Journal
CHEMCATCHEM
Volume 11, Issue 20, Pages 5027-5031Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201901285
Keywords
Biocatalysis; Diels-Alderase; natural products; protein folding; cycloaddition
Categories
Funding
- BBSRC
- EPSRC through the BrisSynBio Synthetic Biology Research Centre [BB/L01386X/1]
- BBSRC [BB/M025624/1, BB/I006478/1]
- DSTL [DSTLX1000098188]
- EPSRC Bristol Centre for Doctoral Training in Chemical Synthesis [EP/G0367641/1]
- GSK
- EPSRC Centre for Doctoral training in Synthetic Biology [EP/L016494/1]
- DSTL
- BBSRC [BB/M025624/1, BB/L01386X/1, BB/I006478/1, BB/M012107/1] Funding Source: UKRI
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Carbon-carbon bond formation is a fundamental transformation in both synthetic chemistry and biosynthesis. Enzymes catalyze such reactions with exquisite selectivity which often cannot be achieved using non-biological methods but may suffer from an intolerance of high temperature and the presence of organic solvents limiting their applications. Here we report the thermodynamic and kinetic stability of the beta-barrel natural Diels-Alderase AbyU, which catalyzes formation of the spirotetronate core of the antimicrobial natural product abyssomicin C, with creation of 3 new asymmetric centers. This enzyme is shown to catalyze [4+2] cycloadditions at elevated temperature (up to 65 degrees C), and in the presence of organic solvents (MeOH, CH3CN and DMSO) and the chemical denaturant guanidinium hydrochloride, revealing that AbyU has potential widespread value as a biocatalyst.
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