ArticleProceedings of the National Academy of Sciences of the United States of America2023
Animal FAS-like polyketide synthases produce diverse polypropionates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 18 citations in OpenAlex.
- Inverse stable isotopic labeling for natural product characterization and discovery.Natural product reports · 2026Review
- An Alkaloid Biosynthetic Gene Bundle in Animals.Journal of the American Chemical Society · 2026Article
- An endosymbiotic origin of the crimson pigment from the lac insect.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phylogenetic systematics of the genusZoological journal of the Linnean Society · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Defensive polyketides produced by an abundant gastropod are candidate keystone molecules in estuarine ecology.Science advances · 2024Article
- Chromosome-level genome assembly of the sacoglossan sea slug Elysia timida (Risso, 1818).BMC genomics · 2024Article
- Article
- A cryptic radiation of Caribbean sea slugs revealed by integrative analysis:Zoological journal of the Linnean Society · 2024Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Animal cytoplasmic fatty acid synthase (FAS) represents a unique family of enzymes that are classically thought to be most closely related to fungal polyketide synthase (PKS). Recently, a widespread family of animal lipid metabolic enzymes has been described that bridges the gap between these two ubiquitous and important enzyme classes: the animal FAS-like PKSs (AFPKs). Although very similar in sequence to FAS enzymes that produce saturated lipids widely found in animals, AFPKs instead produce structurally diverse compounds that resemble bioactive polyketides. Little is known about the factors that bridge lipid and polyketide synthesis in the animals. Here, we describe the function of EcPKS2 from
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