Purification and characterization of two phage PBSX-induced lytic enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine amidase and an N-acetylmuramidase.
After heat-induction of the defective phage PBSX in a xhi-1479 mutant of Bacillus subtilis 168, the culture lysed rapidly even if the lyt-2 mutation was present (which greatly reduces the amount of the bacterial autolysins). Two lytic enzymes, an N-acetylmuramoyl-L-alanine amidase and an endo-N-acetylmuramidase, were purified from the culture supernatant. The amidase was readily distinguished from the bacterial amidase by its low molecular weight. In addition, it was not inhibited by antibody directed against the bacterial enzyme. These results indicate that PBSX does not rely on the bacterial autolysins to accomplish lysis.
D000581:Amidohydrolases / Q000302:isolation & purification*; D001412:Bacillus subtilis / Q000032:analysis / Q000187:drug effects / Q000201:enzymology*; D001435:Bacteriophages / Q000201:enzymology*; D002473:Cell Wall / Q000032:analysis / Q000187:drug effects; D004790:Enzyme Induction; D006026:Glycoside Hydrolases / Q000302:isolation & purification*; D006595:Hexosamines / Q000032:analysis; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000302:isolation & purification* / Q000494:pharmacology
D006595:Hexosamines; D006026:Glycoside Hydrolases; C026255:endo-N-acetylmuramidase; D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase