『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=272514EID:272514, Map:0, LastModified:2015年4月1日(水) 20:22:53, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[真板 宣夫], 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): 研究 [継承]
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨):
著者 (必須): 1.真板 宣夫
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[継承]
2. (英) Tsukimura Takahiro (日) (読)
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3.谷口 貴子
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4. (英) Saito Seiji (日) (読)
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[継承]
5. (英) Ohno Kazuki (日) (読)
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6.谷口 寿章
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7. (英) Sakuraba Hitoshi (日) (読)
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題名 (必須): (英) Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module  (日)    [継承]
副題 (任意):
要約 (任意): (英) N-glycosylation is a major posttranslational modification that endows proteins with various functions. It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood. Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module. Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate. A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372. The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes. Our study demonstrates a previously unrecognized function of N-glycans.  (日)    [継承]
キーワード (推奨): 1. (英) Amino Acid Sequence (日) (読) [継承]
2. (英) Binding Sites (日) (読) [継承]
3. (英) Biocatalysis (日) (読) [継承]
4. (英) Circular Dichroism (日) (読) [継承]
5. (英) Crystallography, X-Ray (日) (読) [継承]
6. (英) Dermatan Sulfate (日) (読) [継承]
7. (英) Electrophoresis, Polyacrylamide Gel (日) (読) [継承]
8. (英) Heparitin Sulfate (日) (読) [継承]
9. (英) Humans (日) (読) [継承]
10. (英) Iduronidase (日) (読) [継承]
11. (英) Kinetics (日) (読) [継承]
12. (英) Mannose (日) (読) [継承]
13. (英) Models, Molecular (日) (読) [継承]
14. (英) Molecular Sequence Data (日) (読) [継承]
15. (英) Mucopolysaccharidosis I (日) (読) [継承]
16. (英) Mutation (日) (読) [継承]
17. (英) Polysaccharides (日) (読) [継承]
18. (英) Protein Binding (日) (読) [継承]
19. (英) Protein Structure, Tertiary (日) (読) [継承]
20. (英) Sequence Homology, Amino Acid (日) (読) [継承]
21. (英) Substrate Specificity (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): 1091-6490
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): 110 [継承]
(必須): 36 [継承]
(必須): 14628 14633 [継承]
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年月日 (必須): 西暦 2013年 9月 3日 (平成 25年 9月 3日) [継承]
URL (任意):
DOI (任意): 10.1073/pnas.1306939110    (→Scopusで検索) [継承]
PMID (任意): 23959878    (→Scopusで検索) [継承]
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WOS (任意): 000323886200039 [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1073/pnas.1306939110  (日)    [継承]
2.(英) Article.DataBankList.DataBank.DataBankName: PDB  (日)    [継承]
3.(英) Article.DataBankList.DataBank.AccessionNumberList.AccessionNumber: 3W81  (日)    [継承]
4.(英) Article.DataBankList.DataBank.AccessionNumberList.AccessionNumber: 3W82  (日)    [継承]
5.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
6.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]
7.(英) OtherID: PMC3767532  (日)    [継承]
8.(英) KeywordList.Keyword: N-linked glycan  (日)    [継承]
9.(英) KeywordList.Keyword: X-ray crystallography  (日)    [継承]
10.(英) KeywordList.Keyword: glycoside hydrolase family 39  (日)    [継承]

標準的な表示

和文冊子 ● Nobuo Maita, Takahiro Tsukimura, Takako Taniguchi, Seiji Saito, Kazuki Ohno, Hisaaki Taniguchi and Hitoshi Sakuraba : Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module, Proceedings of the National Academy of Sciences of the United States of America, Vol.110, No.36, 14628-14633, 2013.
欧文冊子 ● Nobuo Maita, Takahiro Tsukimura, Takako Taniguchi, Seiji Saito, Kazuki Ohno, Hisaaki Taniguchi and Hitoshi Sakuraba : Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module, Proceedings of the National Academy of Sciences of the United States of America, Vol.110, No.36, 14628-14633, 2013.

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