title: Studies on bacterial cell wall inhibitors. X. Properties of phosph-N-acetylmuramoyl-pentapeptide-transferase in peptidoglycan synthesis of Bacillus megaterium and its inhibition by amphomycin.
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.
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001410:Bacillus megaterium / Q000378:metabolism*; D002473:Cell Wall / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D055666:Lipopeptides; D008274:Magnesium / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology; D010457:Peptidoglycan / Q000096:biosynthesis*; D010770:Phosphotransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013997:Time Factors; D014542:Uridine Monophosphate / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D055666:Lipopeptides; D009842:Oligopeptides; D010457:Peptidoglycan; C004423:amphomycin; D000255:Adenosine Triphosphate; D014542:Uridine Monophosphate; D010770:Phosphotransferases; D008274:Magnesium