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.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Qin JC,Zhang YM,Lang CY,Yao YH,Pan HY,Li Xdoi
10.1007/s11033-011-0899-7subject
Has Abstractpub_date
2012-02-01 00:00:00pages
1601-8issue
2eissn
0301-4851issn
1573-4978journal_volume
39pub_type
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