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

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 sub...

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Veröffentlicht in:Zeitschrift für Naturforschung C. A journal of biosciences 1987-10, Vol.42 (9), p.1146-1148
Hauptverfasser: Forkmann, G., Ruhnau, B.
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0939-5075
1865-7125
DOI:10.1515/znc-1987-9-1026