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Lookup NU author(s): Dr James StachORCiD, Professor Paul RaceORCiD
This is the authors' accepted manuscript of an article that has been published in its final definitive form by American Chemical Society, 2016.
For re-use rights please refer to the publisher's terms and conditions.
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.
Author(s): Byrne MJ, Lees NR, Han LC, van der Kamp MW, Mulholland AJ, Stach JEM, Willis CL, Race PR
Publication type: Article
Publication status: Published
Journal: Journal of the American Chemical Society
Year: 2016
Volume: 138
Issue: 19
Pages: 6095-6098
Print publication date: 18/05/2016
Online publication date: 03/05/2016
Acceptance date: 02/04/2016
Date deposited: 23/09/2016
ISSN (print): 0002-7863
ISSN (electronic): 1520-5126
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/jacs.6b00232
DOI: 10.1021/jacs.6b00232
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