Titre du document / Document title
Regiospecific methylation of naringenin to ponciretin by soybean O-methyltransferase expressed in Escherichia coli
Auteur(s) / Author(s)
DAE HWAN KIM (1) ;
KIM Bong-Gyu (1) ;
LEE Youngshim (1) ;
JI YOUNG RYU (2) ;
LIM Yoongho (1) ;
HUR Hor-Gil (2) ;
AHN Joong-Hoon (1) ;
Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)
(1) Department of Molecular Biotechnology, Bio/Molecular Informatics Center, Konkuk University, 1 Hwayang-dong, Kwangjin-gu, Seoul 143-701, COREE, REPUBLIQUE DE
(2) Department of Environmental Science and Engineering, Gwangju Institute of Science and Technology, Gwangju, COREE, REPUBLIQUE DE
Résumé / Abstract
Flavonoids found in plants most likely undergo a variety of modification reactions such as hydroxylation, glycosylation, and/or methylation. Among these, O-methylation has an effect on the solubility and thus on the antimicrobial activity of the flavonoids. We analyzed the conversion of naringenin with a methyltransferase, SOMT-2, from Glycine max. SOMT-2 was expressed in Escherichia coli as a glutathion S-transferase fusion protein. E. coli harboring SOMT-2 was grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC. SOMT-2 could convert apigenin, daidzein, genistein, and quercetin into the corresponding 4'-O-methylated compounds such as acacetin, formononetin, biochanine A, and 4'-methylated quercetin whereas naringenin turned out to be the best substrate tested. SOMT-2 stoichiometically converted naringenin (4',5,7-trihyroxyflavanone) into a ponciretin (4'-methoxy-5,7-dihydroxyflavanone), whose structure was determined by NMR and LC/mass spectral analyses. Considering the reactions, SOMT-2 may have a regiospecific methylation activity, resulting in transforming 4'-hydroxyl group of flavonoids B-ring to 4'-methyl group.
Revue / Journal Title
Journal of biotechnology
ISSN
0168-1656
CODEN JBITD4
Source / Source
2005, vol. 119, n
o2, pp. 155-162 [8 page(s) (article)] (17 ref.)
Langue / Language
Anglais
Editeur / Publisher
Elsevier, Amsterdam, PAYS-BAS
(1984)
(Revue)
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Localisation / Location
INIST-CNRS, Cote INIST : 20305, 35400013265369.0050
Nº notice refdoc (ud4) : 17084575
