ArticlePlant cell reports2026
A conserved germanicol synthase lineage and a single-residue switch controlling triterpene scaffold divergence in Panax.
Article in Plant cell reports, 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
key messageA conserved germanicol synthase (GNS) lineage exists in Panax; a single methionine-to-asparagine switch at residue 728 controls triterpene scaffold divergence from β-amyrin to germanicol. Triterpenoid scaffold diversification in Panax is governed by oxidosqualene cyclases (OSCs); however, it remains unclear whether this genus has the ability to produce noncanonical pentacyclic skeletons. In this study, we functionally characterized a previously unrecognized germanicol synthase (PvOSC9) alongside its paralog, β-amyrin synthase (βAS), known as PvOSC8, from Panax vietnamensis var. fuscidiscus. Structural comparisons reveal a single residue 728 (Asn ↔ Met) that alters carbocation folding trajectories, thereby establishing a minimal molecular switch for scaffold identity. Notably, PvOSC9 is enriched in flowers and responds to jasmonate, suggesting a possible context-dependent role of PvOSC9 in floral tissues. Collectively, these findings broaden the triterpene scaffold repertoire in Panax and offer a mechanistically grounded framework for programmable triterpenoid biosynthesis.
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