@article{810f4b9a944e4787bfc0e63c6da1eb02,
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",
note = "Funding Information: This work was supported by the NIH (1DP1GM106413 and 1R35GM118056 to Y.T.), the NSF (CHE-1361104 to K.N.H.) and JSPS Program for Advancing Strategic International Networks to Accelerate the Circulation of Talented Researchers (No. G2604 to K.W.). This work was also supported in part by the Japan Society for the Promotion of Science (JSPS) (K.W., 15KT0068, 26560450), Innovative Areas from MEXT, Japan (K.W., 16H06449), the Institution of Fermentation at Osaka (K.W.), the Takeda Science Foundation (K.W.), the Uehara Memorial Foundation (K.W.) and the Princess Takamatsu Cancer Research Fund (K.W.). P.A.C acknowledges the Fonds de recherche du Qu{\'e}bec-Nature et Technologies (FRQNT) for a postdoctoral fellowship. Computations were performed on the Hoffman2 cluster at UCLA. We acknowledge the kind support of the beamline staff of Photon Factory for X-ray data collection. Publisher Copyright: {\textcopyright} 2018, The Author(s).",
year = "2018",
month = dec,
day = "1",
doi = "10.1038/s41467-018-05221-5",
language = "English (US)",
volume = "9",
journal = "Nature communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",
}