Identification of an inducible glucosyltransferase from Phytolacca americana L. cells that are capable of glucosylating capsaicin
-
- Noguchi Akio
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Kunikane Satoshi
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Homma Hiroaki
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Liu Wenhai
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Sekiya Takashi
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Hosoya Miho
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Kwon Soonil
- Department of Life Science, Faculty of Science, Okayama University of Science
-
- Ohiwa Shingo
- Department of Life Science, Faculty of Science, Okayama University of Science
-
- Katsuragi Hisashi
- Sunny Health Co. Ltd.
-
- Nishino Tokuzo
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Takahashi Seiji
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
-
- Hamada Hiroki
- Department of Life Science, Faculty of Science, Okayama University of Science
-
- Nakayama Toru
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Search this article
Abstract
Cell suspension cultures of Phytolacca americana L. (pokeweed) are capable of glycosylating capsaicinoids that have several biomedical applications. To identify the capsaicinoid glucosyltransferase involved in this biotransformation, we isolated three full-length cDNAs (PaGTs) encoding homologs of plant secondary product glycosyltransferases from cultured cells of P. americana L. These glycosyltransferase cDNAs were heterologously expressed in Escherichia coli cells and the expressed products were functionally characterized. Although all of these glycosyltransferases displayed broad glucosyl-acceptor specificities toward phenolics, capsaicinoid glucosyltransferase activity was found only for one of the cloned enzymes, PaGT3. Phylogenetic analysis showed that PaGT3 is the most closely related to betanidin 5-O-glucosyltransferase from Dorotheanthus bellidiformis, and in fact, it displayed a weak betanidin 5-O-glucosyltransferase activity. Transcription analyses showed that the expression of PaGT3 in P. americana L. was strongly induced by exposure of the cells to capsaicin (0.65 mM). These results show that PaGT3 should be, at least in part, responsible for the capsaicinoid glucosyltransferase activity of this plant.
Journal
-
- Plant Biotechnology
-
Plant Biotechnology 26 (3), 285-292, 2009
Japanese Society for Plant Biotechnology
- Tweet
Details 詳細情報について
-
- CRID
- 1390282679303626112
-
- NII Article ID
- 10024853783
-
- NII Book ID
- AA11250821
-
- ISSN
- 13476114
- 13424580
-
- NDL BIB ID
- 10258697
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed