title: Cloning and functional characterization of a caffeic acid O-methyltransferase from Trigonella foenum-graecum L.
abstract: A cDNA encoding an O-methyltransferase (namely FGCOMT1) was identified from the medicinal plant Trigonella foenum-graecum L. The FGCOMT1 enzyme is a functional caffeic acid O-methyltransferase (COMT) and is localized in the cytosol. Kinetic analysis indicated that FGCOMT1 protein exhibited the highest catalyzing efficiency towards 5-hydroxy ferulic acid and caffeic acid as substrates, but did not possess the abilities to methylate either quercetin or tricetin in vitro. Furthermore, transformation of Arabidopsis loss-of-function Atomt1 mutant with a FGCOMT1 cDNA partially complements accumulation of sinapoyl derivatives but did not function to produce the major methylated flavonol isorhamnetin in seeds. The results from this study indicated that FGCOMT1 is a COMT with substrate preference to monomeric lignin precursors but is not involved in the flavonoid methylation in T. foenum-graecum L.
authors: College of Plant Sciences, Jilin University, 5333 Xi'An Road, Changchun 130062, China.
authors: Jian-Chun
authors: JC
authors: Qin
authors: Ya-Mei
authors: YM
authors: Zhang
authors: Chen-Yong
authors: CY
authors: Lang
authors: Yan-Hua
authors: YH
authors: Yao
authors: Hong-Yu
authors: HY
authors: Pan
authors: Xiang
authors: X
authors: Li
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