{"created":"2023-05-15T14:56:50.296460+00:00","id":77138,"links":{},"metadata":{"_buckets":{"deposit":"bbebef89-4744-482e-a532-ccf227c47e1a"},"_deposit":{"created_by":1,"id":"77138","owners":[1],"pid":{"revision_id":0,"type":"depid","value":"77138"},"status":"published"},"_oai":{"id":"oai:repo.qst.go.jp:00077138","sets":["10:28"]},"author_link":["794912","794910","794909","794911","794914","794913","794908"],"item_10005_date_7":{"attribute_name":"発表年月日","attribute_value_mlt":[{"subitem_date_issued_datetime":"2019-10-18","subitem_date_issued_type":"Issued"}]},"item_10005_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The earthworm Eisenia fetida has some cold-adapted carbohydrases including alpha-amylase, cellulase, glucanase and beta-mannanase. We have identified two types of raw-starch digesting alpha-amylases from E. fetida (Ef-Amy I and II), which exhibit activities at low-temperatures. In this study, X-ray structure analyses were performed to understand the molecular mechanisms in biochemical properties of Ef-Amy I. Ef-Amy I shows structural similarities with alpha-amylases from porcine pancreatic and human pancreatic. The surface electrostatic potential indicates that large part of surface area consists of acidic residues in Ef-Amy I. We also determined X-ray crystal structures of the inactive mutant (E249Q) of Ef-Amy I both in apo and substrate complex forms. An electron density map shows a maltohexaose molecule binding at the active site and an electron density blob corresponds to maltotetraose was observed around the cleft between the N and C terminal domains. These structural features display important characteristics for cold-adaptation and substrate recognition in Ef-Amy I.","subitem_description_type":"Abstract"}]},"item_10005_description_6":{"attribute_name":"会議概要（会議名, 開催地, 会期, 主催者等）","attribute_value_mlt":[{"subitem_description":"International symposium on diffraction structural biology 2019","subitem_description_type":"Other"}]},"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":"794908","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Tsukamoto, Kana"}],"nameIdentifiers":[{"nameIdentifier":"794909","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Yuki, Naka"}],"nameIdentifiers":[{"nameIdentifier":"794910","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Ueda, Mitsuhiro"}],"nameIdentifiers":[{"nameIdentifier":"794911","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Tamada, Taro"}],"nameIdentifiers":[{"nameIdentifier":"794912","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Hirano, Yuu","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"794913","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Tamada, Taro","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"794914","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":"conference object","resourceuri":"http://purl.org/coar/resource_type/c_c94f"}]},"item_title":"X-ray crystal structures of alpha-amylase I from Eisenia fetida","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"X-ray crystal structures of alpha-amylase I from Eisenia fetida"}]},"item_type_id":"10005","owner":"1","path":["28"],"pubdate":{"attribute_name":"公開日","attribute_value":"2019-10-09"},"publish_date":"2019-10-09","publish_status":"0","recid":"77138","relation_version_is_last":true,"title":["X-ray crystal structures of alpha-amylase I from Eisenia fetida"],"weko_creator_id":"1","weko_shared_id":-1},"updated":"2023-05-15T23:55:47.538622+00:00"}