ArticleChembiochem : a European journal of chemical biology2019
Targeted Rediscovery and Biosynthesis of the Farnesyl-Transferase Inhibitor Pepticinnamin E.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Logical Exploration of Cinnamoyl-Containing Nonribosomal Peptides via Metabologenomic Targeting and Regulator Overexpression.Journal of the American Chemical Society · 2025Article
- Karakum desert: a unique source of cultivable novel and rare actinomycetes with a remarkable biosynthetic potential.World journal of microbiology & biotechnology · 2025Article
- Nocardia noduli sp. nov., a novel actinobacterium with biotechnological potential.Archives of microbiology · 2022Article
- Small-Molecule RAS Inhibitors as Anticancer Agents: Discovery, Development, and Mechanistic Studies.International journal of molecular sciences · 2022Review
- Genome insights into the pharmaceutical and plant growth promoting features of the novel species Nocardia alni sp. nov.BMC genomics · 2022Article
- Production of chain-extended cinnamoyl compounds by overexpressing two adjacent cluster-situated LuxR regulators inFrontiers in microbiology · 2022Article
- Natural Products Attenuating Biosynthesis, Processing, and Activity of Ras Oncoproteins: State of the Art and Future Perspectives.Biomolecules · 2020Review
- Metabolomic study of marine Streptomyces sp.: Secondary metabolites and the production of potential anticancer compounds.PloS one · 2020Article
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Authors and funding
4 authors.
Funding
Abstract
The natural product pepticinnamin E potently inhibits protein farnesyl transferases and has potential applications in treating cancer and malaria. Pepticinnamin E contains a rare N-terminal cinnamoyl moiety as well as several nonproteinogenic amino acids, including the unusual 2-chloro-3-hydroxy-4-methoxy-N-methyl-L-phenylalanine. The biosynthesis of pepticinnamin E has remained uncharacterized because its original producing strain is no longer available. Here we identified a gene cluster (pcm) for this natural product in a new producer, Actinobacteria bacterium OK006, by means of a targeted rediscovery strategy. We demonstrated that the pcm cluster is responsible for the biosynthesis of pepticinnamin E, a nonribosomal peptide/polyketide hybrid. We also characterized a key O-methyltransferase that modifies 3,4-dihydroxy-l-phenylalanine. Our work has identified the gene cluster for pepticinnamins for the first time and sets the stage for elucidating the unique chemistry required for biosynthesis.
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