Characterization of the autolytic enzymes of Clostridium perfringens.
Clostridium perfringens and isolated walls of this organism autolysed rapidly when incubated in buffer at pH 7.0 with the release of free-reducing groups but no N-terminal amino acids. The predominant autolytic enzyme was an endo-beta-N-acetylglucosaminidase, and an endo-beta-N-acetylmuramidase was also present. The autolytic enzymes could be solubilized by extraction of the organisms with 5 M-LiCl and would then subsequently bind to and rapidly lyse walls of Micrococcus luteus and, more slowly, formamide-extracted walls of C. perfringens and walls of Bacillus subtilis. Lysis of C. perfringens walls by these extracted enzymes could not be demonstrated.
D000118:Acetylglucosaminidase / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D003016:Clostridium perfringens / Q000201:enzymology* / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D009113:Muramidase / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism
D011134:Polysaccharides; D006026:Glycoside Hydrolases; D009113:Muramidase; D000118:Acetylglucosaminidase