Journal
ORGANIC LETTERS
Volume 24, Issue 12, Pages 2332-2337Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.2c00473
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Funding
- New Zealand Ministry of Business, Innovation, and Employment [RTVU1809]
- New Zealand Ministry of Business, Innovation & Employment (MBIE) [RTVU1809] Funding Source: New Zealand Ministry of Business, Innovation & Employment (MBIE)
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Decoration of the core scaffolds of indole diterpene natural products is crucial for generating structural and bioactivity diversity. Aminoacylation, a rarely observed tailoring step in terpene biosynthesis, is found to be involved in IDT biosynthesis through the unusual participation of monomodular nonribosomal peptide synthetase-like enzymes.
Decoration of the core scaffolds of indole diterpene (IDT) natural products is key to generating structural and bioactivity diversity. Aminoacylation as a tailoring step is rarely linked to terpene biosynthesis and is extremely rare in IDT biosynthesis. Through heterologous pathway reconstruction, we have illuminated the genetic and biochemical basis for the only reported examples of aminoacylation in IDT biosynthesis, demonstrating the unusual involvement of monomodular nonribosomal peptide synthetase (NRPS)-like enzymes in IDT decoration.
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