title: Peptidoglycan hydrolases in an autolytic mutant of Salmonella typhimurium.
abstract: Two peptidoglycan hydrolases were isolated from the autolytic mutant Salmonella typhimurium DA361 (envD). One of them, resistant to penicillin, was found free in the supernatant of partially purified envelopes sedimented by ultracentrifugation, and the other bound to the envelopes proved to be sensitive to the antibiotic. Both were able to hydrolyse in vitro high molecular weight non-specific peptidoglycan isolated from E. coli W7 labelled with [14C]diaminopimelic acid. Similar enzymatic activities were separated also from S. typhimurium DA362 (envD+) a non-lytic isogenic pair of the above and from the wild type strain LT-2. All of the hydrolytic activities reported here were strongly inhibited when DNA was added to the assay systems. The peptidoglycan hydrolases isolated from the autolytic mutant suffered a competitive inhibition while those from the non-lytic strains were apparently inhibited in uncompetitive modal relationship. It is postulated that the inhibitory effect may bear affinity with the preservation of DNA sites of attachment to cell membranes sustaining peptidoglycan structure and functions.
authors: Departamento de Radiobiología, Comisión Nacional de Energía Atómica, Buenos Aires, Argentina.
authors: R A
authors: RA
authors: Pizarro
authors: R O
authors: RO
authors: Fernández
authors: L V
authors: LV
authors: Orce
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D001329:Autolysis; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000235:genetics
chemical_list: D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase