Autolytic enzyme associated with cell walls of Bacillus subtilis.

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