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Enzymatic one-step ring contraction for quinolone biosynthesis.

  • Author(s): Kishimoto, Shinji
  • Hara, Kodai
  • Hashimoto, Hiroshi
  • Hirayama, Yuichiro
  • Champagne, Pier Alexandre
  • Houk, Kendall N
  • Tang, Yi
  • Watanabe, Kenji
  • et al.

The 6,6-quinolone scaffolds on which viridicatin-type fungal alkaloids are built are frequently found in metabolites that display useful biological activities. Here we report in vitro and computational analyses leading to the discovery of a hemocyanin-like protein AsqI from the Aspergillus nidulans aspoquinolone biosynthetic pathway that forms viridicatins via a conversion of the cyclopenin-type 6,7-bicyclic system into the viridicatin-type 6,6-bicyclic core through elimination of carbon dioxide and methylamine through methyl isocyanate.

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