Purification and properties of a bacteriophage-induced cell wall peptidase from Staphylococcus aureus.
A phage-induced cell wall solubilizing enzyme isolated from phage-infected Staphylococcus aureus phage type 80 was purified 588-fold. The pH optimal activity was 6.8 to 7.3, and pH optimal stability, 6.5 to 7.5. It was inhibited by p-hydroxymercuribenzoate, ethylenediaminetetraacetic acid, and specific rabbit antisera. The cell wall lytic reaction is a peptidase resulting in cleavage of the cell wall peptide at N-terminal alanine, glutamic acid, and glycine. Electron micrographs are shown of cell wall "ghosts" remaining after the enzymatic digestion of cell walls.
D001433:Bacteriolysis; D002473:Cell Wall / Q000187:drug effects*; D004790:Enzyme Induction; D004798:Enzymes / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D010447:Peptide Hydrolases / Q000096:biosynthesis*; D013210:Staphylococcus / Q000201:enzymology*; D013204:Staphylococcus Phages / Q000378:metabolism*
D004798:Enzymes; D010447:Peptide Hydrolases