Peptidoglycan-degrading enzymes in ether-treated cells of Neisseria gonorrhoeae.
The incubation of peptidoglycan fragments with ether-treated cells of Neisseria gonorrhoeae resulted in breakdown products that showed the presence of previously undescribed lytic enzymes. The properties of an endopeptidase able to hydrolyse 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 antibiotics.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism; D004986:Ether / Q000494:pharmacology*; D005019:Ethyl Ethers / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007769:Lactams; D009344:Neisseria gonorrhoeae / Q000187:drug effects / Q000201:enzymology*; D010457:Peptidoglycan / Q000378:metabolism*; D013696:Temperature
D000900:Anti-Bacterial Agents; D005019:Ethyl Ethers; D007769:Lactams; D010457:Peptidoglycan; D004986:Ether; D000118:Acetylglucosaminidase; D010450:Endopeptidases