『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=244551EID:244551, Map:0, LastModified:2013年4月11日(木) 14:04:54, Operator:[松井 栄里], Avail:TRUE, Censor:0, Owner:[宇都 義浩], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
招待 (推奨):
審査 (推奨): Peer Review [継承]
カテゴリ (推奨): 研究 [継承]
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨): 1.生命情報工学 (2006年4月1日〜2016年3月31日) [継承]
著者 (必須): 1. (英) Tsurumaru Yusuke (日) (読)
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学籍番号 (推奨):
[継承]
2. (英) Sasaki Kanako (日) (読)
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学籍番号 (推奨):
[継承]
3. (英) Miyawaki Tatsuya (日) (読)
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4.宇都 義浩 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.応用生命系.応用生物資源学分野]/[徳島大学.生物資源産業学部.生物資源産業学科.応用生命講座])
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[継承]
5. (英) Momma Takayuki (日) (読)
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6. (英) Umemoto Naoyuki (日) (読)
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学籍番号 (推奨):
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7. (英) Momose Masaki (日) (読)
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[継承]
8. (英) Yazaki Kazufumi (日) (読)
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題名 (必須): (英) HlPT-1, a membrane-bound prenyltransferase responsible for the biosynthesis of bitter acids in hops  (日)    [継承]
副題 (任意):
要約 (任意): (英) Female flowers of hop (Humulus lupulus L.) develop a large number of glandular trichomes called lupulin glands that contain a variety of prenylated compounds such as α- and β-acid (humulone and lupulone, respectively), as well as xanthohumol, a chalcone derivative. These prenylated compounds are biosynthesized by prenyltransferases catalyzing the transfer of dimethylallyl moiety to aromatic substances. In our previous work, we found HlPT-1 a candidate gene for such a prenyltransferase in a cDNA library constructed from lupulin-enriched flower tissues. In this study, we have characterized the enzymatic properties of HlPT-1 using a recombinant protein expressed in baculovirus-infected insect cells. HlPT-1 catalyzed the first transfer of dimethylallyl moiety to phloroglucinol derivatives, phlorisovalerophenone, phlorisobutyrophenone and phlormethylbutanophenone, leading to the formation of humulone and lupulone derivatives. HlPT-1 also recognized naringenin chalcone as a flavonoid substrate to yield xanthohumol, and this broad substrate specificity is a unique character of HlPT-1 that is not seen in other reported flavonoid prenyltransferases, all of which show strict specificity for their aromatic substrates. Moreover, unlike other aromatic substrate prenyltransferases, HlPT-1 revealed an exclusive requirement for Mg(2+) as a divalent cation for its enzymatic activity and also showed exceptionally narrow optimum pH at around pH 7.0.  (日)    [継承]
キーワード (推奨): 1. (英) Aromatic substrate prenyltransferase (日) (読) [継承]
2. (英) Acylphloroglucinol (日) (読) [継承]
3. (英) Hop (日) (読) [継承]
4. (英) Humulone (日) (読) [継承]
5. (英) Lupulone (日) (読) [継承]
発行所 (推奨): Elsevier (->組織[Elsevier Science]) [継承]
誌名 (必須): Biochemical and Biophysical Research Communications ([Elsevier])
(pISSN: 0006-291X, eISSN: 1090-2104)

ISSN (任意): 1090-2104
ISSN: 0006-291X (pISSN: 0006-291X, eISSN: 1090-2104)
Title: Biochemical and biophysical research communications
Title(ISO): Biochem. Biophys. Res. Commun.
Publisher: Elsevier Inc.
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 417 [継承]
(必須): 1 [継承]
(必須): 393 398 [継承]
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年月日 (必須): 西暦 2012年 1月 6日 (平成 24年 1月 6日) [継承]
URL (任意):
DOI (任意): 10.1016/j.bbrc.2011.11.125    (→Scopusで検索) [継承]
PMID (任意): 22166201    (→Scopusで検索) [継承]
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WOS (任意): 000299491600067 [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1016/j.bbrc.2011.11.125  (日)    [継承]
2.(英) Article.Affiliation: Laboratory of Plant Gene Expression, Research Institute for Sustainable Humanosphere, Kyoto University, Gokasho, Uji, Japan.  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Yusuke Tsurumaru, Kanako Sasaki, Tatsuya Miyawaki, Yoshihiro Uto, Takayuki Momma, Naoyuki Umemoto, Masaki Momose and Kazufumi Yazaki : HlPT-1, a membrane-bound prenyltransferase responsible for the biosynthesis of bitter acids in hops, Biochemical and Biophysical Research Communications, Vol.417, No.1, 393-398, 2012.
欧文冊子 ● Yusuke Tsurumaru, Kanako Sasaki, Tatsuya Miyawaki, Yoshihiro Uto, Takayuki Momma, Naoyuki Umemoto, Masaki Momose and Kazufumi Yazaki : HlPT-1, a membrane-bound prenyltransferase responsible for the biosynthesis of bitter acids in hops, Biochemical and Biophysical Research Communications, Vol.417, No.1, 393-398, 2012.

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