ArticleNature chemistry2026
A system of paired polyether epoxide hydrolases enables a mouldable enzyme for consecutive ring cyclization cascades.
Article in Nature chemistry, 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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Who cites it
1 citing paper in PubMed.
- High-Throughput Prediction of Protein-Protein Interactions Uncovers Hidden Molecular Networks in Biosynthetic Gene Clusters.Computational and structural biotechnology journal · 2026Article
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25 authors.
Funding
Abstract
Ionophore polyethers, a major class of polyketide-derived natural products, are characterized by molecular skeletons featuring arrays of tetrahydrofuran and tetrahydropyran rings. However, the precise mechanism underlying their biosynthesis, suggested to occur by a sequential epoxide-opening and ether cyclization cascade to generate more than two ether rings, remains elusive. Here we explore the biosynthesis of monensin and reveal the indispensability of a heterodimeric assembly of polyether epoxide hydrolases (MonBI·MonBII), with MonBII providing the sole active site. Structural analysis demonstrated that MonBII harbours an unusually large cavity, enabling the consecutive cyclization of substrates containing γ-hydroxy triepoxide moieties. This cavity is formed by the remarkable flexibility of MonBII, which undergoes a dramatic structural transition from a predominantly disordered state to its active folded conformation exclusively in the presence of MonBI. Given the widespread conservation of MonBI- and MonBII-type enzymes, this study emphasizes a unified pairing mechanism, wherein one protomer functions as a molecular mould, facilitating the folding process and stabilizing the structure of its partner for catalysis.
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