『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=65078EID:65078, Map:0, LastModified:2017年4月8日(土) 18:52:14, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[佐藤 高則], 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]
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学究種別 (推奨):
組織 (推奨): 1.青山学院大学.理工学部 [継承]
著者 (必須): 1. (英) Shinoda Hiroshi (日) (読)
役割 (任意): 共著 [継承]
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2. (英) Hattori Manabu (日) (読)
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3. (英) Shimizu Atsushi (日) (読)
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4. (英) Samejima Tatsuya (日) (読)
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5.佐藤 高則
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題名 (必須): (英) Hydrophobic Interactions of Val-75 are Critical for Oligomeric Thermostability of Inorganic Pyrophosphatase from Bacillus stearothermophilus.  (日)    [継承]
副題 (任意):
要約 (任意): (英) To determine the role of Val75 in the oligomeric structure of trimeric inorganic pyrophosphatase (PPase) [EC 3.6.1.1] from Bacillus stearothermophilus (Bst.), we used site-directed mutagenesis to prepare variants in which Val75 was replaced by Ala, Phe, Leu, Ile, Lys, Gln, and Asp. As a result, the variants in which valine is replaced by hydrophobic residues such as Ala, Phe, Leu, and Ile (V75A, F, L, and I) show almost the same level of enzyme activity and thermostability as the wild type enzyme, whereas variants with hydrophilic residue replacements such as Lys, Gln, and Asp (V75K, Q, and D) showed gross reductions in enzyme activity and thermostability. The dissociation of V75K and V75D from trimer to monomers occurred rapidly as the temperature rose, while V75F, V75L, and V75I dissociated more slowly than the wild type. There was no particular effect of heat treatment on the dissociation of V75A or V75Q, but these variants were slightly dissociated even in the native state. Thus, we conclude that Val75 may locate at the interface between the monomers and its hydrophobic interactions with its surroundings may play a key role in the thermostability and oligomeric subunit interactions of the enzyme.  (日) 中等度好熱性細菌Bacillus stearothermophilus由来無機ピロリン酸加水分解酵素は,通常3量体を形成している.サブユニット構造と耐熱性の関係を検討するために,単量体界面に存在すると推定されるVal75に着目し,部位特異的変異法を用いて7種の置換変異体を作製し,それらの解析を行なった.その結果,この部位の親水性残基への置換は,大幅な耐熱性および四次構造の安定性の減少を導いた.   [継承]
キーワード (推奨): 1. (英) Enzyme Stability (日) (読) [継承]
2. (英) Geobacillus stearothermophilus (日) (読) [継承]
3. (英) Hot Temperature (日) (読) [継承]
4. (英) Inorganic Pyrophosphatase (日) (読) [継承]
5. (英) Mutagenesis, Site-Directed (日) (読) [継承]
6. (英) Protein Conformation (日) (読) [継承]
7. (英) Pyrophosphatases (日) (読) [継承]
8. (英) Recombinant Proteins (日) (読) [継承]
9. (英) Structure-Activity Relationship (日) (読) [継承]
10. (英) Temperature (日) (読) [継承]
11. (英) Valine (日) (読) [継承]
発行所 (推奨): 日本生化学会 [継承]
誌名 (必須): The Journal of Biochemistry ([日本生化学会])
(pISSN: 0021-924X, eISSN: 1756-2651)

ISSN (任意): 0021-924X
ISSN: 0021-924X (pISSN: 0021-924X, eISSN: 1756-2651)
Title: Journal of biochemistry
Title(ISO): J Biochem
Supplier: Oxford University Press
Publisher: Oxford University Press
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年月日 (必須): 西暦 1999年 1月 1日 (平成 11年 1月 1日) [継承]
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PMID (任意): 9880797    (→Scopusで検索) [継承]
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WOS (任意): 000078361100010 [継承]
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備考 (任意): 1.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]

標準的な表示

和文冊子 ● Hiroshi Shinoda, Manabu Hattori, Atsushi Shimizu, Tatsuya Samejima and Takanori Satoh : Hydrophobic Interactions of Val-75 are Critical for Oligomeric Thermostability of Inorganic Pyrophosphatase from Bacillus stearothermophilus., The Journal of Biochemistry, Vol.125, No.1, 58-63, 1999.
欧文冊子 ● Hiroshi Shinoda, Manabu Hattori, Atsushi Shimizu, Tatsuya Samejima and Takanori Satoh : Hydrophobic Interactions of Val-75 are Critical for Oligomeric Thermostability of Inorganic Pyrophosphatase from Bacillus stearothermophilus., The Journal of Biochemistry, Vol.125, No.1, 58-63, 1999.

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