Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 138, Issue 19, Pages 6095-6098Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b00232
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Funding
- BBSRC [BB/D526037/1]
- EPSRC through the BrisSynBio Synthetic Biology Research Centre [BB/L01386X/1]
- EPSRC [EP/G0367641/1]
- GSK
- BBSRC David Phillips Fellowship [BB/M026280/1]
- Biotechnology and Biological Sciences Research Council [BB/L018756/1, BB/M026280/1, BB/L01386X/1, BB/K016601/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/K035746/1, GR/R86119/01, EP/M015378/1, EP/L000253/1, EP/L011999/1, 1501341, EP/E022197/1, EP/K03927X/1, EP/M022609/1, EP/J010588/1, EP/G007705/1, EP/M027546/1] Funding Source: researchfish
- BBSRC [BB/L01386X/1, BB/M026280/1, BB/L018756/1, BB/K016601/1] Funding Source: UKRI
- EPSRC [EP/K03927X/1, EP/L011999/1, EP/E022197/1, EP/L000253/1, EP/M022609/1, EP/G007705/1, EP/M015378/1, EP/J010588/1, EP/K035746/1, EP/M027546/1] Funding Source: UKRI
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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.
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