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Catalase Involved in Oxidative Cyclization of the Tetracyclic Ergoline of Fungal Ergot Alkaloids.
Yao, Yongpeng; An, Chunyan; Evans, Declan; Liu, Weiwei; Wang, Wei; Wei, Guangzheng; Ding, Ning; Houk, K N; Gao, Shu-Shan.
Afiliación
  • Yao Y; State Key Laboratory of Microbial Resources , Institute of Microbiology, Chinese Academy of Sciences , Beijing 100101 , P. R. China.
  • An C; State Key Laboratory of Microbial Resources , Institute of Microbiology, Chinese Academy of Sciences , Beijing 100101 , P. R. China.
  • Evans D; Department of Chemistry and Biochemistry , University of California , Los Angeles California 90095 , United States.
  • Liu W; State Key Laboratory of Microbial Resources , Institute of Microbiology, Chinese Academy of Sciences , Beijing 100101 , P. R. China.
  • Wang W; State Key Laboratory of Microbial Resources , Institute of Microbiology, Chinese Academy of Sciences , Beijing 100101 , P. R. China.
  • Wei G; University of Chinese Academy of Sciences , Beijing 100049 , P. R. China.
  • Ding N; State Key Laboratory of Microbial Resources , Institute of Microbiology, Chinese Academy of Sciences , Beijing 100101 , P. R. China.
  • Houk KN; University of Chinese Academy of Sciences , Beijing 100049 , P. R. China.
  • Gao SS; School of Food Science and Technology , Jiangnan University , Wuxi , Jiangsu 214122 , P. R. China.
J Am Chem Soc ; 141(44): 17517-17521, 2019 11 06.
Article en En | MEDLINE | ID: mdl-31621316
ABSTRACT
A dedicated enzyme for the formation of the central C ring in the tetracyclic ergoline of clinically important ergot alkaloids has never been found. Herein, we report a dual role catalase (EasC), unexpectedly using O2 as the oxidant, that catalyzes the oxidative cyclization of the central C ring from a 1,3-diene intermediate. Our study showcases how nature evolves the common catalase for enantioselective C-C bond construction of complex polycyclic scaffolds.
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas Fúngicas / Catalasa / Ergolinas Idioma: En Revista: J Am Chem Soc Año: 2019 Tipo del documento: Article
Texto completo
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PubMed Links
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Proteínas Fúngicas / Catalasa / Ergolinas Idioma: En Revista: J Am Chem Soc Año: 2019 Tipo del documento: Article