Zur Biosynthese des formgebenden Elements der Bakterienzellwand

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Abstract
Two stages in murein biosynthesis (the partial degradation of the preexistent murein and the neosynthesis immediately following it under normal conditions) can be separated by 2,6-diaminopimelic acid (DAP) starvation of the DAP-dependent mutant of Escherichia coli W 173-25. The degradation of murein growing cells was studied in order to investigate the function of murein hydrolases in murein biosynthesis. A muramylendopeptidase may be important in the process. The activity of this enzyme is revealed by a conversion of the cells into spheroplasts during DAP starvation. A hypothesis concerning the insertion of new murein moieties due to transpeptidation by this enzyme is discussed.