In vitro selection for catalytic turnover from a library of beta-lactamase mutants and penicillin-binding proteins.

Avalle, B;Vanwetswinkel, S.;Fastrez, Jacques
(1997) Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology — Vol. 7, n° 4, p. 479-484 (1997)

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  • Avalle, B
    Author
  • Vanwetswinkel, S.
    Author
  • Fastrez, JacquesUCLouvain
    Author
Abstract
A library of mutants of the RTEM beta-lactamase displayed on phage was created; it contained penicillin binding proteins (PBPs) as well as a small fraction of active beta-lactamases. The library was submitted to a selection process to extract the beta-lactamases i.e. the enzymes that turnover efficiently. This was achieved by a two steps procedure. In the first step, the beta-lactamases were labelled by reaction with a biotinylated suicide inhibitor while the PBPs were blocked by incubation in the presence of benzylpenicillin. In the second step, the labelled active phage-enzymes were separated by affinity chromatography on streptavidin coated beads. (C) 1997, Elsevier Science Ltd.
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Avalle, B., Vanwetswinkel, S., & Fastrez, J. (1997). In vitro selection for catalytic turnover from a library of beta-lactamase mutants and penicillin-binding proteins. Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology, 7(4), 479-484. https://doi.org/10.1016/S0960-894X(97)00040-1 (Original work published 1997)