ArticleJournal of industrial microbiology & biotechnology2021
Discovery of ammosesters by mining the Streptomyces uncialis DCA2648 genome revealing new insight into ammosamide biosynthesis.
Article in Journal of industrial microbiology & biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The Biosynthetic Pathway to the Pyrroloiminoquinone Marine Natural Product Ammosamide C.Journal of the American Chemical Society · 2025Article
- The Biosynthetic Pathway to the Pyrroloiminoquinone Marine Natural Product Ammosamide C.bioRxiv : the preprint server for biology · 2025Article
- Unexpected Transformations during Pyrroloiminoquinone Biosynthesis.Journal of the American Chemical Society · 2024Article
- Genomic Organization of Streptomyces flavotricini NGL1 and Streptomyces erythrochromogenes HMS4 Reveals Differential Plant Beneficial Attributes and Laccase Production Capabilities.Molecular biotechnology · 2022Article
- A biosynthetic pathway to aromatic amines that uses glycyl-tRNA as nitrogen donor.Nature chemistry · 2022Article
- Introduction to the special issue: "Natural Product Discovery and Development in the Genomic Era: 2021".Journal of industrial microbiology & biotechnology · 2021Article
- Submerged fermentation of Streptomyces uncialis providing a biotechnology platform for uncialamycin biosynthesis, engineering, and production.Journal of industrial microbiology & biotechnology · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The ammosamides (AMMs) are a family of pyrroloquinoline alkaloids that exhibits a wide variety of bioactivities. A biosynthetic gene cluster (BGC) that is highly homologous in both gene content and genetic organization to the amm BGC was identified by mining the Streptomyces uncialis DCA2648 genome, leading to the discovery of a sub-family of new AMM congeners, named ammosesters (AMEs). The AMEs feature a C-4a methyl ester, differing from the C-4a amide functional group characteristic to AMMs, and exhibit modest cytotoxicity against a broad spectrum of human cancer cell lines, expanding the structure-activity relationship for the pyrroloquinoline family of natural products. Comparative analysis of the ame and amm BGCs supports the use of a scaffold peptide as an emerging paradigm for the biosynthesis of the pyrroloquinoline family of natural products. AME and AMM biosynthesis diverges from a common intermediate by evolving the pathway-specific Ame24 O-methyltransferase and Amm20 amide synthetase, respectively. These findings will surely inspire future efforts to mimic Nature's combinatorial biosynthetic strategies for natural product structural diversity.
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Registered trials
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