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KMID : 0545120070170030539
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Journal of Microbiology and Biotechnology
2007 Volume.17 No. 3 p.539 ~ p.542
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Glycosylation of Flavonoids with E. coli Expressing Glycosyltransferase from Xanthomonas campestris
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Kim Jeong-Ho
Kim Bong-Gyu
Kim Jae-Ah
Park Young-Hee
Lee Yoon-Jung
Lim Yoong-Ho
Ahn Joong-Hoon
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Abstract
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Glycosyltransferase family 1 (UGT) uses small chemicals including phenolics, antibiotics, and alkaloids as substrates to have an influence in biological activities. A glycosyltransferase (XcGT-2) from Xanthomonas campestris was cloned and consisted of a 1,257 bp open reading frame encoding a 45.5 kDa protein. In order to use this for the modification of phenolic compounds, XcGT-2 was expressed in Escherichia coli as a glutathione S-transferase fusion protein. With the E. coli transformant expressing XcGT-2, biotransformation of flavonoids was carried out. Flavonoids having a double bond between carbons 2 and 3, and hydroxyl groups at both C-3’ and C-4’, were glycosylated and the glycosylation position was determined to be at the hydroxyl group of C-3’, using nuclear magnetic resonance spectroscopy. These results showed that XcGT-2 regiospecifically transferred a glucose molecule to the 3’-hydroxyl group of flavonoids containing both 3’ and 4’-hydroxyl groups.
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KEYWORD
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Biotransformation, flavonoids, glycosyltransferase
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