Amphomycin inhibits phospho-N-acetylmuramyl-pentapeptide translocase in peptidoglycan synthesis of Bacillus. |
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Authors: | H Tanaka R Oiwa S Matsukura S Omura |
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Institution: | 1. Kitasato University, Minato-ku, Tokyo 108, Japan;2. The Kitasato Institute, Minato-ku, Tokyo 108, Japan |
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Abstract: | Amphomycin, a selective inhibitor of peptidoglycan synthesis of bacteria, inhibited the lipid intermediates accumulation and the peptidoglycan synthesis from UDP-N-acetylmuramyl-L-Ala-D-Glu-3H]-meso-Dpm-D-Ala-D-Ala (UDP-MurNAc-pentapeptide) and UDP-N-acetylglucosamine (UDP-GlcNAc) with a particulate fraction from KM, and also inhibited the formation of MurNAc (-pentapeptide)-P-P-lipid in the absence of UDP-GlcNAc. But it did not inhibit the formation of peptidoglycan from MurNAc(-pentapeptide)-P-P-lipid and UDP-GlcNAc with the same system of the organism.Thus, it is concluded that the site of action of amphomycin is phospho-MurNAc-pentapeptide translocase in peptidoglycan synthesis. |
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Keywords: | MurNAc N-acetylmuramyl GlcNAc N-acetylglucosamine Dpm diaminopimelic acid |
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