title: Regulation of retrochalcone biosynthesis: Activity changes of O-methyltransferases in the yeast extract-induced Glycyrrhiza echinata cells.
abstract: Three O-methyltransferases which catalyze S-adenosyl-L-methionine (SAM)-dependent O-methylation of licodione (LMT), flavone/flavonol (FMT), and caffeic acid (CMT) were separated from the callus culture of Glycyrrhiza echinata, and characteristic differences between their pH optima and Mg(2+) requirement for activity were demonstrated. The activity of LMT, which is involved in retrochalcone (echinatin) biosynthesis, but not of FMT or CMT, was found to be stimulated when suspension-cultured G. echinata cells were treated with yeast extract (YE), which causes rapid production of echinatin in the cells. Cycloheximide suppressed both the YE-induced echinatin formation and LMT enhancement. The results indicate a selective induction of retrochalcone pathway in Glycyrrhiza cells in response to stress.
authors.affiliation: School of Pharmaceutical Sciences, Kitasato University, Minato-ku, 108, Tokyo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Ayabe
authors.forename: A
authors.initials: A
authors.lastname: Udagawa
authors.forename: K
authors.initials: K
authors.lastname: Iida
authors.forename: T
authors.initials: T
authors.lastname: Yoshikawa
authors.forename: T
authors.initials: T
authors.lastname: Furuya