Nature Communications (Jul 2017)

De novo active sites for resurrected Precambrian enzymes

  • Valeria A. Risso,
  • Sergio Martinez-Rodriguez,
  • Adela M. Candel,
  • Dennis M. Krüger,
  • David Pantoja-Uceda,
  • Mariano Ortega-Muñoz,
  • Francisco Santoyo-Gonzalez,
  • Eric A. Gaucher,
  • Shina C. L. Kamerlin,
  • Marta Bruix,
  • Jose A. Gavira,
  • Jose M. Sanchez-Ruiz

DOI
https://doi.org/10.1038/ncomms16113
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 13

Abstract

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The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable amino acid mutation can lead to substantial Kemp eliminase activity.