Goffin C, Ayala J A, Nguyen-Distèche M, Ghuysen J M
Centre d'Ingénierie des Protéines, Université de Liège, Belgium.
FEMS Microbiol Lett. 1993 Nov 1;113(3):247-51. doi: 10.1111/j.1574-6968.1993.tb06522.x.
The glutamic acid E396, aspartic acid D409 and glutamic acid E411 residues of the Escherichia coli penicillin-binding protein 3 were each converted into an alanine residue. As deduced from penicillin-binding and complementation experiments, none of these dicarboxylic acid residues is involved in the mechanism of acylation by penicillin and none of them is essential for the in vivo functioning of the PBP. The mutation E396, however, causes an increased thermolability of the protein.
将大肠杆菌青霉素结合蛋白3的谷氨酸E396、天冬氨酸D409和谷氨酸E411残基分别转化为丙氨酸残基。从青霉素结合和互补实验推断，这些二羧酸残基均不参与青霉素的酰化机制，且它们对PBP的体内功能均非必需。然而，E396突变导致该蛋白的热稳定性增加。
