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

doi:10.1038/s41467-018-05221-5

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 journal › Article › peer-review

26 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 language	English (US)
Article number	2826
Journal	Nature communications
Volume	9
Issue number	1
DOIs	https://doi.org/10.1038/s41467-018-05221-5
State	Published - Dec 1 2018
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

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10.1038/s41467-018-05221-5

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title = "Enzymatic one-step ring contraction for quinolone biosynthesis",

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.",

author = "Shinji Kishimoto and Kodai Hara and Hiroshi Hashimoto and Yuichiro Hirayama and Champagne, \{Pier Alexandre\} and Houk, \{Kendall N.\} and Yi Tang and Kenji Watanabe",

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doi = "10.1038/s41467-018-05221-5",

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AU - Kishimoto, Shinji

AU - Hara, Kodai

AU - Hashimoto, Hiroshi

AU - Hirayama, Yuichiro

AU - Champagne, Pier Alexandre

AU - Houk, Kendall N.

AU - Tang, Yi

AU - Watanabe, Kenji

PY - 2018/12/1

Y1 - 2018/12/1

N2 - 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.

AB - 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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VL - 9

JO - Nature communications

JF - Nature communications

IS - 1

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ER -

Enzymatic one-step ring contraction for quinolone biosynthesis

Abstract

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