Structure and synthesis of a lipid-containing bacteriophage. An endolysin activity associated with bacteriophage PM2.
Endolysin was induced in Pseudomonas BAL-31 infected with bacteriophage PM2 and was also associated with the purified virion. This enzyme required divalent cations for its activity, Ca2+ being the most effective cation. Endolysin activity in the virion increased up to three-fold upon disruption and the activity could be localized in the viral nucleocapsid. Thus the enzyme is localized within the virion. After purification of the structural proteins of bacteriophage PM2, only the nucleocapsid protein (III) had endolysin activity.
D001433:Bacteriolysis; D001435:Bacteriophages / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D002413:Cations, Divalent; D004790:Enzyme Induction / Q000187:drug effects; D007700:Kinetics; D010447:Peptide Hydrolases / Q000096:biosynthesis*; D010457:Peptidoglycan; D011549:Pseudomonas / Q000201:enzymology*
D002413:Cations, Divalent; D010457:Peptidoglycan; D010447:Peptide Hydrolases; D002118:Calcium