{"created":"2023-05-15T14:59:21.988433+00:00","id":80542,"links":{},"metadata":{"_buckets":{"deposit":"807a1cf4-5db6-4714-bd1d-10717d4069b7"},"_deposit":{"created_by":1,"id":"80542","owners":[1],"pid":{"revision_id":0,"type":"depid","value":"80542"},"status":"published"},"_oai":{"id":"oai:repo.qst.go.jp:00080542","sets":["1"]},"author_link":["1011814","1011820","1011817","1011815","1011816","1011819","1011818","1011821"],"item_8_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2020-08","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"844","bibliographicPageStart":"834","bibliographicVolumeNumber":"76","bibliographic_titles":[{"bibliographic_title":"Acta Crystallographica Section D"}]}]},"item_8_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The earthworm Eisenia fetida has some cold-active enzymes including α-amylase, β-glucanase, and β-mannanase. E. fetida possesses two isoforms of α-amylase (Ef-Amy I and II), to digest raw starch. Ef-Amy I retains its catalytic activity at temperatures below 10˚C. To identify the molecular properties of Ef-Amy I, X-ray crystal structures were determined using wild type and the inactive E249Q mutant. Ef-Amy I has structural similarities to mammalian α-amylases, including porcine pancreatic and human pancreatic α-amylases. Structural comparisons between both the overall structures as well as the Ca2+ binding sites in Ef-Amy I and the mammalian α-amylases indicate that the Ef-Amy I has increased structural flexibility and more solvent-exposed acidic residues. These structural features in Ef-Amy I can contribute to the observed catalytic activities at low temperatures because many cold-adapted enzymes have similar structural properties. The structure of the substrate complex in the inactive mutant of Ef-Amy I shows that a maltohexaose molecule is bound at the active site and a maltotetraose is bound at the cleft between the N- and C-terminal domains. The recognition of substrate molecules in Ef-Amy I exhibits some differences from those observed in the structures of human pancreatic α-amylase. This result provides insights into the structural modulation of the recognition of substrates and inhibitors.","subitem_description_type":"Abstract"}]},"item_8_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1107/S2059798320010165","subitem_relation_type_select":"DOI"}}]},"item_8_relation_17":{"attribute_name":"関連サイト","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"http://scripts.iucr.org/cgi-bin/paper?yl5001","subitem_relation_type_select":"URI"}}]},"item_8_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"2059-7983","subitem_source_identifier_type":"ISSN"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"metadata only access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_14cb"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Hirano, Yuu"}],"nameIdentifiers":[{"nameIdentifier":"1011814","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Tsukamoto, Kana"}],"nameIdentifiers":[{"nameIdentifier":"1011815","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Ariki, Shingo"}],"nameIdentifiers":[{"nameIdentifier":"1011816","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Naka, Yuki"}],"nameIdentifiers":[{"nameIdentifier":"1011817","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Ueda, Mitsuhiro"}],"nameIdentifiers":[{"nameIdentifier":"1011818","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Tamada, Taro"}],"nameIdentifiers":[{"nameIdentifier":"1011819","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Yuu, Hirano","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"1011820","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Taro, Tamada","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"1011821","nameIdentifierScheme":"WEKO"}]}]},"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":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"X-ray crystallographic structural studies of α-amylase I from Eisenia fetida ","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"X-ray crystallographic structural studies of α-amylase I from Eisenia fetida "}]},"item_type_id":"8","owner":"1","path":["1"],"pubdate":{"attribute_name":"公開日","attribute_value":"2020-07-27"},"publish_date":"2020-07-27","publish_status":"0","recid":"80542","relation_version_is_last":true,"title":["X-ray crystallographic structural studies of α-amylase I from Eisenia fetida "],"weko_creator_id":"1","weko_shared_id":-1},"updated":"2023-05-15T18:58:19.525630+00:00"}