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Clemens, S; Hinderer, W; Wittkampf, U; Barz, W: Characterization of cytochrome P450-dependent isoflavone hydroxylases from chickpea, Phytochemistry, 32, 653-657 (1993), doi:10.1016/S0031-9422(00)95150-1
Abstract:
Microsomal fractions from elicited chickpea cell cultures, roots and leaves in the presence of O2 and NADPH catalyse the 2′- and 3′-hydroxylations of the isoflavones formononetin and biochanin A. The enzymes were characterized as to their substrate specificity, cofactor requirements and inhibition by cytochrome P450 inhibitors. The activities, which are low or not measurable in non-elicited cultures, roots and leaves, are strongly induced upon biotic and abiotic elicitation. Their induction pattern, however, is different depending on the source of the microsomal fraction. Induction of the 2′-hydroxylation of formononetin precedes accumulation of the chickpea phytoalexin medicarpin by two to four hours. The role of 2′-hydroxylation of formononetin in medicarpin synthesis is discussed.

last modified 2021-03-01