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Autolytic Enzyme Associated with Cell Walls of Bacillus subtilis

From the ¹ From the Department of Pathology, Western Reserve University, Cleveland, Ohio 44106, and Divisions of Microbiology and Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California 92037

Autolysis of cell walls of the highly transformable strain 168 of Bacillus subtilis is accompanied by the release of N-terminal L-alanine without a concomitant release of C-terminal amino acids, reducing groups, or phosphomonoester groups. These observations show that the enzyme is an N-acylmuramyl-L-alanine amidase. Autolysis follows first order kinetics, requires an energy of activation of 9.2 kcal per mole, and results in the hydrolysis of 87% of the amide bonds between muramic acid and L-alanine. Since the enzyme is most active during logarithmic growth of the population, it is suggested that its action coupled with a transpeptidase is involved in the expansion of the cell wall.

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