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J Am Chem Soc. 2017 Mar 15;139(10):3639-3642. doi: 10.1021/jacs.7b01089. Epub 2017 Mar 1.

Enzyme-Catalyzed Intramolecular Enantioselective Hydroalkoxylation.

Author information

1
Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.

Abstract

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 × 105-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.

PMID:
28240554
PMCID:
PMC5474393
DOI:
10.1021/jacs.7b01089
[Indexed for MEDLINE]
Free PMC Article

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