title: Chalcone isomerase isozymes with different substrate specificities towards 6'-hydroxy- and 6'-deoxychalcones in cultured cells of Glycyrrhiza echinata, a leguminous plant producing 5-deoxyflavonoids.
abstract: Three chalcone isomerase isozymes in Glycyrrhiza echinata (Fabaceae) were separated by chromatofocusing and partially purified to examine their substrate specificities. Two isozymes, one of which was elicitor-inducible, acted on both 6'-hydroxychalcone and 6'-deoxychalcone and presumably are involved in the legume-specific 5-deoxyflavonoid pathway, while another acted on only 6'-hydroxychalcone.
authors.affiliation: Department of Applied Biological Sciences, Nihon University, Fujisawa, Kanagawa, 252-8510 Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kimura
authors.forename: T
authors.initials: T
authors.lastname: Aoki
authors.forename: S
authors.initials: S
authors.lastname: Ayabe
mesh_terms: D002478:Cells, Cultured; D002599:Chalcone / Q000378:metabolism*; D005419:Flavonoids / Q000096:biosynthesis*; D006035:Glycyrrhiza / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D019753:Intramolecular Lyases / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D005419:Flavonoids; D007527:Isoenzymes; D002599:Chalcone; D019753:Intramolecular Lyases; C019865:chalcone isomerase