A v Schijndel-van Dam

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Five temperature-sensitive lysis mutants were found to possess very low diaminopimelic acid (Dpm) adding enzyme activity in vitro. Murein synthesis at 42 C was impaired, and uridine-5'-diphosphate-N-acetyl-muramyl-l-Ala- d-Glu (UDP-MurNAc-dipeptide) was accumulated. In the presence of NaCl, the mutants could grow at 42 C. NaCl had no influence on the Dpm(More)
The temperature-sensitive Escherichia coli mutant strain ST-640 lyses at the restrictive temperature except when an osmotic stabilizer or a high concentration of d-alanine is present. The presence of dl-alanyl-dl-alanine does not prevent lysis. The rate of murein synthesis, followed in a wall medium, is decreased at both 30 and 42 C. d-Alanyl-d-alanine and(More)
A number of properties of temperature-sensitive mutants in murein synthesis are described. The mutants grow at 30 C but lyse at 42 C. One mutant possesses a temperature-sensitive d-alanyl-d-alanine adding enzyme, has an impaired rate of murein synthesis in vivo at both 30 and 42 C, and contains elevated levels of uridine(More)
Recent literature on the antibiotics enduracidin, moenomycin, prasinomycin, and 11.837 RP suggested an interaction with murein synthesis. Incubation of sensitive strains from Bacillus cereus and Staphylococcus aureus in a "wall medium" containing labeled l-alanine showed that all four antibiotics inhibited the incorporation of alanine into murein and gave(More)
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