Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 10, Pages 3639-3642Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b01089
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Funding
- NIH [1DP1GM106413, 1R35GM118056]
- NSF [CHE-1361104]
- Chemistry Biology Interface training program [NRSA 5T32GM008496-20]
- Ramon Areces Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1361104] Funding Source: National Science Foundation
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Hydroalkoxylation is a powerful and efficient method of forming C-O bonds and cyclic ethers in synthetic chemistry. In studying the biosynthesis of the fungal natural product herqueinone, we identified an enzyme that can perform an intramolecular enantioselective hydroalkoxylation reaction. PhnH catalyzes the addition of a phenol to the terminal olefin of a reverse prenyl group to give a dihydrobenzofuran product. The enzyme accelerates the reaction by 3 x 10(5)-fold compared to the uncatalyzed reaction. PhnH belongs to a superfamily of proteins with a domain of unknown function (DUF3237), of which no member has a previously verified function. The discovery of PhnH demonstrates that enzymes can be used to promote the enantioselective hydroalkoxylation reaction and form cyclic ethers.
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