Biochemical characterization of a putative wheat caffeic acid O-methyltransferase

Jian Min Zhou; Yong Weon Seo; Ragai K. Ibrahim

doi:10.1016/j.plaphy.2008.11.011

Biochemical characterization of a putative wheat caffeic acid O-methyltransferase

Jian Min Zhou, Yong Weon Seo, Ragai K. Ibrahim

Research output: Contribution to journal › Article › peer-review

25 Citations (Scopus)

Abstract

A wheat (Triticum aestivum L., near isogenic line of Hamlet) O-methyltransferase (OMT) was previously reported as a putative caffeic acid OMT (TaCOMT1), involved in lignin biosynthesis, based on its high sequence similarity with a number of graminaceous COMTs. The fact that the putative TaCOMT1 exhibits a significantly high sequence homology to another recently characterized wheat flavone-specific OMT (TaOMT2), and that molecular modeling studies indicated several conserved amino acid residues involved in substrate binding and catalysis of both proteins, prompted an investigation of its appropriate substrate specificity. We report here that TaCOMT1 exhibits highest preference for the flavone tricetin, and lowest activity with the lignin precursors, caffeic acid/5-hydroxyferulic acid as the methyl acceptor molecules, indicating that it is not involved in lignin biosynthesis. We recommend its reannotation to a flavone-specific TaOMT1 that is distinct from TaOMT2. Crown

Original language	English
Pages (from-to)	322-326
Number of pages	5
Journal	Plant Physiology and Biochemistry
Volume	47
Issue number	4
DOIs	https://doi.org/10.1016/j.plaphy.2008.11.011
Publication status	Published - 2009 Apr

Bibliographical note

Funding Information:
This work was supported by grants from the Natural Sciences and Engineering Research Council (NSERC) of Canada to R.K.I., and partially supported by the Technology Development Program for Agriculture and Forestry, Ministry of Agriculture and Forestry, Republic of Korea to Y.W.S. We wish to thank Dr. Y. Fukushi, Hokkaido University, Japan, for the synthesis of the tricetin methyl ether derivatives, and Professor Yoongho Lim, Dept. of Bioscience and Biotechnology, Konkuk University, S. Korea, for molecular modeling of TaOMT2 and production of Fig. 5 .

Keywords

Biochemical characterization
Flavone-specific O-methyltransferase
Reannotation
Tricetin
Triticum aestivum L.
Wheat

ASJC Scopus subject areas

Physiology
Genetics
Plant Science

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10.1016/j.plaphy.2008.11.011

Cite this

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title = "Biochemical characterization of a putative wheat caffeic acid O-methyltransferase",

abstract = "A wheat (Triticum aestivum L., near isogenic line of Hamlet) O-methyltransferase (OMT) was previously reported as a putative caffeic acid OMT (TaCOMT1), involved in lignin biosynthesis, based on its high sequence similarity with a number of graminaceous COMTs. The fact that the putative TaCOMT1 exhibits a significantly high sequence homology to another recently characterized wheat flavone-specific OMT (TaOMT2), and that molecular modeling studies indicated several conserved amino acid residues involved in substrate binding and catalysis of both proteins, prompted an investigation of its appropriate substrate specificity. We report here that TaCOMT1 exhibits highest preference for the flavone tricetin, and lowest activity with the lignin precursors, caffeic acid/5-hydroxyferulic acid as the methyl acceptor molecules, indicating that it is not involved in lignin biosynthesis. We recommend its reannotation to a flavone-specific TaOMT1 that is distinct from TaOMT2. Crown",

keywords = "Biochemical characterization, Flavone-specific O-methyltransferase, Reannotation, Tricetin, Triticum aestivum L., Wheat",

author = "Zhou, {Jian Min} and Seo, {Yong Weon} and Ibrahim, {Ragai K.}",

note = "Funding Information: This work was supported by grants from the Natural Sciences and Engineering Research Council (NSERC) of Canada to R.K.I., and partially supported by the Technology Development Program for Agriculture and Forestry, Ministry of Agriculture and Forestry, Republic of Korea to Y.W.S. We wish to thank Dr. Y. Fukushi, Hokkaido University, Japan, for the synthesis of the tricetin methyl ether derivatives, and Professor Yoongho Lim, Dept. of Bioscience and Biotechnology, Konkuk University, S. Korea, for molecular modeling of TaOMT2 and production of Fig. 5 .",

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N2 - A wheat (Triticum aestivum L., near isogenic line of Hamlet) O-methyltransferase (OMT) was previously reported as a putative caffeic acid OMT (TaCOMT1), involved in lignin biosynthesis, based on its high sequence similarity with a number of graminaceous COMTs. The fact that the putative TaCOMT1 exhibits a significantly high sequence homology to another recently characterized wheat flavone-specific OMT (TaOMT2), and that molecular modeling studies indicated several conserved amino acid residues involved in substrate binding and catalysis of both proteins, prompted an investigation of its appropriate substrate specificity. We report here that TaCOMT1 exhibits highest preference for the flavone tricetin, and lowest activity with the lignin precursors, caffeic acid/5-hydroxyferulic acid as the methyl acceptor molecules, indicating that it is not involved in lignin biosynthesis. We recommend its reannotation to a flavone-specific TaOMT1 that is distinct from TaOMT2. Crown

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Biochemical characterization of a putative wheat caffeic acid O-methyltransferase

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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