Peptidoglycan-degrading Enzymes in Ether-treated Cells of Neisseria gonorrhoeae

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Abstract
The incubation of peptidoglycan fragments with ether-treated cells of N. gonorrhoeae resulted in breakdown products that showed the presence of previously undescribed lytic enzymes. The properties of an endopeptidase able to hydrolyze peptide-linked bis-disaccharide peptide dimer to monomer units were examined. An exo-N-acetyl-glucosaminidase was also shown to release free N-acetylglucosamine. The breakdown pattern of glycosidically-linked dimer indicated the existence of an endo-N-acetylglucosaminidase. The activities of the latter enzyme and of the endopeptidase were both sensitive to .beta.-lactam antibiotic.