O-Methyltransferase from Soybean Uses Both Caffeoyl-CoA and Flavonoids as Substrates

被引：4

作者：

Kim, Dae Hwan ^{[1
]}

Kim, Bong Gyu ^{[1
]}

Park, So Hyun ^{[1
]}

Kim, Na Yeon ^{[1
]}

Lee, Yoon Jung ^{[1
]}

Min, Shin Young ^{[1
]}

Park, Yong-Bae ^{[2
]}

Lee, Jung-Bok ^{[2
]}

Kim, Jong-Chan ^{[2
]}

Lim, Yoongho ^{[1
]}

Chong, Youhoon ^{[1
]}

Ahn, Joong-Hoon ^{[1
]}

机构：

[1] Konkuk Univ, Dept Biosci & Biotechnol, Seoul 143701, South Korea

[2] Gyeonggido Inst Hlth & Environm, Suwon 440290, South Korea

来源：

JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY | 2009年 / 52卷 / 02期

关键词：

caffeoyl-CoA; flavonoid; O-methyltransferase; phenylpropanoid; soybean; FUNCTIONAL EXPRESSION; GENE-PRODUCT; RICE; 3'-O-METHYLTRANSFERASE; BIOSYNTHESIS; METHYLATION; CLONING; L;

D O I：

10.3839/jksabc.2009.022

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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.

引用

页码：114 / 120

页数：7

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