Item type |
学術雑誌論文 / Journal Article(1) |
公開日 |
2010-05-26 |
タイトル |
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タイトル |
Purification and characterization of UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase, with broad substrate specificity from tobacco cultured cells |
言語 |
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言語 |
eng |
DOI |
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関連識別子 |
https://doi.org/10.1016/S0168-9452(00)00270-3 |
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関連名称 |
10.1016/S0168-9452(00)00270-3 |
キーワード |
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主題 |
Nicotiana tabacum L. cv Bright Yellow, glucosyltransferase, scopoletin, esculetin, flavonoid |
資源タイプ |
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資源 |
http://purl.org/coar/resource_type/c_6501 |
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タイプ |
journal article |
著者 |
Taguchi, G
Imura, H
Maeda, Y
Kodaira, R
Hayashida, N
Shimosaka, M
Okazaki, M
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信州大学研究者総覧へのリンク |
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氏名 |
Taguchi, G |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.uCDpjekV.html |
信州大学研究者総覧へのリンク |
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氏名 |
Hayashida, N |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.HVfmjekV.html |
信州大学研究者総覧へのリンク |
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氏名 |
Shimosaka, M |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.ZekmjekV.html |
出版者 |
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出版者 |
Elsevier |
引用 |
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内容記述 |
Plant Science. 157(1):105-112 (2000) |
書誌情報 |
Plant Science
巻 157,
号 1,
p. 105-112,
発行日 2000
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抄録 |
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内容記述 |
The enzyme UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase (CGTase), which catalyzes the formation of scopolin from scopoletin, was purified approximately 1200-fold from a culture of 2,4-D-treated tobacco cells (Nicotiana tabacum L. cv. Bright Yellow T-13) with a yield of 7%. Purification to apparent homogeneity, as judged by SDS-PAGE, was achieved by sequential anion-exchange chromatography, hydroxyapatite chromatography, gel filtration, a second round of anion-exchange chromatography, and affinity chromatography on UDP-glucuronic acid agarose. The purified enzyme had a pH optimum of 7.5, an isoelectric point (pI) of 5.0, and a molecular mass of 49 kDa. The enzyme did not require metal cofactors for activity. Its activity was inhibited by Zn2+, Co2+ and Cu2+ ions, as well as by SH-blocking reagents. The K-m values for UDP-glucose, scopoletin and esculetin were 43, 150 and 25 mu M. respectively. A study of the initial rate of the reaction suggested that the reaction proceeded via a sequential mechanism. The purified enzyme preferred hydroxycoumarins as substrates but also exhibited significant activity with flavonoids. A database search using the amino terminus amino acid sequence of CGTase revealed strong homology to the amino acid sequences of other glucosyltransferases in plants. |
資源タイプ(コンテンツの種類) |
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内容記述 |
Article |
ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
0168-9452 |
書誌レコードID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA10531279 |
他の資源との関係:URI |
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関連識別子 |
http://www.elsevier.com/locate/plantsci |
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関連名称 |
http://www.elsevier.com/locate/plantsci |
PubMed |
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関連識別子 |
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=10940474 |
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関連名称 |
10940474 |
出版タイプ |
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出版タイプ |
AM |
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出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
WoS |
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URL |
http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000088553500011 |