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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Main Authors:	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
Format:	Article
Language:	English
Published:	Nature Publishing Group 2016-03-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/ncomms10911

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spelling	doaj-9cfd7194e093495a81ae07646995d9a22021-05-11T10:53:37ZengNature Publishing GroupNature Communications2041-17232016-03-017111610.1038/ncomms10911Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective MichaelasesJan-Ytzen van der Meer0Harshwardhan Poddar1Bert-Jan Baas2Yufeng Miao3Mehran Rahimi4Andreas Kunzendorf5Ronald van Merkerk6Pieter G. Tepper7Edzard M. Geertsema8Andy-Mark W. H. Thunnissen9Wim J. Quax10Gerrit J. Poelarends11Department of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenDepartment of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of GroningenThe 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.https://doi.org/10.1038/ncomms10911
collection	DOAJ
language	English
format	Article
sources	DOAJ
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
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2016-03-01
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.
url	https://doi.org/10.1038/ncomms10911
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Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases

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