『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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登録内容 (EID=67190)

EID=67190EID:67190, Map:0, LastModified:2014年4月28日(月) 14:50:49, Operator:[松井 栄里], Avail:TRUE, Censor:0, Owner:[福井 清], 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.分子酵素学研究センター (〜2007年3月31日/->組織[疾患酵素学研究センター]) [継承]
著者 (必須): 1. (英) Raibekas A. Andrei (日) (読)
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学籍番号 (推奨):
[継承]
2.福井 清 ([徳島大学])
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貢献度 (任意):
学籍番号 (推奨):
[継承]
3. (英) Massey Vincent (日) (読)
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貢献度 (任意):
学籍番号 (推奨):
[継承]
題名 (必須): (英) Design and properties of human D-amino acid oxidase with covalently attached flavin  (日)    [継承]
副題 (任意):
要約 (任意): (英) An "artificial flavinylation" approach was developed to replace a native noncovalent flavin prosthetic group with a covalently attached flavin analogue in recombinant human d-amino acid oxidase. The protein residue Gly-281 was replaced with Cys by site-directed mutagenesis, followed by reaction between mutated apoenzyme and the thiol-reactive flavin analogue, 8-methylsulfonyl FAD. The stoichiometric process of flavin attachment was accompanied by gain in enzymatic activity, reaching up to 26% activity of the recombinant native enzyme. The steady-state kinetic data together with the results of limited proteolysis and benzoate-binding studies suggest that, although mutation perturbs protein structural and catalytic properties, the flavinylation alone does not have any negative impact. We conclude that, despite the implemented restraints on its mobility, the covalently attached flavin is properly positioned within the protein active site and acts efficiently during d-amino acid oxidase catalytic turnover.  (日)    [継承]
キーワード (推奨): 1. (英) Base Sequence (日) (読) [継承]
2. (英) Benzoates (日) (読) [継承]
3. (英) Catalysis (日) (読) [継承]
4. (英) D-Amino-Acid Oxidase (日) (読) [継承]
5. (英) DNA Primers (日) (読) [継承]
6. (英) Flavins (日) (読) [継承]
7. (英) Humans (日) (読) [継承]
8. (英) Hydrolysis (日) (読) [継承]
9. (英) Kinetics (日) (読) [継承]
10. (英) Mutagenesis, Site-Directed (日) (読) [継承]
11. (英) Oxidation-Reduction (日) (読) [継承]
12. (英) Spectrum Analysis (日) (読) [継承]
発行所 (推奨):
誌名 (必須): Proceedings of the National Academy of Sciences of the United States of America ([The National Academy of Sciences of the United States of America])
(pISSN: 0027-8424, eISSN: 1091-6490)

ISSN (任意): 0027-8424
ISSN: 0027-8424 (pISSN: 0027-8424, eISSN: 1091-6490)
Title: Proceedings of the National Academy of Sciences of the United States of America
Title(ISO): Proc. Natl. Acad. Sci. U.S.A.
Publisher: National Academy of Sciences
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 97 [継承]
(必須): 7 [継承]
(必須): 3089 3093 [継承]
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年月日 (必須): 西暦 2000年 3月 28日 (平成 12年 3月 28日) [継承]
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DOI (任意): 10.1073/pnas.040559597    (→Scopusで検索) [継承]
PMID (任意): 10716694    (→Scopusで検索) [継承]
NAID (任意):
WOS (任意): 000086195200026 [継承]
Scopus (任意): 2-s2.0-0034724295 [継承]
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備考 (任意): 1.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Research Support, U.S. Gov't, P.H.S.  (日)    [継承]
3.(英) OtherID: PMC16197  (日)    [継承]

標準的な表示

和文冊子 ● Andrei A. Raibekas, Kiyoshi Fukui and Vincent Massey : Design and properties of human D-amino acid oxidase with covalently attached flavin, Proceedings of the National Academy of Sciences of the United States of America, Vol.97, No.7, 3089-3093, 2000.
欧文冊子 ● Andrei A. Raibekas, Kiyoshi Fukui and Vincent Massey : Design and properties of human D-amino acid oxidase with covalently attached flavin, Proceedings of the National Academy of Sciences of the United States of America, Vol.97, No.7, 3089-3093, 2000.

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