Mechanism of autolysis of Neisseria gonorrhoeae

Abstract

The major autolysin(s) of N. gonorrhoeae was solubilized from envelopes by extraction with 2% Triton X 100 containing 0.5 M NaCl. Neither Triton X 100 nor NaCl alone could effectively release the autolysin(s). The major autolysin is N acetylmuramyl L alanine amidase (E.C. 3.5.1.28). The pH optimum for this reaction was broad, ranging from 5.5 to 8.5. Optimal hydrolysis of peptidoglycan occurred in 2% Triton X 100 in 0.1 M KCl. Attempts to purify the autolysin were unsuccessful. A rapid assay for enzyme activity was developed using radioactive cell walls as a substrate ([3H]diaminopimelic acid).