Chapman S J, Perkins H R
J Gen Microbiol. 1983 Mar;129(3):877-83. doi: 10.1099/00221287-129-3-877.
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.
将肽聚糖片段与经乙醚处理的淋病奈瑟菌细胞一起温育，产生了一些降解产物，这些产物表明存在以前未描述的裂解酶。对一种能够将肽连接的双二糖肽二聚体水解为单体单元的内肽酶的特性进行了研究。还发现一种外切N-乙酰葡糖胺酶能够释放游离的N-乙酰葡糖胺。糖苷连接的二聚体的降解模式表明存在一种内切N-乙酰葡糖胺酶。后一种酶和内肽酶的活性均对β-内酰胺抗生素敏感。
