Projects per year
Abstract
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 β‐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 oC), 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.
Original language | English |
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Number of pages | 6 |
Journal | ChemCatChem |
Early online date | 25 Aug 2019 |
DOIs | |
Publication status | E-pub ahead of print - 25 Aug 2019 |
Research Groups and Themes
- BrisSynBio
- Bristol BioDesign Institute
- BCS and TECS CDTs
Keywords
- cycloaddition
- protein folding
- natural products
- Diels-Alderase
- Biocatalysis
- Synthetic biology
Fingerprint
Dive into the research topics of 'A Natural Diels-Alder Biocatalyst Enables Efficient [4 + 2] Cycloaddition Under Harsh Reaction Conditions'. Together they form a unique fingerprint.Projects
- 1 Finished
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BrisSynBio: Bristol Centre for Synthetic Biology
Woolfson, D. N. (Principal Investigator)
31/07/14 → 31/03/22
Project: Research
Student theses
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Structural and Functional Interrogation of the Abyssomicin C Biosynthetic Pathway
Maschio, L. (Author), Race, P. (Supervisor) & Willis, C. (Supervisor), 29 Sept 2020Student thesis: Doctoral Thesis › Doctor of Philosophy (PhD)
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