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UDP-GalNAc : Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) の構造活性相関 : GalNAc-T1のレクチン様ドメインの機能解析
http://hdl.handle.net/10965/464
http://hdl.handle.net/10965/46437b9d03a-ab7d-4498-ace2-045c93365912
名前 / ファイル | ライセンス | アクション |
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Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2017-09-30 | |||||
タイトル | ||||||
言語 | ja | |||||
タイトル | UDP-GalNAc : Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) の構造活性相関 : GalNAc-T1のレクチン様ドメインの機能解析 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Structure-function Relationship of UDP-GalNAc : Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) : Function of the Lectin Domain of GalNAc-T1 | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | ムチン型O-グリコシレーション,GalNAc 転移酵素,レクチン様ドメイン,構造活性相関,部位特異的変異 | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | mucin-type O-glycosylation | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | GalNAc-transferase | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | lectin domain | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | structurefunction relationship | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | site-directed mutagenesis | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | departmental bulletin paper | |||||
著者 |
天野, 麻理
× 天野, 麻理 |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The initial step of mucin-type O-glycosylation is catalyzed by UDP-GalNAc : polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). GalNAc-transferases contain a lectin domain at the C-terminus, consisting of three tandem repeats (α, β, and γ). I have reevaluated the role of the GalNAc-T1 lectin domain in this study, because the putative lectin domain of this enzyme is reportedly not functional. Deletion of the lectin domain resulted in a complete loss of enzymatic activity. I found that GalNAc-T1 has two activities distinguished by their sensitivities to inhibition with free GalNAc; one activity is sensitive, the other is resistant. In my experiments, the former activity is represented by the O-glycosylation of apomucin, an acceptor that contains multiple glycosylation sites, and the latter by synthetic peptides that contain a single glycosylation site. Site-directed mutagenesis of the lectin domain selectively reduced the follow-up activity, and identified Asp444 in the α repeat as the most important site for GalNAc recognition. I also found that the β repeat recognizes GalNAc and is involved in glycosylation of acceptors with multiple glycosylation sites. These results indicate that the lectin domain of GalNAc-T1 has at least two functional repeats, allowing the possibility of multivalent interactions with GalNAc residues on the acceptor peptide during glycosylation. | |||||
書誌情報 |
京都産業大学論集. 自然科学系列 巻 33, p. 60-85, 発行日 2004-03 |
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出版者 | ||||||
出版者 | 京都産業大学 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 1348-3323 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA11923897 | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |