Ferrier Research Institute, Victoria University of Wellington, Wellington 6012, New Zealand.
Maurice Wilkins Centre for Molecular Biodiscovery, Victoria University of Wellington, P.O. Box 600, Wellington 6012, New Zealand.
Org Lett. 2022 Apr 1;24(12):2332-2337. doi: 10.1021/acs.orglett.2c00473. Epub 2022 Mar 22.
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.
吲哚二萜（IDT）天然产物核心支架的修饰是产生结构和生物活性多样性的关键。作为修饰步骤的氨酰化很少与萜烯生物合成相关联，在 IDT 生物合成中也极为罕见。通过异源途径重建，我们阐明了 IDT 生物合成中唯一报道的氨酰化的遗传和生化基础，证明了单模块非核糖体肽合酶（NRPS）样酶在 IDT 修饰中的不寻常参与。
