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金属プロテアーゼにおける亜鉛結合モチーフの金属選択性(発表論文抄録(2011))
https://fukuyama-u.repo.nii.ac.jp/records/8824
https://fukuyama-u.repo.nii.ac.jp/records/8824a0869552-d6ac-4985-855b-092359673237
名前 / ファイル | ライセンス | アクション |
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深澤加與子(発表論文抄録(2011)) (80.7 kB)
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Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2017-12-25 | |||||
タイトル | ||||||
タイトル | 金属プロテアーゼにおける亜鉛結合モチーフの金属選択性(発表論文抄録(2011)) | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Metal preferences of zinc-binding motif on metalloproteases. | |||||
言語 | ||||||
言語 | eng | |||||
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 |
Fukasawa, Kayoko M
× Fukasawa, Kayoko M× Hata, Toshiyuki× Ono, Yukio× Hirose, Junzo |
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著者別名 | ||||||
識別子Scheme | WEKO | |||||
識別子 | 45884 | |||||
識別子Scheme | CiNii ID | |||||
識別子URI | http://ci.nii.ac.jp/nrid/9000000181432 | |||||
識別子 | 9000000181432 | |||||
姓名 | 深沢, 加与子 | |||||
著者別名 | ||||||
識別子Scheme | WEKO | |||||
識別子 | 45236 | |||||
識別子Scheme | CiNii ID | |||||
識別子URI | http://ci.nii.ac.jp/nrid/9000014625803 | |||||
識別子 | 9000014625803 | |||||
姓名 | 秦, 季之 | |||||
著者別名 | ||||||
識別子Scheme | WEKO | |||||
識別子 | 45238 | |||||
識別子Scheme | CiNii ID | |||||
識別子URI | http://ci.nii.ac.jp/nrid/9000002578762 | |||||
識別子 | 9000002578762 | |||||
姓名 | 小野, 行雄 | |||||
著者別名 | ||||||
識別子Scheme | WEKO | |||||
識別子 | 45879 | |||||
識別子Scheme | CiNii ID | |||||
識別子URI | http://ci.nii.ac.jp/nrid/1000070080215 | |||||
識別子 | 1000070080215 | |||||
姓名 | 廣瀬, 順造 | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other divalent cation. Almost all Co(II)- or Mn(II)-substituted enzymes maintain the catalytic activity of their zinc counterparts. However, in the case of Cu(II) substitution of zinc proteases, a great number of enzymes are not active, for example, thermolysin, carboxypeptidase A, endopeptidase from Lactococcus lactis, or aminopeptidase B, while some do have catalytic activity, for example, astacin (37%) and DPP III (100%). Based on structural studies of various metal-substituted enzymes, for example, thermolysin, astacin, aminopeptidase B, dipeptidyl peptidase (DPP) III, and del-DPP III, the metal coordination geometries of both active and inactive Cu(II)-substituted enzymes are shown to be the same as those of the wild-type Zn(II) enzymes. Therefore, the enzyme activity of a copper-ion-substituted zinc metalloprotease may depend on the flexibility of catalytic domain. | |||||
内容記述 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other divalent cation. Almost all Co(II)- or Mn(II)-substituted enzymes maintain the catalytic activity of their zinc counterparts. However, in the case of Cu(II) substitution of zinc proteases, a great number of enzymes are not active, for example, thermolysin, carboxypeptidase A, endopeptidase from Lactococcus lactis, or aminopeptidase B, while some do have catalytic activity, for example, astacin (37%) and DPP III (100%). Based on structural studies of various metal-substituted enzymes, for example, thermolysin, astacin, aminopeptidase B, dipeptidyl peptidase (DPP) III, and del-DPP III, the metal coordination geometries of both active and inactive Cu(II)-substituted enzymes are shown to be the same as those of the wild-type Zn(II) enzymes. Therefore, the enzyme activity of a copper-ion-substituted zinc metalloprotease may depend on the flexibility of catalytic domain. | |||||
書誌情報 |
福山大学薬学部研究年報 en : Annual report of the Faculty of Pharmacy & Pharmaceutical Sciences, Fukuyama University 号 30, p. 22-22, 発行日 2012-12-25 |
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出版者 | ||||||
出版者 | 福山大学薬学部 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0288-724X | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN10064550 | |||||
PubMed番号 | ||||||
識別子タイプ | PMID | |||||
関連識別子 | 22312463 | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | 10.4061/2011/574816 |