Nature Communications (Mar 2016)

Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases

  • Jan-Ytzen van der Meer,
  • Harshwardhan Poddar,
  • Bert-Jan Baas,
  • Yufeng Miao,
  • Mehran Rahimi,
  • Andreas Kunzendorf,
  • Ronald van Merkerk,
  • Pieter G. Tepper,
  • Edzard M. Geertsema,
  • Andy-Mark W. H. Thunnissen,
  • Wim J. Quax,
  • Gerrit J. Poelarends

DOI
https://doi.org/10.1038/ncomms10911
Journal volume & issue
Vol. 7, no. 1
pp. 1 – 16

Abstract

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The Michael-type addition reaction is used for carbon-carbon bond formation; however biocatalytic methods for this reaction are rare. Here, the authors generate and exploit mutability landscapes of 4-oxalocrotonate tautomerase to direct the redesign of this promiscuous enzyme into enantio-complementary Michaelases.