『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=171768EID:171768, Map:0, LastModified:2016年9月27日(火) 16:45:06, Operator:[福井 清], 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.疾患酵素学研究センター (2007年4月1日〜2016年3月31日/->組織[徳島大学.先端酵素学研究所.次世代酵素学研究領域]) [継承]
著者 (必須): 1. (英) Kawazoe Tomoya (日) 川添 僚也 (読) かわぞえ ともや
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2. (英) Park Ki Hwan (日) 朴 煥埼 (読) ぱく はんき
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3. (英) Iwana Sanae (日) 岩名 沙奈恵 (読) いわな さなえ
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4.津下 英明 (徳島文理大学健康科学研究所)
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5.福井 清 ([徳島大学])
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題名 (必須): (英) Human D-amino acid oxidase: an update and review  (日)    [継承]
副題 (任意):
要約 (任意): (英) The flavoprotein D-amino acid oxidase (DAO) degrades the gliotransmitter D-Ser, a potent activator of N-methyl-D-aspartate-type glutamate receptors. A body of evidence suggests that DAO, together with its activator, G72 protein, may play a key role in the pathophysiology of schizophrenia. It has also been suggested that 3,4-dihydroxy-D-phenylalanine (D-DOPA), the stereoisomer of 3,4-dihydroxy-L-phenylalanine (L-DOPA), is oxidized by DAO and converted to dopamine via an alternative biosynthetic pathway. We determined the crystal structures of human DAO in complex with the reaction products of two clinically important substrates, D-Ser and D-DOPA. Kinetic data show that the maximum velocity is much greater for D-DOPA than that for D-Ser, which strongly supports the proposed alternative pathway for dopamine biosynthesis in the treatment of Parkinson's disease. In addition, biochemical characterization of human DAO indicates that it binds FAD more weakly than does porcine D-amino acid oxidase (pDAO) and exists as a stable homodimer, even in the apoprotein form. Determination of the structures of human DAO in various states reveals that, in contrast to pDAO, the hydrophobic-Val-Ala-Ala-Gly-Leu (VAAGL) stretch (residues 47-51, structurally ambivalent peptide) located at the si-face of the flavin ring assumes a uniquely stable conformation, which provides a structural basis for the unique kinetic features of human DAO.  (日)    [継承]
キーワード (推奨): 1.D-アミノ酸酸化酵素 (D-amino acid oxidase) [継承]
2.D-セリン (D-serine) [継承]
3.統合失調症 (schizophrenia) [継承]
4. (英) D-DOPA (日) (読) [継承]
5.パーキンソン病 (Parkinson's disease) [継承]
発行所 (推奨): Wiley Periodicals, Inc. [継承]
誌名 (必須): Chemical Record ([社団法人 日本化学会])
(pISSN: 1527-8999, eISSN: 1528-0691)

ISSN (任意): 1527-8999
ISSN: 1527-8999 (pISSN: 1527-8999, eISSN: 1528-0691)
Title: Chemical record (New York, N.Y.)
Title(ISO): Chem Rec
Supplier: The Chemical Society of Japan
Publisher: Wiley Publishing
 (NLM Catalog  (Wiley  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 7 [継承]
(必須): 5 [継承]
(必須): 305 315 [継承]
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年月日 (必須): 西暦 2007年 10月 22日 (平成 19年 10月 22日) [継承]
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DOI (任意): 10.1002/tcr.20129    (→Scopusで検索) [継承]
PMID (任意): 17924443    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.Affiliation: Institute for Enzyme Research, The University of Tokushima, 3-18-15 Kuramoto, Tokushima 770-8503, Japan.  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Review  (日)    [継承]
4.(英) NumberOfReferences: 39  (日)    [継承]

標準的な表示

和文冊子 ● Tomoya Kawazoe, Hwan Ki Park, Sanae Iwana, Hideaki Tsuge and Kiyoshi Fukui : Human D-amino acid oxidase: an update and review, Chemical Record, Vol.7, No.5, 305-315, 2007.
欧文冊子 ● Tomoya Kawazoe, Hwan Ki Park, Sanae Iwana, Hideaki Tsuge and Kiyoshi Fukui : Human D-amino acid oxidase: an update and review, Chemical Record, Vol.7, No.5, 305-315, 2007.

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