Enzymatic one-step ring contraction for quinolone biosynthesis.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30026518.
- Also identified by DOI 10.1038/s41467-018-05221-5 and PMC identifier 6053404.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Alkaloids
- Aspergillus nidulans
- Fungal Proteins
- Hemocyanins
- Quinolones
- Zinc