Regulation of retrochalcone biosynthesis: Activity changes of O-methyltransferases in the yeast extract-induced Glycyrrhiza echinata cells |
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Authors: | S Ayabe A Udagawa K Iida T Yoshikawa T Furuya |
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Institution: | (1) School of Pharmaceutical Sciences, Kitasato University, Minato-ku, 108 Tokyo, Japan |
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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 Mg2+ 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.Abbreviations SAM
S-adenosyl-L-methionine
- LMT, SAM
licodione 2-O-methyltransferase
- FMT, SAM
flavone/flavonol O-methyltransferase
- CMT, SAM
caffeate 3-O-methyltransferase
- OMT
O-methyltransferase
- CH
cycloheximide
- YE
yeast extract
This paper is Part 47 in the series Studies on Plant Tissue Cultures. For Part 46, see Ayabe S, Iida K, Furuya T (1986) Phytochemistry: in press |
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