Abstract
The involvement of the serine residue 318 in the specificity of a class C β-lactamase was investigated. Multiple site-directed mutants at this position were generated using a polymerase chain reaction technique. These mutants were then probed for their activity towards various β-lactam compounds. One mutant, S318G was further purified and its physico-chemical and catalytic properties determined. It was shown that the observed minimal inhibitory concentration values of this mutant could be correlation to its kinetic properties using a ‘diffusion-hydrolysis’ model. However, the data showed that residue 318 has little influence on the specificity of class C β-lactamases.
Published Version
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