{"created":"2023-07-27T06:26:34.088414+00:00","id":10337,"links":{},"metadata":{"_buckets":{"deposit":"437fc5e4-4038-4658-bf9e-f3fa21eb6a3d"},"_deposit":{"created_by":3,"id":"10337","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"10337"},"status":"draft"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00010337","sets":["934:935:937"]},"author_link":["15566","15567","15568","15084"],"control_number":"10337","item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1991-01-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"4","bibliographicPageEnd":"586","bibliographicPageStart":"581","bibliographicVolumeNumber":"109","bibliographic_titles":[{"bibliographic_title":"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":[{}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The inducible 3-keto-5α-steroid-Δ4-dehydrogenase of Nocardia corallina was purified to homogeneity using affinity chromatography on 19-nortestosterone-17-acetoxyaminoethyl Sepharose 4B. SDS-polyacrylamide gel electrophoresis, gel filtration and spectral analysis of flavin suggest that the purified dehydrogenase is a monomeric protein of M(r) 60,000 containing one flavin. It has a typical absorption spectrum of flavoprotein with maxima at 457, 375, and 277 nm. The values shifted to 470 and 395 nm on binding of 19-nortestosterone. The enzyme catalyzed the dehydrogenation of 3-keto-5α-steroid at the 4- and 5-position, e.g. the conversion of 5α-androst-1-ene-3,17-dione to 1,4-androstadiene-3,17-dione with the reduction of phenazine methosulfate. The substrate 3-ketosteroid has essentially the 5α-configuration. The enzyme did not reduce potassium ferricyanide but did reduce cytochrome c at a moderate rate, and exhibited only a weak steroid oxidase activity. Stereochemical study demonstrated that the enzyme abstracts the 4β, 5α-hydrogens of the substrate as a hydrogen ion through a protein-based reaction and as a hydride ion by transfer to FAD, respectively. The enzyme oxidizes a wide variety of 3-keto-5α-steroids but not 3β-hydroxysteroid. The dehydrogenase also catalyzed steroid transhydrogenation between 3-keto-5α-steroid and 3-keto-1,4-diene-steroid. The properties of this enzyme are compared with those of 3-keto-steroid-Δ1-dehydrogenase.","subitem_description_type":"Abstract"}]},"item_4_description_5":{"attribute_name":"提供者所属","attribute_value_mlt":[{"subitem_description":"金沢大学自然科学研究科　　","subitem_description_type":"Other"},{"subitem_description":"金沢大学理工研究域自然システム学系","subitem_description_type":"Other"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"日本生化学会 = Japanese Biochemical Society"}]},"item_4_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"https://doi.org/10.1093/oxfordjournals.jbchem.a123423","subitem_relation_type_select":"DOI"}}]},"item_4_rights_23":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"Copyright © 1991 Japanese Biochemical Society"}]},"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":"Hatta, Takashi"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Wakabayashi, Teruko"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Itagaki, Eiji"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-10-03"}],"displaytype":"detail","filename":"SC-PR-ITAGAKI-E-581.pdf","filesize":[{"value":"746.1 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"SC-PR-ITAGAKI-E-581.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/10337/files/SC-PR-ITAGAKI-E-581.pdf"},"version_id":"bf309847-03f9-470e-b9a7-a91cd94828bc"}]},"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":"3-keto-5α-steroid-Δ4-dehydrogenase from Nocardia corallina: Purification and characterization","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"3-keto-5α-steroid-Δ4-dehydrogenase from Nocardia corallina: Purification and characterization"}]},"item_type_id":"4","owner":"3","path":["937"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2017-10-03"},"publish_date":"2017-10-03","publish_status":"0","recid":"10337","relation_version_is_last":true,"title":["3-keto-5α-steroid-Δ4-dehydrogenase from Nocardia corallina: Purification and characterization"],"weko_creator_id":"3","weko_shared_id":3},"updated":"2023-12-19T02:36:35.795654+00:00"}