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Cloning of cDNAs encoding P450s in flavonoid/isoflavonoid pathway from elicited leguminous cell cultures
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Description
Publisher Summary This chapter describes the methods of cloning P450 cDNAs from elicited cultures of G. echinate and the procedures for the functional characterization with heterologous eukaryotic cells. Detailed methods of assaying the enzyme activities and the preparation of the 2-hydroxyisoflavanone sample by a large-scale incubation are presented in the chapter. 2-Hydroxyisoflavanone synthase has been of particular interest from the viewpoint of the mechanism of both its catalysis and its physiological functions. It catalyzes the hydroxylation of a nonaromatic carbon (C-2) and, at the same time, constructs the isoflavonoid skeleton through 1,2-aryl migration. It is the most important enzyme in the biosynthesis of legume-specific isoflavonoid phytoalexins, as well as of daidzein and genistein, the constitutive ingredients of soybean, which possess health-promoting phytoestrogenic effects.
Journal
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- Methods in Enzymology
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Methods in Enzymology 360-369, 2002
Elsevier
