Directed selective pressure on a β-lactamase to analyse molecular changes involved in development of enzyme function View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1976-12

AUTHORS

ALAN HALL, JEREMY R. KNOWLES

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. More... »

PAGES

803-804

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/264803a0

DOI

http://dx.doi.org/10.1038/264803a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042012588

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/796732


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