{"created":"2023-06-19T09:51:37.451993+00:00","id":8845,"links":{},"metadata":{"_buckets":{"deposit":"6ff1921d-856e-48de-a0b5-18ae673e4334"},"_deposit":{"created_by":18,"id":"8845","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"8845"},"status":"published"},"_oai":{"id":"oai:fukuyama-u.repo.nii.ac.jp:00008845","sets":["502:503:627:764"]},"author_link":["45238","46313","45879","46312","46311","45236","46310","46309"],"item_10002_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2011-12-25","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"29","bibliographicPageEnd":"56","bibliographicPageStart":"55","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":"Dipeptidyl peptidase (DPP) III is a zinc-dependent exopeptidase that has a unique motif, \"HELLGH,\" as the zinc-binding site. In the present study, a three-dimensional (3D) model of rat DPP III was generated with the X-ray crystal structure of human DPP III (PDB: 3FVY [Dobrovetsky E. et al. (2009) SGC]) as a template. The replacement of the seven charged amino acid residues with a hydrophobic amino acid around the zinc ion did not cause any significant changes in K(m) values or in the substrate specificity. However, the k(cat) values of H568R and H568Y were remarkably reduced, by factors of 50 and 400, respectively. The His⁵⁶⁸ residue of rat DPP III is essential for enzyme catalysis. The k(cat) values of the mutants E507A and E512A were 2.38 and 3.88 s⁻¹ toward Arg-Arg-NA, and 0.097 and 0.59 s⁻¹ toward Phe-Arg-NA, respectively. These values were markedly lower than those of the wild-type DPP III. Furthermore, the zinc contents of E507A and E512A were 0.29 and 0.08 atom per mol of protein, respectively, and those mutations caused remarkable increases in the dissociation constants of the zinc ions from DPP III by factors of 5 x 10³ to 2 x 10⁴. The 3D model of the catalytic domain of rat DPP III showed that the carboxyl oxygen atoms of Glu⁵⁰⁷ and Glu⁵¹² form the hydrogen bonds to the nitrogen atoms of His⁴⁵⁵ and His⁴⁵⁰. All of these results showed that Glu⁵⁰⁷ or Glu⁵¹² stabilizes the coordination bond between the zinc ion and His⁴⁵⁵ or His⁴⁵⁰.","subitem_description_type":"Abstract"}]},"item_10002_description_6":{"attribute_name":"内容記述","attribute_value_mlt":[{"subitem_description":"Dipeptidyl peptidase (DPP) III is a zinc-dependent exopeptidase that has a unique motif, \"HELLGH,\" as the zinc-binding site. In the present study, a three-dimensional (3D) model of rat DPP III was generated with the X-ray crystal structure of human DPP III (PDB: 3FVY [Dobrovetsky E. et al. (2009) SGC]) as a template. The replacement of the seven charged amino acid residues with a hydrophobic amino acid around the zinc ion did not cause any significant changes in K(m) values or in the substrate specificity. However, the k(cat) values of H568R and H568Y were remarkably reduced, by factors of 50 and 400, respectively. The His⁵⁶⁸ residue of rat DPP III is essential for enzyme catalysis. The k(cat) values of the mutants E507A and E512A were 2.38 and 3.88 s⁻¹ toward Arg-Arg-NA, and 0.097 and 0.59 s⁻¹ toward Phe-Arg-NA, respectively. These values were markedly lower than those of the wild-type DPP III. Furthermore, the zinc contents of E507A and E512A were 0.29 and 0.08 atom per mol of protein, respectively, and those mutations caused remarkable increases in the dissociation constants of the zinc ions from DPP III by factors of 5 x 10³ to 2 x 10⁴. The 3D model of the catalytic domain of rat DPP III showed that the carboxyl oxygen atoms of Glu⁵⁰⁷ and Glu⁵¹² form the hydrogen bonds to the nitrogen atoms of His⁴⁵⁵ and His⁴⁵⁰. All of these results showed that Glu⁵⁰⁷ or Glu⁵¹² stabilizes the coordination bond between the zinc ion and His⁴⁵⁵ or His⁴⁵⁰.","subitem_description_type":"Other"}]},"item_10002_full_name_3":{"attribute_name":"著者別名","attribute_value_mlt":[{"nameIdentifiers":[{"nameIdentifier":"46313","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"9000014626005","nameIdentifierScheme":"CiNii ID","nameIdentifierURI":"http://ci.nii.ac.jp/nrid/9000014626005"}],"names":[{"name":"深澤, 加與子"}]},{"nameIdentifiers":[{"nameIdentifier":"45879","nameIdentifierScheme":"WEKO"},{"nameIdentifier":"1000070080215","nameIdentifierScheme":"CiNii ID","nameIdentifierURI":"http://ci.nii.ac.jp/nrid/1000070080215"}],"names":[{"name":"廣瀬, 順造"}]},{"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"}]}]},"item_10002_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"福山大学薬学部"}]},"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":"46309","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hirose, Junzo"}],"nameIdentifiers":[{"nameIdentifier":"46310","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hata, Toshiyuki"}],"nameIdentifiers":[{"nameIdentifier":"46311","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Ono, Yukio"}],"nameIdentifiers":[{"nameIdentifier":"46312","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":"2018-01-15"}],"displaytype":"detail","filename":"ラットジペプチジルペプチダーゼⅢにおいて、His568 は活性発現に必須であり、Glu507及びGlu512は亜鉛イオンと配位残基であるHis455 及びHis450 との配位結合を安定化する。.pdf","filesize":[{"value":"648.2 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"深澤加與子(発表論文抄録(2010))","url":"https://fukuyama-u.repo.nii.ac.jp/record/8845/files/ラットジペプチジルペプチダーゼⅢにおいて、His568 は活性発現に必須であり、Glu507及びGlu512は亜鉛イオンと配位残基であるHis455 及びHis450 との配位結合を安定化する。.pdf"},"version_id":"ef289df5-9656-458d-b6ab-4be9c2cbf1f5"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"Animals","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Catalysis","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Crystallography, X-Ray","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Dipeptides","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Dipeptidyl-Peptidases and Tripeptidyl-Peptidases","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Glutamic Acid","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Histidine","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Humans","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Models, Molecular","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Mutagenesis, Site-Directed","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Mutation","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Protein Conformation","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Rats","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Substrate Specificity","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Zinc","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"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":"ラットジペプチジルペプチダーゼIIIにおいて、His568 は活性発現に必須であり、Glu507及びGlu512は亜鉛イオンと配位残基であるHis455 及びHis450 との配位結合を安定化する。(発表論文抄録(2010))","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"ラットジペプチジルペプチダーゼIIIにおいて、His568 は活性発現に必須であり、Glu507及びGlu512は亜鉛イオンと配位残基であるHis455 及びHis450 との配位結合を安定化する。(発表論文抄録(2010))"},{"subitem_title":"In rat dipeptidyl peptidase III, His⁵⁶⁸ is essential for catalysis, and Glu⁵⁰⁷ or Glu⁵¹² stabilizes the coordination bond between His⁴⁵⁵ or His⁴⁵⁰ and zinc ion.","subitem_title_language":"en"}]},"item_type_id":"10002","owner":"18","path":["764"],"pubdate":{"attribute_name":"公開日","attribute_value":"2018-01-15"},"publish_date":"2018-01-15","publish_status":"0","recid":"8845","relation_version_is_last":true,"title":["ラットジペプチジルペプチダーゼIIIにおいて、His568 は活性発現に必須であり、Glu507及びGlu512は亜鉛イオンと配位残基であるHis455 及びHis450 との配位結合を安定化する。(発表論文抄録(2010))"],"weko_creator_id":"18","weko_shared_id":-1},"updated":"2023-06-19T10:15:31.868841+00:00"}