ArticleJournal of the American Chemical Society2026
Engineered Modular Polyketide Synthases Elucidate How Enoylreductases Collaborate with Downstream Acyl Carrier Proteins and Ketosynthases to Set Stereocenters.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16.Molecular & cellular proteomics : MCP · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
To engineer modular polyketide synthases that reliably yield stereocomplex products, a detailed understanding of how their enzymatic domains collectively operate is essential. How their enoylreductase (ER) domains function to install either d-or l-oriented alkyl substituents remains largely mysterious. In this study, we investigated the stereoselectivity of ERs and how they work with other domains within tetraketide-heptaketide synthase platforms constructed from components of the pikromycin and rapamycin synthases. We first determined how ER and acyl carrier protein (ACP) domains associate by mutagenically probing the consensus solution predicted by AlphaFold using an
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