Fig. 6: Development and analysis of the sesterterpene synthase VenAY88A/W107A/V111A/T112A/F215A/F219A.
From: Molecular insights into the catalytic promiscuity of a bacterial diterpene synthase
a The summary of the protein expression state and sesterterpene biosynthetic activity of VenA mutants. The mutants marked by grey, black, and red colors stand for the insoluble mutants, soluble but inactive mutants, and soluble and active mutants, respectively. b GC-MS analysis of the in vitro activity of the sextuple VenA mutant towards GFPP. The asterisk stands for the uncharacterized sesterterpene. c The proposed biosynthetic mechanism of 19. d The QM/MM model and zoom-in active site of VenAY88A/W107A/V111A/T112A/F215A/F219A with GFPP binding. Only the shorter distances from C1 to C6=C7, C10=C11, and C18=C19 double bonds are shown. The water molecules are hidden to better present the zoom-in pocket (see Supplementary Fig. 16 for details).
