KMID : 0903520090520020114
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology 2009 Volume.52 No. 2 p.114 ~ p.120
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O -Methyltransferase from Soybean Uses Both Caffeoyl-CoA and Flavonoids as Substrates
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Kim Dae-Hwan
Kim Bong-Gyu Park So-Hyun Kim Na-Yeon Lee Yoon-Jung Min Shin-Young Park Yong-Bae Lee Jung-Bok Kim Jong-Chan Lim Yoong-Ho Chong You-Hoon Ahn Joong-Hoon
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Abstract
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A gene encoding O-methyltransferase (SOMT)-10 from soybean, SOMT-10, was cloned by reverse transcription polymerase chain reaction. Phylogenetic analysis revealed that SOMT-10 belonged to caffeoyl-CoA O-methyltransferase (CCoAOMT) and contained conserved catalytic residues found in CCoAOMT. SOMT-10 was expressed in Escherichia coli as a glutathione S-transferase fusion protein and purified to determine its substrate. Several compounds including caffeoyl-CoA, naringenin, quercetin, caffeic acid, kaempferol and luteonin were tested as substrates for the purified recombinant SOMT-10. Analysis of reaction products using high performance liquid chromatography revealed that SOMT-10 used caffeoyl-CoA, quercetin and luteolin as substrates. This result indicated that SOMT-10 used flavones having vicinal hydroxyl groups. The methylation position was determined to be the 3\¡¯ hydroxyl group. It is likely that SOMT-10 is a new class of OMT that uses not only caffeoyl-CoA, but also flavonoids. Molecular docking of tricetin with the modeled structure SOMT-10 disclosed that SOMT-10 showed all combinations of the O- methylated products.
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KEYWORD
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caffeoyl-CoA, flavonoid, O-methyltransferase, phenylpropanoid, soybean
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