Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds

The expanding “toolbox” of biocatalysts opens new opportunities to redesign synthetic strategies to target molecules by incorporating a key enzymatic step into the synthesis. Herein, we describe a general biocatalytic approach for the enantioselective preparation of 2,6-disubstituted piperidines sta...

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Main Authors: Ryan, James, Šiaučiulis, Mindaugas, Gomm, Andrew, Macia, Beatriz, O'Reilly, Elaine, Caprio, Vittorio
Format: Article
Published: American Chemical Society 2016
Online Access:https://eprints.nottingham.ac.uk/39699/
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author Ryan, James
Šiaučiulis, Mindaugas
Gomm, Andrew
Macia, Beatriz
O'Reilly, Elaine
Caprio, Vittorio
author_facet Ryan, James
Šiaučiulis, Mindaugas
Gomm, Andrew
Macia, Beatriz
O'Reilly, Elaine
Caprio, Vittorio
author_sort Ryan, James
building Nottingham Research Data Repository
collection Online Access
description The expanding “toolbox” of biocatalysts opens new opportunities to redesign synthetic strategies to target molecules by incorporating a key enzymatic step into the synthesis. Herein, we describe a general biocatalytic approach for the enantioselective preparation of 2,6-disubstituted piperidines starting from easily accessible pro-chiral ketoenones. The strategy represents a new biocatalytic disconnection, which relies on an ω-TA-mediated aza-Michael reaction. Significantly, we show that the reversible enzymatic process can power the shuttling of amine functionality across a molecular framework, providing access to the desired aza-Michael products.
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institution University of Nottingham Malaysia Campus
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publishDate 2016
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spelling nottingham-396992020-05-04T18:21:44Z https://eprints.nottingham.ac.uk/39699/ Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds Ryan, James Šiaučiulis, Mindaugas Gomm, Andrew Macia, Beatriz O'Reilly, Elaine Caprio, Vittorio The expanding “toolbox” of biocatalysts opens new opportunities to redesign synthetic strategies to target molecules by incorporating a key enzymatic step into the synthesis. Herein, we describe a general biocatalytic approach for the enantioselective preparation of 2,6-disubstituted piperidines starting from easily accessible pro-chiral ketoenones. The strategy represents a new biocatalytic disconnection, which relies on an ω-TA-mediated aza-Michael reaction. Significantly, we show that the reversible enzymatic process can power the shuttling of amine functionality across a molecular framework, providing access to the desired aza-Michael products. American Chemical Society 2016-11-10 Article PeerReviewed Ryan, James, Šiaučiulis, Mindaugas, Gomm, Andrew, Macia, Beatriz, O'Reilly, Elaine and Caprio, Vittorio (2016) Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds. Journal of the American Chemical Society, 138 (49). pp. 15798-15800. ISSN 1520-5126 http://pubs.acs.org/doi/abs/10.1021/jacs.6b07024 doI:10.1021/jacs.6b07024 doI:10.1021/jacs.6b07024
spellingShingle Ryan, James
Šiaučiulis, Mindaugas
Gomm, Andrew
Macia, Beatriz
O'Reilly, Elaine
Caprio, Vittorio
Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds
title Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds
title_full Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds
title_fullStr Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds
title_full_unstemmed Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds
title_short Transaminase triggered aza-Michael approach for the enantioselective synthesis of piperidine scaffolds
title_sort transaminase triggered aza-michael approach for the enantioselective synthesis of piperidine scaffolds
url https://eprints.nottingham.ac.uk/39699/
https://eprints.nottingham.ac.uk/39699/
https://eprints.nottingham.ac.uk/39699/