Figure legends
Scheme 1 Regeneration of UDPG catalyzed by SuSy in the SuSy-GT
coupling reaction.
Fig. 1 Enzymatic properties of the recombinant Mc SuSy.
(A) pH profile; (B) Temperature profile; (C) Thermal stability; (D)
Effect of metal ions on the activity of Mc SuSy. The data are
presented as the means ± standard deviation of triplicates. The relative
activity (%) was calculated in terms of that of the maximum activity
(100%)
Fig. 2 The structure models of Mc SuSy andAt SuSy1. (A) Ribbon drawing of the structure of Mc SuSy
(blue) aligned with that of At SuSy1 (purple). (B) TheMc SuSy complex with two conserved sequence fragments: residues
300-312 (light blue) and residues 648-683 (pink). The residue number
refers to the sites of At SuSy1 in the multiple sequence
alignment. (C, D) The UDP binding sites of Mc SuSy andAt SuSy1.
Fig. 3 Relative activities of the crude extracts containing the
wild-type and mutants of Mc SuSy. (A)The mutations at theN -terminal phosphorylation sites; (B) The mutations at the “QN”
motif
Fig. 4 Synthesis of ginsenoside Rh2 from PPD in the SuSy-GT
reactions. Data are plotted as means ± standard deviation of duplicates.