青霉素和头孢菌素对铜绿假单胞菌和大肠杆菌中肽聚糖转肽酶的抑制作用。
Peptidoglycan transpeptidase inhibition in Pseudomonas aeruginosa and Escherichia coli by Penicillins and Cephalosporins.
作者信息
Moore B A, Jevons S, Brammer K W
出版信息
Antimicrob Agents Chemother. 1979 Apr;15(4):513-7. doi: 10.1128/AAC.15.4.513.
Abstract
Peptidoglycan transpeptidase activity has been studied in cells of Escherichia coli 146 and Pseudomonas aeruginosa 56 made permeable to exogenous, nucleotide-sugar peptidoglycan precursors by ether treatment. Transpeptidase activity was inhibited, in both organisms, by a range of penicillins and cephalosporins, the Pseudomonas enzyme being more sensitive to inhibition in each case. Conversely, growth of E. coli 146 was more susceptible to these antibiotics than growth of P. aeruginosa 56. Furthermore, similar transpeptidase inhibition values were ob-obtained for the four penicillins examined against the Pseudomonas enzyme, although only two of these (carbenicillin and pirbenicillin) inhibited the growth of this organism. We therefore conclude that the high resistance of P. aeruginosa 56 to growth inhibition by most beta-lactam antibiotics cannot be due to an insensitive peptidoglycan transpeptidase.
摘要
已在经乙醚处理对外源核苷酸糖肽聚糖前体具有通透性的大肠杆菌146和铜绿假单胞菌56的细胞中研究了肽聚糖转肽酶活性。在这两种生物体中，一系列青霉素和头孢菌素均抑制转肽酶活性，在每种情况下铜绿假单胞菌的酶对抑制更为敏感。相反，大肠杆菌146的生长比铜绿假单胞菌56的生长对这些抗生素更敏感。此外，针对铜绿假单胞菌的酶检测的四种青霉素获得了相似的转肽酶抑制值，尽管其中只有两种（羧苄青霉素和匹氨西林）抑制了该生物体的生长。因此，我们得出结论，铜绿假单胞菌56对大多数β-内酰胺抗生素生长抑制的高抗性并非由于肽聚糖转肽酶不敏感所致。
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