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A cell wall lytic enzyme has been demonstrated to be a component of the membrane ofBacillus licheniformis NCTC 6346 and anl -form derived from it. The lytic enzyme, characterized as anN -acetylmuramyl-l -alanine amidase, is solubilized from membranes by nonionic detergents. Ionic detergents inactivate the enzyme. In the bacterium the specific activities of amidase andd -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.

N -Acetylmuramyl- l -Alanine Amidase of Bacillus licheniformis and Its l -Form