ArticleJournal of the American Chemical Society2026
Dimerization-Dependent Trans-Domain Coupling Enables Intermediate Transfer in Fungal Haloacid Dehalogenase-Like Terpene Cyclases.
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. Not yet cited in PubMed.
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Abstract
Drimane-type sesquiterpenes (DTSs) are a widely distributed terpenoid family with diverse and potent bioactivities. Although DTS synthases occur in plants, bacteria, and fungi, they share little sequence identity across kingdoms, obscuring the mechanistic principles that govern drimane scaffold formation and product phosphorylation states. Haloacid dehalogenase (HAD)-like terpene cyclases (TCs), TC domains fused to HAD-like phosphatases, are especially intriguing because they couple cyclization with dephosphorylation, yet how these enzymes control scaffold outcomes and phosphorylation states across kingdoms remains unresolved. Here, we identify the fungal enzyme AacA as a bifunctional albicanoyl monophosphate synthase that catalyzes class II cyclization of farnesyl pyrophosphate, followed by Mg
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