Induction of bacteriolytic enzyme from pyocinogenic Pseudomonas aeruginosa and its enzymatic properties.
Mitomycin C induced a pyocinogenic Pseudomonas aeruginosa P15 to produce a bacteriolytic enzyme, PR1-lysozyme, together with pyocin R1. No significant accumulation of the enzyme was observed inside the induced cells. The enzyme was partially purified by acrinol treatment and Amberlie CG-50 column chromatography. The mode of action of the enzyme on the host bacterial cells as well as on Micrococcus lysodeikticus cells or peptidoglycan isolated from Salmonella typhimurium, was compared with that of hen egg-white lysozyme or phage lambda-lysozyme. It is suggested that PR1-lysozyme should be classified as a glycosidase, rather than an amidase or an endopeptidase.
D001433:Bacteriolysis; D004790:Enzyme Induction; D008837:Micrococcus / Q000378:metabolism; D008937:Mitomycins / Q000494:pharmacology*; D009113:Muramidase / Q000096:biosynthesis* / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D011709:Pyocins / Q000096:biosynthesis; D012486:Salmonella typhimurium / Q000378:metabolism
D008937:Mitomycins; D010457:Peptidoglycan; D011709:Pyocins; D009113:Muramidase