Enzymatic one-step ring contraction for quinolone biosynthesis

Shinji Kishimoto, Kodai Hara, Hiroshi Hashimoto, Yuichiro Hirayama, Pier Alexandre Champagne, Kendall N. Houk, Yi Tang, Kenji Watanabe

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish (US)
Article number2826
JournalNature communications
Volume9
Issue number1
DOIs
StatePublished - Dec 1 2018
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Fingerprint

Dive into the research topics of 'Enzymatic one-step ring contraction for quinolone biosynthesis'. Together they form a unique fingerprint.

Cite this