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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Nature Portfolio
2016
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oai:doaj.org-article:9cfd7194e093495a81ae07646995d9a22021-12-02T17:31:49ZUsing mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases10.1038/ncomms109112041-1723https://doaj.org/article/9cfd7194e093495a81ae07646995d9a22016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms10911https://doaj.org/toc/2041-1723The 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.Jan-Ytzen van der MeerHarshwardhan PoddarBert-Jan BaasYufeng MiaoMehran RahimiAndreas KunzendorfRonald van MerkerkPieter G. TepperEdzard M. GeertsemaAndy-Mark W. H. ThunnissenWim J. QuaxGerrit J. PoelarendsNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-16 (2016) |
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Science Q 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 Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases |
description |
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. |
format |
article |
author |
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 |
author_facet |
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 |
author_sort |
Jan-Ytzen van der Meer |
title |
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases |
title_short |
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases |
title_full |
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases |
title_fullStr |
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases |
title_full_unstemmed |
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases |
title_sort |
using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective michaelases |
publisher |
Nature Portfolio |
publishDate |
2016 |
url |
https://doaj.org/article/9cfd7194e093495a81ae07646995d9a2 |
work_keys_str_mv |
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