Specificity of a bacteriolytic enzyme from Pseudomonas aeruginosa.
A bacteriolytic enzyme isolated from shake-flask cultures of Pseudomonas aeruginosa and capable of lysing cells of Staphylococcus aureus was purified approximately 500-fold by passage through diethylaminoethyl cellulose and chromatography on carboxymethyl-cellulose. The purified enzyme was shown to act as an endopeptidase, cleaving the pentaglycine cross-bridges of the cell wall peptidoglycan at d-alanyl-glycine and glycyl-glycine linkages with the release of di-, tri-, and tetraglycine fragments. Release of NH(2)-alanine indicated weak N-acetylmuramyl-l-alanine amidase activity, but most of the residual peptide remained attached to the glycan. No hydrolysis of the glycan occurred. The lytic spectrum of the enzyme toward a variety of other cell walls of known peptidoglycan composition indicated relatively high specificity for peptidoglycans with polyglycine bridges.
D000619:Aminohydrolases / Q000032:analysis; D001433:Bacteriolysis; D002473:Cell Wall; D002845:Chromatography; D010447:Peptide Hydrolases / Q000032:analysis; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013210:Staphylococcus
D010447:Peptide Hydrolases; D000619:Aminohydrolases