Aminoacylation of Indole Diterpenes by Cluster-Specific Monomodular NRPS-like Enzymes
Rose M McLellan1,2, Rosannah C Cameron1,2, Matthew J Nicholson1
1Ferrier Research Institute, Victoria University of Wellington, Wellington 6012, New Zealand.
Abstract:
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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