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Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean.
Arch Biochem Biophys. 1999 Jul 01; 367(1):146-50.AB

Abstract

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.

Authors+Show Affiliations

Plant Biology Division, Samuel Roberts Noble Foundation, 2510 Sam Noble Parkway, Ardmore, Oklahoma, 73401, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10375412

Citation

Steele, C L., et al. "Molecular Characterization of the Enzyme Catalyzing the Aryl Migration Reaction of Isoflavonoid Biosynthesis in Soybean." Archives of Biochemistry and Biophysics, vol. 367, no. 1, 1999, pp. 146-50.
Steele CL, Gijzen M, Qutob D, et al. Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean. Arch Biochem Biophys. 1999;367(1):146-50.
Steele, C. L., Gijzen, M., Qutob, D., & Dixon, R. A. (1999). Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean. Archives of Biochemistry and Biophysics, 367(1), 146-50.
Steele CL, et al. Molecular Characterization of the Enzyme Catalyzing the Aryl Migration Reaction of Isoflavonoid Biosynthesis in Soybean. Arch Biochem Biophys. 1999 Jul 1;367(1):146-50. PubMed PMID: 10375412.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean. AU - Steele,C L, AU - Gijzen,M, AU - Qutob,D, AU - Dixon,R A, PY - 1999/6/22/pubmed PY - 1999/6/22/medline PY - 1999/6/22/entrez SP - 146 EP - 50 JF - Archives of biochemistry and biophysics JO - Arch. Biochem. Biophys. VL - 367 IS - 1 N2 - 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. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/10375412/Molecular_characterization_of_the_enzyme_catalyzing_the_aryl_migration_reaction_of_isoflavonoid_biosynthesis_in_soybean_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003-9861(99)91238-9 DB - PRIME DP - Unbound Medicine ER -