Byrne, MJ orcid.org/0000-0001-8111-4605, Lees, NR, Han, LC et al. (5 more authors) (2016) The Catalytic Mechanism of a Natural Diels-Alderase Revealed in Molecular Detail. Journal of the American Chemical Society, 138 (19). pp. 6095-6098. ISSN 0002-7863
Abstract
The Diels-Alder reaction, a [4 + 2] cycloaddition of a conjugated diene to a dienophile, is one of the most powerful reactions in synthetic chemistry. Biocatalysts capable of unlocking new and efficient Diels-Alder reactions would have major impact. Here we present a molecular-level description of the reaction mechanism of the spirotetronate cyclase AbyU, an enzyme shown here to be a bona fide natural Diels-Alderase. Using enzyme assays, X-ray crystal structures, and simulations of the reaction in the enzyme, we reveal how linear substrate chains are contorted within the AbyU active site to facilitate a transannular pericyclic reaction. This study provides compelling evidence for the existence of a natural enzyme evolved to catalyze a Diels-Alder reaction and shows how catalysis is achieved.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 09 Sep 2016 14:03 |
Last Modified: | 09 Sep 2016 14:03 |
Published Version: | http://dx.doi.org/10.1021/jacs.6b00232 |
Status: | Published |
Publisher: | American Chemical Society |
Identification Number: | 10.1021/jacs.6b00232 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:104526 |