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

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-complement...

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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/9cfd7194e093495a81ae07646995d9a2
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Sumario: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.