Structure-function relationships of wheat flavone <Emphasis Type="Italic">O</Emphasis>-methyltransferase: Homology modeling and site-directed mutagenesis |
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| Authors: | Jian-Min Zhou Eunjung Lee Francesca Kanapathy-Sinnaiaha Younghee Park Jack A Kornblatt Yoongho Lim Ragai K Ibrahim |
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| Institution: | (1) Plant Biochemistry Laboratory and Centre for Structural-Functional Genomics, Concordia University, Montreal, QC, H4B 1R6, Canada;(2) Division of Bioscience and Biotechnology, BMIC, RCD, Konkuk University, Seoul, 143-701, Korea;(3) Enzyme Research Group, Department of Chemistry & Biochemistry, Concordia University, Montreal, QC, H4B 1R6, Canada |
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| Abstract: | Background Wheat (Triticum aestivum L.) O-methyltransferase (TaOMT2) catalyzes the sequential methylation of the flavone, tricetin, to its 3'-methyl- (selgin), 3',5'-dimethyl-
(tricin) and 3',4',5'-trimethyl ether derivatives. Tricin, a potential multifunctional nutraceutical, is the major enzyme
reaction product. These successive methylations raised the question as to whether they take place in one, or different active
sites. We constructed a 3-D model of this protein using the crystal structure of the highly homologous Medicago sativa caffeic acid/5-hydroxyferulic acid O-methyltransferase (MsCOMT) as a template with the aim of proposing a mechanism for multiple methyl transfer reactions in
wheat. |
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