Endo-N-acetyl-glucosaminidase from Clostridium perfringens, lytic for cell wall murein of gram-negative bacteria.
An endo-N-acetyl-glucosaminidase which degrades the murein (peptidoglycan) sacculi of the cell walls of Escherichia coli and Spirillum serpens, but not those of Micrococcus lysodeikticus and Sarcina lutea, is present as a contaminant in a "phospholipase C" from Clostridium perfringens. The specificity of enzyme action was elucidated by reduction of liberated glycosidic groups with NaBH(4) and identification of glucosaminol as the reduction product. This finding contradicts previous reports associating cell wall breakdown with specific phospholipase action.
D000217:Acyltransferases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000606:Amino Sugars / Q000032:analysis; D001322:Autoanalysis; D001426:Bacterial Proteins / Q000032:analysis*; D002473:Cell Wall / Q000032:analysis / Q000378:metabolism*; D003016:Clostridium perfringens / Q000201:enzymology*; D004926:Escherichia coli / Q000032:analysis / Q000378:metabolism; D005944:Glucosamine / Q000032:analysis; D008854:Microscopy, Electron; D010740:Phospholipases / Q000378:metabolism; D010783:Photometry
D000596:Amino Acids; D000606:Amino Sugars; D001426:Bacterial Proteins; D000217:Acyltransferases; D010740:Phospholipases; D005944:Glucosamine