A natural polymorphism in beta-lactamase is a global suppressor.

By Wanzhi Huang, Timothy G. Palzkill. 1997

Citations in the corpus

• Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs. (2002, background): “The low-stability ESBLs confer less resistance at higher temperatures, and a secondary substitution (M182T) is often further selected, both naturally and by in vitro evolution, to restore stability.(14,17,26) The model that emerges is summarized in Figure 6.”
• β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein–protein interactions (2002, unknown): “We also created a mutant of the first fragment, BLF[1]MT (M182T), that is known to disrupt an inactive molten-globule intermediate of β-lactamase, reasoning that this mutant could be both more active and metabolically more stabl”