Distinct Substrate Specificity of Dihydroflavonol 4-Reductase from Flowers of Petunia hybrida

  • Forkmann G
  • Ruhnau B
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Abstract

Dihydroflavonol 4-reductase from Petunia flowers cata­lyzes the reduction of dihydroquercetin to leucocyanidin and, in particular, of dihydromyricetin to leucodelphinidin, whereas reduction of the simple dihydroflavonol dihydro- kaempferol to leucopelargonidin could not be observed. This special substrate specificity of dihydroflavonol 4-re­ductase is most probably the reason for the observations that delphinidin derivatives are the main end products of anthocyanin biosynthesis in Petunia flowers, whereas an- thocyanins based on pelargonidin are rarely found and, if present, are only formed in very small amounts.

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Forkmann, G., & Ruhnau, B. (1987). Distinct Substrate Specificity of Dihydroflavonol 4-Reductase from Flowers of Petunia hybrida. Zeitschrift Für Naturforschung C, 42(9–10), 1146–1148. https://doi.org/10.1515/znc-1987-9-1026

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