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.

journal_name

Mol Biol Rep

authors

Qin JC,Zhang YM,Lang CY,Yao YH,Pan HY,Li X

doi

10.1007/s11033-011-0899-7

subject

Has Abstract

pub_date

2012-02-01 00:00:00

pages

1601-8

issue

2

eissn

0301-4851

issn

1573-4978

journal_volume

39

pub_type

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