| ○種別 (必須): | □ | 学術論文 (審査論文)
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| ○言語 (必須): | □ | 英語
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| ○招待 (推奨): |
| ○審査 (推奨): |
| ○カテゴリ (推奨): | □ | 研究
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| ○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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| 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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| 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)
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| ○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)
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| ○キーワード (推奨): | 1. | (英) Amino Acid Sequence (日) (読)
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| 2. | (英) Binding Sites (日) (読)
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| 3. | (英) Biocatalysis (日) (読)
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| 4. | (英) Circular Dichroism (日) (読)
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| 5. | (英) Crystallography, X-Ray (日) (読)
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| 6. | (英) Dermatan Sulfate (日) (読)
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| 7. | (英) Electrophoresis, Polyacrylamide Gel (日) (読)
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| 8. | (英) Heparitin Sulfate (日) (読)
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| 9. | (英) Humans (日) (読)
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| 10. | (英) Iduronidase (日) (読)
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| 11. | (英) Kinetics (日) (読)
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| 12. | (英) Mannose (日) (読)
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| 13. | (英) Models, Molecular (日) (読)
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| 14. | (英) Molecular Sequence Data (日) (読)
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| 15. | (英) Mucopolysaccharidosis I (日) (読)
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| 16. | (英) Mutation (日) (読)
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| 17. | (英) Polysaccharides (日) (読)
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| 18. | (英) Protein Binding (日) (読)
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| 19. | (英) Protein Structure, Tertiary (日) (読)
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| 20. | (英) Sequence Homology, Amino Acid (日) (読)
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| 21. | (英) Substrate Specificity (日) (読)
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| ○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 AmericaTitle(ISO): Proc Natl Acad Sci U S APublisher: National Academy of Sciences (NLM Catalog)
(Scopus)
(CrossRef)
(Scopus information is found. [need login]) | [継承] |
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| ○巻 (必須): | □ | 110
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| ○号 (必須): | □ | 36
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| ○頁 (必須): | □ | 14628 14633
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| ○都市 (任意): |
| ○年月日 (必須): | □ | 西暦 2013年 9月 3日 (平成 25年 9月 3日)
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| ○URL (任意): |
| ○DOI (任意): | □ | 10.1073/pnas.1306939110 (→Scopusで検索)
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| ○PMID (任意): | □ | 23959878 (→Scopusで検索)
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| ○NAID (任意): |
| ○WOS (任意): | □ | 000323886200039
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| ○備考 (任意): | 1. | (英) Article.ELocationID: 10.1073/pnas.1306939110 (日)
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| 2. | (英) Article.DataBankList.DataBank.DataBankName: PDB (日)
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| 3. | (英) Article.DataBankList.DataBank.AccessionNumberList.AccessionNumber: 3W81 (日)
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| 4. | (英) Article.DataBankList.DataBank.AccessionNumberList.AccessionNumber: 3W82 (日)
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| 5. | (英) Article.PublicationTypeList.PublicationType: Journal Article (日)
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| 6. | (英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't (日)
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| 7. | (英) OtherID: PMC3767532 (日)
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| 8. | (英) KeywordList.Keyword: N-linked glycan (日)
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| 9. | (英) KeywordList.Keyword: X-ray crystallography (日)
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| 10. | (英) KeywordList.Keyword: glycoside hydrolase family 39 (日)
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