Mechanism of autolysis of Neisseria gonorrhoeae.
The major autolysin(s) of Neisseria 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 (EC 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).
D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism; D001433:Bacteriolysis; D002474:Cell-Free System; D003960:Diaminopimelic Acid / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D009344:Neisseria gonorrhoeae / Q000201:enzymology / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism; D011092:Polyethylene Glycols / Q000494:pharmacology; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature
D010457:Peptidoglycan; D011092:Polyethylene Glycols; D012965:Sodium Chloride; D003960:Diaminopimelic Acid; D011189:Potassium Chloride; D000581:Amidohydrolases