{"created":"2023-07-27T06:56:50.804144+00:00","id":53801,"links":{},"metadata":{"_buckets":{"deposit":"9a78dbe3-2006-477b-b480-3254f05523e3"},"_deposit":{"created_by":18,"id":"53801","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"53801"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00053801","sets":["934:935:937"]},"author_link":["15540","15084"],"item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1986","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"3","bibliographicPageEnd":"824","bibliographicPageStart":"815","bibliographicVolumeNumber":"99","bibliographic_titles":[{"bibliographic_title":"The Journal of Biochemistry"}]}]},"item_4_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"板垣, 英治"}],"nameIdentifiers":[{"nameIdentifier":"15084","nameIdentifierScheme":"WEKO"}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"A steroid monooxygenase from cells of a fungus, Cylindrocarpon radicicola ATCC 11011, grown in the presence of progesterone has been purified by affinity chromatography on a pregnenolone-Sepharose column. The obtained enzyme was gel electrophoretically homogeneous and exhibited a molecular weight of about 115, 000. SDS-gel electrophoresis revealed that the enzyme consisted of two equal-sized subunits with a molecular weight of 56, 000.\nSedimentation equilibrium analysis at 20°C indicated that the enzyme protein behaved as a mixture of monomeric and dimeric subunit species. The enzyme contained one molecule of FAD in each subunit and exhibited absorption maxima at 375 and 440 nm.\nThe monooxygenase catalyzed a Baeyer-Villiger type oxidation, i.e., oxygenative esterification of C21-20-ketosteroid to form an acetate ester of C19- 17β-hydroxysteroid with consumptions of NADPH and molecular oxygen. The enzyme displayed a wide substrate specificity toward C21-20-ketosteroids, while it strictly required NADPH as the external electron donor in a ratio of 1:1:1 for ketosteroid: NADPH: molecular oxygen. Kinetic study showed the enzyme to have very high affinity for progesterone.","subitem_description_type":"Abstract"}]},"item_4_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00060082","subitem_identifier_reg_type":"JaLC"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"The Japanese Biochemical Society"}]},"item_4_publisher_19":{"attribute_name":"出版者（別名）","attribute_value_mlt":[{"subitem_publisher":"日本生化学会"}]},"item_4_relation_28":{"attribute_name":"関連URI","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"http://www.jbsoc.or.jp/"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"http://www.jbsoc.or.jp/","subitem_relation_type_select":"URI"}},{"subitem_relation_name":[{"subitem_relation_name_text":"https://academic.oup.com/jb"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://academic.oup.com/jb","subitem_relation_type_select":"URI"}},{"subitem_relation_name":[{"subitem_relation_name_text":"https://www.jstage.jst.go.jp/browse/biochemistry1922/-char/ja"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://www.jstage.jst.go.jp/browse/biochemistry1922/-char/ja","subitem_relation_type_select":"URI"}}]},"item_4_rights_23":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"Copyright © The Japanese Biochemical Society 日本生化学会"}]},"item_4_source_id_11":{"attribute_name":"NCID","attribute_value_mlt":[{"subitem_source_identifier":"AA00694073","subitem_source_identifier_type":"NCID"}]},"item_4_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0021-924X","subitem_source_identifier_type":"ISSN"}]},"item_4_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Itagaki, Eiji"}],"nameIdentifiers":[{"nameIdentifier":"15540","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":"2020-12-03"}],"displaytype":"detail","filename":"SC-PR-ITAGAKI-E-99_815.pdf","filesize":[{"value":"817.9 kB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"SC-PR-ITAGAKI-E-99_815.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/53801/files/SC-PR-ITAGAKI-E-99_815.pdf"},"version_id":"11bef4a5-aeed-457a-8053-872d3a9ef817"}]},"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":"Studies on Steroid Monooxygenase from Cylindrocarpon radicicola ATCC 11011.1 Purification and Characterization","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Studies on Steroid Monooxygenase from Cylindrocarpon radicicola ATCC 11011.1 Purification and Characterization"}]},"item_type_id":"4","owner":"18","path":["937"],"pubdate":{"attribute_name":"公開日","attribute_value":"2020-12-03"},"publish_date":"2020-12-03","publish_status":"0","recid":"53801","relation_version_is_last":true,"title":["Studies on Steroid Monooxygenase from Cylindrocarpon radicicola ATCC 11011.1 Purification and Characterization"],"weko_creator_id":"18","weko_shared_id":-1},"updated":"2024-06-20T06:09:11.169394+00:00"}