『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
ID: Pass:

登録内容 (EID=154876)

EID=154876EID:154876, Map:0, LastModified:2016年7月5日(火) 20:47:31, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[木戸 博], 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):
カテゴリ (推奨):
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨): 1.徳島大学.分子酵素学研究センター (〜2007年3月31日/->組織[徳島大学.疾患酵素学研究センター]) [継承]
著者 (必須): 1.矢野 仁康
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
2. (英) S. Mori (日) (読)
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
3.木戸 博 ([徳島大学.先端酵素学研究所.重点研究部門])
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
題名 (必須): (英) Intrinsic Nucleoside Diphosphate Kinase-like Activity is a Novel Function of the 20S Proteasome  (日)    [継承]
副題 (任意):
要約 (任意): (英) The eukaryotic 20 S proteasome is the prototype of a new family of the N-terminal nucleophil hydrolases and is composed of numerous low molecular mass subunits arranged in a stack of four rings, each containing seven different alpha- or beta-subunits. Among the beta-type subunits in the yeast proteasome, three proteolytically active ones were identified, although the functions of the other beta- and alpha-type subunits remain to be clarified. We report here that the purified 20 S proteasome exhibits intrinsic nucleoside diphosphate (NDP) kinase-like activity. The proteasome exhibited a preference for ATP and dATP as phosphate donors, and a broad specificity for NDPs, other than GDP, as phosphate acceptors, unlike conventional NDP kinase, which catalyzes the transfer of gamma-phosphate between NDPs and nucleoside triphosphates. During the transfer of gamma-phosphate, the proteasome formed acid-labile phosphohistidine as autophosphorylated intermediates, and NDP-dependent dephosphorylation of the latter then occurred. These enzymatic properties are similar to those of the molecular chaperone, Hsp70, which also exhibits intrinsic NDP kinase-like activity, instead of ATPase activity. C5 among the beta-type subunits and C8 among the alpha-type subunits were autophosphorylated during the gamma-phosphate transfer reaction and were photoaffinity labeled with 8-azido-[alpha-(32)P]ATP, suggesting that the C5 and C8 subunits of the proteasome are responsible for the NDP kinase-like activity.  (日)    [継承]
キーワード (推奨): 1. (英) Adenosine Diphosphate (日) (読) [継承]
2. (英) Adenosine Triphosphate (日) (読) [継承]
3. (英) Amino Acid Sequence (日) (読) [継承]
4. (英) Cysteine Endopeptidases (日) (読) [継承]
5. (英) Cytidine Diphosphate (日) (読) [継承]
6. (英) Humans (日) (読) [継承]
7. (英) Kinetics (日) (読) [継承]
8. (英) Molecular Sequence Data (日) (読) [継承]
9. (英) Multienzyme Complexes (日) (読) [継承]
10. (英) Nucleoside-Diphosphate Kinase (日) (読) [継承]
11. (英) Peptide Fragments (日) (読) [継承]
12. (英) Phosphorylation (日) (読) [継承]
13. (英) Proteasome Endopeptidase Complex (日) (読) [継承]
14. (英) Sequence Analysis, Protein (日) (読) [継承]
15. (英) Substrate Specificity (日) (読) [継承]
16. (英) Tumor Cells, Cultured (日) (読) [継承]
発行所 (推奨):
誌名 (必須): The Journal of Biological Chemistry ([The American Society for Biochemistry and Molecular Biology])
(pISSN: 0021-9258, eISSN: 1083-351X)

ISSN (任意): 0021-9258
ISSN: 0021-9258 (pISSN: 0021-9258, eISSN: 1083-351X)
Title: The Journal of biological chemistry
Title(ISO): J Biol Chem
Publisher: American Society for Biochemistry and Molecular Biology
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
[継承]
[継承]
(必須): 274 [継承]
(必須): 48 [継承]
(必須): 34375 34382 [継承]
都市 (任意):
年月日 (必須): 西暦 1999年 4月 12日 (平成 11年 4月 12日) [継承]
URL (任意):
DOI (任意): 10.1074/jbc.274.48.34375    (→Scopusで検索) [継承]
PMID (任意): 10567415    (→Scopusで検索) [継承]
NAID (任意):
WOS (任意):
Scopus (任意):
評価値 (任意):
被引用数 (任意):
指導教員 (推奨):
備考 (任意): 1.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Mihiro Yano, Mori S. and Hiroshi Kido : Intrinsic Nucleoside Diphosphate Kinase-like Activity is a Novel Function of the 20S Proteasome, The Journal of Biological Chemistry, Vol.274, No.48, 34375-34382, 1999.
欧文冊子 ● Mihiro Yano, Mori S. and Hiroshi Kido : Intrinsic Nucleoside Diphosphate Kinase-like Activity is a Novel Function of the 20S Proteasome, The Journal of Biological Chemistry, Vol.274, No.48, 34375-34382, 1999.

関連情報

Number of session users = 0, LA = 1.09, Max(EID) = 382839, Max(EOID) = 1022791.