著作: [真板 宣夫]/Tsukimura Takahiro/[谷口 貴子]/Saito Seiji/Ohno Kazuki/[谷口 寿章]/Sakuraba Hitoshi/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]
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削除する| 種別 | 必須 | 学術論文(審査論文) | |||
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| 言語 | 必須 | 英語 | |||
| 招待 | 推奨 | ||||
| 審査 | 推奨 | ||||
| カテゴリ | 推奨 | 研究 | |||
| 共著種別 | 推奨 | ||||
| 学究種別 | 推奨 | ||||
| 組織 | 推奨 | ||||
| 著者 | 必須 | ||||
| 題名 | 必須 |
(英) Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module |
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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. |
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| キーワード | 推奨 |
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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)
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| 巻 | 必須 | 110 | |||
| 号 | 必須 | 36 | |||
| 頁 | 必須 | 14628 14633 | |||
| 都市 | 任意 | ||||
| 年月日 | 必須 | 2013年 9月 3日 | |||
| URL | 任意 | ||||
| DOI | 任意 | 10.1073/pnas.1306939110 (→Scopusで検索) | |||
| PMID | 任意 | 23959878 (→Scopusで検索) | |||
| NAID | 任意 | ||||
| WOS | 任意 | 000323886200039 | |||
| Scopus | 任意 | ||||
| 評価値 | 任意 | ||||
| 被引用数 | 任意 | ||||
| 指導教員 | 推奨 | ||||
| 備考 | 任意 |
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