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Hydroxylation with Unusual Stereoinversion Catalyzed by an FeII/2‐OG Dependent Oxidase and 3,6‐Diene‐2,5‐diketopiperazine Formation in the Biosynthesis of Brevianamide K.
- Source :
-
Angewandte Chemie . 3/27/2023, Vol. 135 Issue 14, p1-7. 7p. - Publication Year :
- 2023
-
Abstract
- Natural products with the 3,6‐diene‐2,5‐diketopiperazine core are widely distributed in nature; however, the biosynthetic mechanism of 3,6‐diene‐2,5‐diketopiperazine in fungi remains to be further elucidated. Through heterologous expression and biochemical investigation of an FeII/2‐oxoglutarate‐dependent oxidase (AspE) and a heme‐dependent P450 enzyme (AspF), we report that AspE, AspF and subsequent dehydration account for the formation of the 3,6‐diene‐2,5‐diketopiperazine substructure of brevianamide K from Aspergillus sp. SK‐28, a symbiotic fungus of mangrove plant Kandelia candel. More interestingly, in‐depth investigation of the enzymatic mechanism showed that AspE promotes hydroxylation of brevianamide Q with unprecedented stereoinversion through hydrogen atom abstraction and water nucleophilic attack from the opposite face of the resultant iminium cation intermediate. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00448249
- Volume :
- 135
- Issue :
- 14
- Database :
- Academic Search Index
- Journal :
- Angewandte Chemie
- Publication Type :
- Academic Journal
- Accession number :
- 162569969
- Full Text :
- https://doi.org/10.1002/ange.202216989