Microbiology
Issue number3
StatePublished - Sep 1976
Externally publishedYes


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