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 |
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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. |
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ISSN: | 0939-5075 1865-7125 |
DOI: | 10.1515/znc-1987-9-1026 |