Abstract
THE study of protein mutants has proved a powerful technique in the elucidation of structure–function relationships (see for example refs 1 and 2), but this approach has hardly been used strategically in the investigation of enzyme mechanisms, though its potential for clarifying the role of individual amino acids and their effect on catalytic rates is obvious. We report here the consequences of directed selective pressure on the plasmid-coded β-lactamase from Escherichia coli RTEM. Selection for strains with increased resistance to cephalosporin C has allowed the isolation of mutant enzymes whose catalytic properties are changed in the desired direction.
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HALL, A., KNOWLES, J. Directed selective pressure on a β-lactamase to analyse molecular changes involved in development of enzyme function. Nature 264, 803–804 (1976). https://doi.org/10.1038/264803a0
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DOI: https://doi.org/10.1038/264803a0
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