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Enzyme-Catalyzed Intramolecular Enantioselective Hydroalkoxylation.
Gao, Shu-Shan; Garcia-Borràs, Marc; Barber, Joyann S; Hai, Yang; Duan, Abing; Garg, Neil K; Houk, K N; Tang, Yi.
Afiliação
  • Gao SS; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Garcia-Borràs M; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Barber JS; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Hai Y; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Duan A; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Garg NK; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Houk KN; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
  • Tang Y; Department of Chemical and Biomolecular Engineering and ⊥Department of Chemistry and Biochemistry, University of California , Los Angeles, California 90095, United States.
J Am Chem Soc ; 139(10): 3639-3642, 2017 03 15.
Article em En | MEDLINE | ID: mdl-28240554
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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fenalenos / Liases Idioma: En Revista: J Am Chem Soc Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fenalenos / Liases Idioma: En Revista: J Am Chem Soc Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos