Abstract
The absolute configuration of fusaterpenol (GJ1012E) has been revised by an enantioselective deuteration strategy. A bifunctional enzyme with a terpene synthase and a prenyltransferase domain from Aspergillus brasiliensis was characterised as variediene synthase, and the absolute configuration of its product was elucidated. The uniform absolute configurations of these and structurally related di‐ and sesterterpenes together with a common stereochemical course for the geminal methyl groups of GGPP unravel a similar conformational fold of the substrate in the active sites of the terpene synthases. For variediene, a thermal reaction observed during GC/MS analysis was studied in detail for which a surprising mechanism was uncovered.
Highlights
The absolute configuration of fusaterpenol (GJ1012E) has been revised by an enantioselective deuteration strategy
The known fungal representatives are generally made by bifunctional enzymes containing a terpene synthase domain and a prenyltransferase domain for geranylgeranyl diphosphate (GGPP) or geranylfarnesyl diphosphate (GFPP) biosynthesis (TS + PT)[3] and include phomopsene (1) and its derivative methyl phomopsenoate (2) from Phomopsis amygdali,[4] variediene (3) from Emericella variecolor[5] and the cyclopiane
The resulting GGPP isotopomers labelled at C1, C5, C9 and C13 were converted by FgGS to give enantioselectively deuterated products whose HSQC spectra pointed to the same absolute configuration of ent-8 (Figure 1 B)
Summary
The absolute configuration of fusaterpenol (GJ1012E) has been revised by an enantioselective deuteration strategy. A newly characterised variediene synthase from Aspergillus brasiliensis is reported, and its stereochemical course is compared to that of the known related bacterial and fungal enzymes.
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