N-acetylmuramyl-L-alanine amidase of Bacillus licheniformis and its L-form.
A cell wall lytic enzyme has been demonstrated to be a component of the membrane of Bacillus licheniformis NCTC 6346 and an l-form derived from it. The lytic enzyme, characterized as an N-acetylmuramyl-l-alanine amidase, is solubilized from membranes by nonionic detergents. Ionic detergents inactivate the enzyme. In the bacterium the specific activities of amidase and d-alanine carboxypeptidase in mesosomes are approximately 65% of those in membranes. Selective transfer of lytic enzyme from nongrowing L-forms, L-form membranes, and protoplasts to added walls occurred after mixing, and 31 to 77% of the enzyme lost from L-form membranes was recovered on the walls. Membranes isolated from L-forms growing in the presence of added walls contained as little as 13% of the amidase found in membranes of a control culture. These results have been interpreted as showing that in vivo the amidase is "bound" to the surface of the bacterial cell membrane in such a location that it can be readily accessible to the cell wall.
D000409:Alanine; D000581:Amidohydrolases / Q000378:metabolism*; D000606:Amino Sugars; D001224:Aspartic Acid / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology* / Q000254:growth & development; D001665:Binding Sites; D002247:Carbon Isotopes; D002268:Carboxypeptidases / Q000378:metabolism; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology; D002473:Cell Wall / Q000201:enzymology; D002499:Centrifugation, Density Gradient; D002855:Chromatography, Thin Layer; D003902:Detergents; D007740:L Forms / Q000201:enzymology* / Q000254:growth & development; D009113:Muramidase / Q000378:metabolism; D011523:Protoplasts / Q000201:enzymology; D013053:Spectrophotometry; D013385:Succinate Dehydrogenase / Q000378:metabolism
D000606:Amino Sugars; D002247:Carbon Isotopes; D003902:Detergents; D001224:Aspartic Acid; D013385:Succinate Dehydrogenase; D009113:Muramidase; D002268:Carboxypeptidases; D000581:Amidohydrolases; D000409:Alanine