STUDIES ON BACTERIAL CELL WALL INHIBITORS X. PROPERTIES OF PHOSPHO-<i>N</i>-ACETYLMURAMOYL- PENTAPEPTIDE-TRANSFERASE IN PEPTIDOGLYCAN SYNTHESIS OF <i>BACILLUS MEGATERIUM</i> AND ITS INHIBITION BY AMPHOMYCIN

HARUO TANAKA; RUIKO OIWA; SHIGEKAZU MATSUKURA; JUNJI INOKOSHI; SATOSHI OMURA

doi:10.7164/antibiotics.35.1216

STUDIES ON BACTERIAL CELL WALL INHIBITORS

X. PROPERTIES OF PHOSPHO-N-ACETYLMURAMOYL- PENTAPEPTIDE-TRANSFERASE IN PEPTIDOGLYCAN SYNTHESIS OF BACILLUS MEGATERIUM AND ITS INHIBITION BY AMPHOMYCIN

HARUO TANAKA, RUIKO OIWA, SHIGEKAZU MATSUKURA, JUNJI INOKOSHI, SATOSHI OMURA

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JOURNAL FREE ACCESS

1982 Volume 35 Issue 9 Pages 1216-1221

DOI https://doi.org/10.7164/antibiotics.35.1216

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Abstract

The phospho-N-acetylmuramoyl-pentapeptide-transferase from Bacillus megaterium KM was characterized by the transfer reaction. The particulate enzyme preparation had the activity to transfer phospho-N-acetylmuramoyl-pentapeptide from UDP-N-acetylmuramoyl-pentapeptide to undecaprenoid-1-ol-phosphate. The optimum pH for activity was about 8.5. The reaction required the presence of Mg²⁺ and an SH-protector. With 25 mM Mg²⁺ the maximum activity was observed. The reaction was reversible and so the addition of UMP decreased the formation of undecaprenoid-1-ol-diphospho-N-acetylmuramoyl-pentapeptide. Amphomycin inhibited non-competitively the transferase for the substrate UDP-N-acetylmuramoyl-pentapeptide.

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