title: An osmotically fragile mutant of Bacillus subtilis with an active membrane-associated phospholipase A 1 .
abstract: By use of a newly developed procedure for the isolation of mutants with osmotically fragile protoplasts, a mutant of Bacillus subtilis was isolated that has a very active enzyme system for the catabolism of phospholipids via the sequential action of a phospholipase A(1) (EC 3.1.1.4) and a lysophospholipase (EC 3.1.1.5). The wild-type bacteria contain no detectable phospholipase A(1) activity, but do contain a protein that specifically inhibits the phospholipase A(1) in the mutant. This protein may play an important role in the control of phospholipid catabolism.
mesh_terms: D000818:Animals; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology*; D002854:Chromatography, Paper; D002855:Chromatography, Thin Layer; D003470:Culture Media; D007532:Isoleucine / Q000378:metabolism; D007930:Leucine / Q000378:metabolism; D050356:Lipid Metabolism; D008055:Lipids / Q000096:biosynthesis; D009113:Muramidase / Q000378:metabolism; D009154:Mutation; D009996:Osmotic Fragility; D010740:Phospholipases / Q000378:metabolism*; D010759:Phosphorus Isotopes; D012911:Snakes; D014316:Tritium; D014688:Venoms
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D008055:Lipids; D010759:Phosphorus Isotopes; D014688:Venoms; D007532:Isoleucine; D014316:Tritium; D010740:Phospholipases; D009113:Muramidase; D007930:Leucine