一种青霉素结合蛋白5有缺陷且缺乏D-丙氨酸羧肽酶IA的大肠杆菌突变体。
A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking D-alanine carboxypeptidase IA.
作者信息
Nishimura Y, Suzuki H, Hirota Y, Park J T
出版信息
J Bacteriol. 1980 Jul;143(1):531-4. doi: 10.1128/jb.143.1.531-534.1980.
Abstract
A mutant of Escherichia coli defective in penicillin-binding protein 5 activity was isolated. The mutation (pfv) was shown to be located at 14.0 min on the E. coli chromosome map. Loss of penicillin-binding protein 5 in the pfv mutant was associated with the loss of D-alanine carboxypeptidase IA activity and increased sensitivity to beta-lactam antibiotics. We conclude that penicillin-binding protein 5 catalyzes the major D-alanine carboxypeptidase IA activity and that the enzyme activity, in vivo, protects E. coli cells from killing by low inhibitory concentrations of beta-lactam antibiotics.
摘要
分离出一株青霉素结合蛋白5活性有缺陷的大肠杆菌突变体。该突变（pfv）位于大肠杆菌染色体图谱上的14.0分钟处。pfv突变体中青霉素结合蛋白5的缺失与D-丙氨酸羧肽酶IA活性的丧失以及对β-内酰胺抗生素敏感性的增加有关。我们得出结论，青霉素结合蛋白5催化主要的D-丙氨酸羧肽酶IA活性，并且该酶活性在体内可保护大肠杆菌细胞免受低抑制浓度β-内酰胺抗生素的杀伤。
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