Aminoacylation of Indole Diterpenes by Cluster-Specific Monomodular NRPS-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.

Automated summary

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.