ArticleNature communications2023
Discovery of type II polyketide synthase-like enzymes for the biosynthesis of cispentacin.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Unveiling the Taxonomic Diversity and Unprecedented Biosynthetic Treasure of the Phylum Myxococcota.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Heterologous Expression of Type II PKS Gene Cluster Leads to Diversified Angucyclines inMarine drugs · 2024Article
- Synthetic Biology of Natural Products Engineering: Recent Advances Across the Discover-Design-Build-Test-Learn Cycle.ACS synthetic biology · 2024Review
- Giant polyketide synthase enzymes biosynthesize a giant marine polyether biotoxin.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
7 authors.
Funding
Abstract
Type II polyketide synthases (PKSs) normally synthesize polycyclic aromatic compounds in nature, and the potential to elaborate further diverse skeletons was recently revealed by the discovery of a polyene subgroup. Here, we show a type II PKS machinery for the biosynthesis of a five-membered nonaromatic skeleton contained in the nonproteinogenic amino acid cispentacin and the plant toxin coronatine. We successfully produce cispentacin in a heterologous host and reconstruct its biosynthesis using seven recombinant proteins in vitro. Biochemical analyses of each protein reveal the unique enzymatic reactions, indicating that a heterodimer of type II PKS-like enzymes (AmcF-AmcG) catalyzes a single C
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