Enzymatic preparation of 1-O-hydroxycinnamoyl-β-D-glucoses and their application to the study of 1-O-hydroxycinnamoyl-β-D-glucose-dependent acyltransferase in anthocyanin-producing cultured cells of Daucus carota and Glehnia littoralis
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Four 1-<i>O</i>-hydroxycinnamoyl-β-<small>D</small>-glucoses (HCA-Glcs), sinapoyl-, feruloyl-, caffeoyl-, and 4-coumaroyl-glucoses, were synthesized using a recombinant protein of sinapate glucosyltransferase from <i>Gomphrena globosa</i> coupled with a recycling system of UDP-glucose by sucrose synthase from <i>Arabidopsis thaliana</i>. The substrate preference of HCA-Glc-dependent acyltransferase activity was examined in a protein extract prepared from anthocyanin-producing cultured cells of <i>Daucus carota</i> and <i>Glehnia littoralis</i>. The main anthocyanin molecule of the aglycon and the sugar moiety produced and accumulated in both cultured cells were exactly the same; the only difference was found in modification with sinapoyl moiety in <i>D. carota</i> and with feruloyl moiety in <i>G. littoralis</i>. The protein extracts from both <i>D. carota</i> and <i>G. littoralis</i> cultured cells showed higher activity with feruloyl-Glc than with sinapoyl-Glc. The major HCA-Glcs that accumulated in cultured cells of <i>D. carota</i> and <i>G. littoralis</i> were sinapoyl-Glc and feruloyl-Glc, respectively. These results suggested that the specificity of HCA moieties of major anthocyanin molecules in cultured cells of <i>D. carota</i> and <i>G. littoralis</i> might be dominated by produced and accumulated acyl donor molecules <i>in vivo</i> rather than by the substrate specificity of acyltransferase enzymes.
- Plant tissue culture letters
Plant tissue culture letters 25(4), 369-375, 2008-09-01
Japanese Society for Plant Cell and Molecular Biology