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https://soar-ir.repo.nii.ac.jp/oai
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2022-12-14T04:21:52Z
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Purification, molecular cloning and functional characterization of flavonoid C-glucosyltransferases from Fagopyrum esculentum M. (buckwheat) cotyledon
Nagatomo, Yoshihisa
Usui, Shiori
Ito, Takamitsu
Kato, Akira
Shimosaka, Makoto
Taguchi, Goro
This is the peer reviewed version of the following article: Nagatomo, Y., Usui, S., Ito, T., Kato, A., Shimosaka, M. and Taguchi, G. (2014), Purification, molecular cloning and functional characterization of flavonoid C-glucosyltransferases from Fagopyrum esculentum M. (buckwheat) cotyledon. Plant J, 80: 437–448., which has been published in final form at https://doi.org/10.1111/tpj.12645 . This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
flavonoid C-glucosyltransferase
buckwheat
Fagopyrum esculentum
cotyledon
2-hydroxyflavanone
germination
vitexin
C-Glycosides are characterized by their C-C bonds in which the anomeric carbon of the sugar moieties is directly bound to the carbon atom of aglycon. C-Glycosides are remarkably stable, as their C-C bonds are resistant to glycosidase or acid hydrolysis. A variety of plant species are known to accumulate C-glycosylflavonoids
however, the genes encoding for enzymes that catalyze C-glycosylation of flavonoids have been identified only from Oryza sativa (rice) and Zea mays (maize), and have not been identified from dicot plants. In this study, we identified the C-glucosyltransferase gene from the dicot plant Fagopyrum esculentumM. (buckwheat). We purified two isozymes from buckwheat seedlings that catalyze C-glucosylation of 2-hydroxyflavanones, which are expressed specifically in the cotyledon during seed germination. Following purification we isolated the cDNA corresponding to each isozyme [FeCGTa (UGT708C1) and FeCGTb (UGT708C2)]. When expressed in Escherichia coli, both proteins demonstrated C-glucosylation activity towards 2-hydroxyflavanones, dihydrochalcone, trihydroxyacetophenones and other related compounds with chemical structures similar to 2,4,6-trihydroxyacetophenone. Molecular phylogenetic analysis of plant glycosyltransferases shows that flavonoid C-glycosyltransferases form a different clade with other functionally analyzed plant glycosyltransferases.
Article
PLANT JOURNAL. 80(3):437-448 (2014)
WILEY-BLACKWELL
2014-11
eng
journal article
VoR
http://hdl.handle.net/10091/00019714
https://soar-ir.repo.nii.ac.jp/records/18952
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=25142187
25142187
https://doi.org/10.1111/tpj.12645
10.1111/tpj.12645
0960-7412
AA10846815
PLANT JOURNAL
80
3
437
448
https://soar-ir.repo.nii.ac.jp/record/18952/files/Purification_molecular_cloning_functional_characterization.pdf
application/pdf
9.7 MB
2017-05-23