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金属プロテアーゼの活性部位の構造 : 新奇な酵素活性部位を持つジペプチジルペプチダーゼⅢを中心に
https://mdu.repo.nii.ac.jp/records/495
https://mdu.repo.nii.ac.jp/records/49566a394af-0a22-480b-b386-d43a7a0db6bc
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
matsumoto_shigaku_32-01-02.pdf (2.1 MB)
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| Item type | Journal Article(1) | |||||||
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| 公開日 | 2012-05-24 | |||||||
| タイトル | ||||||||
| タイトル | 金属プロテアーゼの活性部位の構造 : 新奇な酵素活性部位を持つジペプチジルペプチダーゼⅢを中心に | |||||||
| 言語 | ||||||||
| 言語 | jpn | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | metalloprotease | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | catalytic domain | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | dipeptidyl peptidase | |||||||
| 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 | journal article | |||||||
| その他（別言語等）のタイトル | ||||||||
| その他のタイトル | Structure of catalytic domain of metalloprotease : mainly considering the novel motifidentified on DPP III | |||||||
| 著者 |
深澤, 加與子
× 深澤, 加與子
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| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | Almost metalloproteases contain a zinc atom in the active domain coordinating three amino acid residues on the protein and a single water molecule. Metalloproteases are classified into several groups according to the amino acid sequence of the catalytic domain. Dipeptidyl peptidase (DPP) III, which catalyzes the removal of unsubstituted, N-terminal dipeptide from peptides and β-naphthylamide derivatives, had been classified as a serine protease until the amino acid sequence of DPP III was determined. The presence of a similar HELLGH motif on DPP III as the zinc metalloprotease motif HEXXH raises the possibility that DPP III is a metalloprotease. By electrothermal atomic absorption spectrometry, DPP III was demonstrated to contain one mol of zinc per mol of protein, and on zinc-binding study, the dissociation constant (K_d) of DPP III was detected to be (2.5±0.5)×10^<-13> M. These findings show that DPP III is a mono zinc metalloprotease. Furthermore, mutagenesis experiments confirmed that residues His^<450>, His^<455> and Glu^<451> on DPP III are involved in zinc coordination and catalytic activity, and that residue Glu^<508> is a third ligand of zinc atom. DPP III has been newly classified as a metalloprotease containing a novel zinc-binding domain "HELLGH motif". The three-dimensional structure of the catalytic domain and putative catalytic mechanism of DPP III are deduced from that of thermolysin proposed by Matthews along with these site-directed mutagenesis studies on DPP III. | |||||||
| 書誌情報 |
松本歯学 巻 32, 号 1, p. 11-20, 発行日 2006-04-30 |
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| 出版者 | ||||||||
| 出版者 | 松本歯科大学学会 | |||||||
| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0385-1613 | |||||||
| 書誌レコードID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AN00232590 | |||||||
| フォーマット | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | application/pdf | |||||||
| 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 | |||||||
