Fig. 7: Divergent activities of HsCPTa and HpCPTa1 yield hyperforin analogues.

HPLC-DAD analysis of enzyme assays containing recombinant yeast microsomes. HsCPTa and HpCPTa1 catalysed the conversion of triprenylated phlorisobutyrophenone to secohyperforin endo and exo epimers, respectively. HsCPTa transformed diprenylated-monogeranylated phlorisobutyrophenone to the aliphatic nemosampsone analogue 7, whereas HpCPTa1 catalysed a different mode of cyclization that resulted in the formation of hyperforin. No conversions were observed in control assays containing microsomes from empty vector-transformed yeast cells. S, substrate peak.