ArticleJACS Au2026
Investigation of Domain-Domain Interaction between Acyl Carrier Protein and Thioesterase in Modular Polyketide Synthases.
Article in JACS Au, 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.
- Reprogramming the enduracidin NRPS assembly line via thioesterase domain relocation.Synthetic and systems biotechnology · 2027Article
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4 authors.
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Abstract
Modular polyketide synthases are multidomain assembly line enzymes that biosynthesize complex polyketide natural products. The thioesterase (TE) domain plays a critical role in product release by catalyzing the hydrolysis or lactonization of the polyketide intermediate tethered to the acyl carrier protein (ACP). Here, we report that, contrary to the prevailing assumption that TE recognizes only the polyketide moiety, efficient product release requires a specific interaction between the TE domain and the ACP domain. In vitro enzyme assays combined with molecular dynamics simulations revealed a potential mechanism of the ACP-TE interaction, in which loop I of ACP exhibits strong interaction with the TE in mediomycin biosynthesis. Comparative analysis of TE single-domain and ACP-TE didomain insertions in various polyketide biosynthetic pathways showed that ACP-TE didomain insertion generally results in higher product titers in the engineered pathways. Our results illustrate the crucial contribution of ACP-TE interaction for proper product release in polyketide biosynthesis and will guide rational engineering of modular polyketide synthases.
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