Fig. 2: Interrogation of substrate channeling. | Nature Communications

Fig. 2: Interrogation of substrate channeling.

From: Structure of bifunctional variediene synthase yields unique insight on biosynthetic diterpene assembly and cyclization

Fig. 2

A When an equimolar mixture of variediene synthase (EvVS) and cyclooctatenol synthase (CotB2) is incubated with geranylgeranyl diphosphate (GGPP), variediene (VA) and cyclooctatenol (CO) are generated at a 1:1.1 ratio (trace 1). When incubated with dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) instead, only a small change is observed in the product ratio (trace 2). B When an equimolar mixture of EvVS and spatadiene synthase is incubated with GGPP, variediene (VA) and spatadiene (SP) are generated at a 1:0.6 ratio (trace 1). When incubated with DMAPP and IPP instead, no substantial change is observed in the product ratio (trace 2). C When an equimolar mixture of EvVS and the cyclase domain of fusicoccadiene synthase (PaFSCY) is incubated with GGPP, variediene and fusicoccadiene (FS) are generated at a 1:1.1 ratio. When incubated with DMAPP and IPP instead, the variediene:fusicoccadiene product ratio is 1:5.4. Substantial enrichment of fusicoccadiene indicates that the GGPP generated by the EvVS prenyltransferase preferentially transits to PaFSCY.

Back to article page