Regulation of retrochalcone biosynthesis: Activity changes of O-methyltransferases in the yeast extract-induced Glycyrrhiza echinata cells View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-02

AUTHORS

S. Ayabe, A. Udagawa, K. Iida, T. Yoshikawa, T. Furuya

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. More... »

PAGES

16-19

References to SciGraph publications

Journal

TITLE

Plant Cell Reports

ISSUE

1

VOLUME

6

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00269729

DOI

http://dx.doi.org/10.1007/bf00269729

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042446464

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24248440


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145 schema:name School of Pharmaceutical Sciences, Kitasato University, Minato-ku, 108, Tokyo, Japan
146 rdf:type schema:Organization
 




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