Conserved residues Glu37 and Trp229 play an essential role in protein folding of β-lactamase.

ABSTRACT: Evolutionary robustness requires that the number of highly conserved amino acid residues in proteins is minimized. In enzymes, such conservation is observed for catalytic residues but also for some residues in the second shell or even further from the active site. β-Lactamases evolve in response to changing antibiotic selection pressures and are thus expected to be evolutionarily robust, with a limited number of highly conserved amino acid residues. As part of the effort to understand the roles of conserved residues in class A β-lactamases, we investigate the reasons leading to the conservation of two amino acid residues in the β-lactamase BlaC, Glu37, and Trp229. Using site-directed mutagenesis, we have generated point mutations of these residues and observed a drastic decrease in the lev

SUBMITTER: Chikunova A 

PROVIDER: S-EPMC8518976 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature