ArticleProtein science : a publication of the Protein Society2006
Selection of allosteric beta-lactamase mutants featuring an activity regulation by transition metal ions.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 22 citations in OpenAlex.
- On the origin of non-specific binders isolated in the selection of phage display peptide libraries.Frontiers in microbiology · 2025Review
- Crystallization and preliminary X-ray diffraction analysis of kanamycin-binding β-lactamase in complex with its ligand.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Phage display: selecting straws instead of a needle from a haystack.Molecules (Basel, Switzerland) · 2011Review
- Ligand binding and allostery can emerge simultaneously.Protein science : a publication of the Protein Society · 2007Article
- Active TEM-1 beta-lactamase mutants with random peptides inserted in three contiguous surface loops.Protein science : a publication of the Protein Society · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Libraries of phage-displayed beta-lactamase mutants in which up to three loops have been engineered by genetic introduction of random peptide sequences or by randomization of the wild-type sequence have been submitted to selection protocols designed to find mutants in which binding of transition metal ions to the engineered secondary binding site leads to significant effects on the enzymatic activity. A double-selection protocol was applied: The phage-displayed libraries were first selected for transition metal ions affinity by panning on IMAC support, then a second selection step was applied to isolate mutants that have retained significant catalytic activity. The analysis of the kinetic properties of mutants in the presence of nickel, copper, or zinc ions allowed isolation of a few mutants whose activity was either enhanced or inhibited by factors up to three and >10, respectively, in a metal-specific manner. A remarkable mutant exhibiting differential allosteric regulation depending on the metal was found. Its activity was activated by nickel ion binding, inhibited by cupric ion binding, and nearly unaffected by zinc ions. These observations point to an interesting potential for up- or down-regulation of activity within a monomeric enzyme by binding to an "allosteric site" relatively remote from the active site.
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