{"created":"2023-06-19T09:51:36.615738+00:00","id":8824,"links":{},"metadata":{"_buckets":{"deposit":"c6d81ba5-0a15-4ada-bd52-d409a9f035b5"},"_deposit":{"created_by":18,"id":"8824","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"8824"},"status":"published"},"_oai":{"id":"oai:fukuyama-u.repo.nii.ac.jp:00008824","sets":["502:503:627:779"]},"author_link":["45238","46187","46186","46189","45884","45879","45236","46188"],"item_10002_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2012-12-25","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"30","bibliographicPageEnd":"22","bibliographicPageStart":"22","bibliographic_titles":[{"bibliographic_title":"福山大学薬学部研究年報"},{"bibliographic_title":"Annual report of the Faculty of Pharmacy & Pharmaceutical Sciences, Fukuyama University","bibliographic_titleLang":"en"}]}]},"item_10002_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"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.","subitem_description_type":"Abstract"}]},"item_10002_description_6":{"attribute_name":"内容記述","attribute_value_mlt":[{"subitem_description":"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.","subitem_description_type":"Other"}]},"item_10002_full_name_3":{"attribute_name":"著者別名","attribute_value_mlt":[{"nameIdentifiers":[{"nameIdentifier":"45884","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"9000000181432","nameIdentifierScheme":"CiNii ID","nameIdentifierURI":"http://ci.nii.ac.jp/nrid/9000000181432"}],"names":[{"name":"深沢, 加与子"}]},{"nameIdentifiers":[{"nameIdentifier":"45236","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"9000014625803","nameIdentifierScheme":"CiNii ID","nameIdentifierURI":"http://ci.nii.ac.jp/nrid/9000014625803"}],"names":[{"name":"秦, 季之"}]},{"nameIdentifiers":[{"nameIdentifier":"45238","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"9000002578762","nameIdentifierScheme":"CiNii ID","nameIdentifierURI":"http://ci.nii.ac.jp/nrid/9000002578762"}],"names":[{"name":"小野, 行雄"}]},{"nameIdentifiers":[{"nameIdentifier":"45879","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"1000070080215","nameIdentifierScheme":"CiNii ID","nameIdentifierURI":"http://ci.nii.ac.jp/nrid/1000070080215"}],"names":[{"name":"廣瀬, 順造"}]}]},"item_10002_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"福山大学薬学部"}]},"item_10002_relation_13":{"attribute_name":"PubMed番号","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"22312463","subitem_relation_type_select":"PMID"}}]},"item_10002_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"10.4061/2011/574816","subitem_relation_type_select":"DOI"}}]},"item_10002_source_id_11":{"attribute_name":"書誌レコードID","attribute_value_mlt":[{"subitem_source_identifier":"AN10064550","subitem_source_identifier_type":"NCID"}]},"item_10002_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0288-724X","subitem_source_identifier_type":"ISSN"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Fukasawa, Kayoko M"}],"nameIdentifiers":[{"nameIdentifier":"46186","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hata, Toshiyuki"}],"nameIdentifiers":[{"nameIdentifier":"46187","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Ono, Yukio"}],"nameIdentifiers":[{"nameIdentifier":"46188","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hirose, Junzo"}],"nameIdentifiers":[{"nameIdentifier":"46189","nameIdentifierScheme":"WEKO"}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-12-25"}],"displaytype":"detail","filename":"30-22.pdf","filesize":[{"value":"80.7 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"深澤加與子(発表論文抄録(2011))","url":"https://fukuyama-u.repo.nii.ac.jp/record/8824/files/30-22.pdf"},"version_id":"bf431068-6355-4b84-9708-dedb8ff57b0f"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"departmental bulletin paper","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"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))","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"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))"},{"subitem_title":"Metal preferences of zinc-binding motif on metalloproteases.","subitem_title_language":"en"}]},"item_type_id":"10002","owner":"18","path":["779"],"pubdate":{"attribute_name":"公開日","attribute_value":"2017-12-25"},"publish_date":"2017-12-25","publish_status":"0","recid":"8824","relation_version_is_last":true,"title":["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))"],"weko_creator_id":"18","weko_shared_id":-1},"updated":"2023-06-19T10:16:04.396503+00:00"}