Enzymatic one-step ring contraction for quinolone biosynthesis

Shinji Kishimoto, Kodai Hara, Hiroshi Hashimoto, Yuichiro Hirayama, Pier Alexandre Champagne, Kendall N. Houk, Yi Tang and Kenji Watanabe ()
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Shinji Kishimoto: University of Shizuoka
Kodai Hara: University of Shizuoka
Hiroshi Hashimoto: University of Shizuoka
Yuichiro Hirayama: University of Shizuoka
Pier Alexandre Champagne: University of California
Kendall N. Houk: University of California
Yi Tang: University of California
Kenji Watanabe: University of Shizuoka

Nature Communications, 2018, vol. 9, issue 1, 1-7

Abstract: Abstract 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.

Date: 2018
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DOI: 10.1038/s41467-018-05221-5

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