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Arch Biochem Biophys. 1999 Jul 1;367(1):146-50.

Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean.

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Plant Biology Division, Samuel Roberts Noble Foundation, 2510 Sam Noble Parkway, Ardmore, Oklahoma, 73401, USA.


The first specific reaction in the biosynthesis of isoflavonoid compounds in plants is the 2-hydroxylation, coupled to aryl migration, of a flavanone. Using a functional genomics approach, we have characterized a cDNA encoding a 2-hydroxyisoflavanone synthase from soybean (Glycine max). Microsomes isolated from insect cells expressing this cytochrome P450 from a baculovirus vector convert 4', 7-dihydroxyflavanone (liquiritigenin) to 4',7-dihydroxyisoflavone (daidzein), most likely via 2,4',7-trihydroxyisoflavanone which spontaneously dehydrates to daidzein. The enzyme also converts naringenin (4',5,7-trihydroxyflavanone) to genistein, but at a lower rate. 2-Hydroxyisoflavanone synthase transcripts are strongly induced in alfalfa cell suspensions in response to elicitation.

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