Skip to main content
. 2017 Nov 20;293(1):28–46. doi: 10.1074/jbc.RA117.000564

Figure 1.

Figure 1.

Enzymatic characterization of recombinant stilbenoid prenyltransferases expressed in N. benthamiana. A, AhR4DT-1 and AhR′3DT-1/2/3/4 from peanut catalyzes the 4- and 3′-prenylation of resveratrol, respectively. B, enzymatic characterization of resveratrol prenyltransferase transiently expressed in N. benthamiana leaf. HPLCs (UV 320 nm) of ethyl acetate extract of 1 ml of reaction mixture of 100 μm resveratrol, 300 μm DMAPP, 10 mm MgCl2, and 10 mm DTT were incubated with 5 mg of crude protein of N. benthamiana leaf after vacuum infiltration with A. tumefaciens LBA4404 harboring pBIB-Kan-AhR4DT-1 (B), pBIB-Kan-AhR3′DT-1 (C), pBIB-Kan-AhR3′DT-2 (D), pBIB-Kan-AhR3′DT-3 (E), pBIB-Kan-AhR3′DT-4 (F), and pBIB-Kan binary vectors (G) in a pH 9.0 Tris-HCl buffer for 40 min. mAU, milli-absorbance units.