{"created":"2023-05-15T16:30:40.619441+00:00","id":1893,"links":{},"metadata":{"_buckets":{"deposit":"7db2b670-b91b-44c5-8df6-82b132a224bf"},"_deposit":{"created_by":2,"id":"1893","owners":[2],"pid":{"revision_id":0,"type":"depid","value":"1893"},"status":"published"},"_oai":{"id":"oai:nagasaki-u.repo.nii.ac.jp:00001893","sets":["27:28"]},"author_link":["112129","112130","112127","112128"],"item_2_biblio_info_6":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2019-08","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"57","bibliographicPageStart":"50","bibliographicVolumeNumber":"163","bibliographic_titles":[{"bibliographic_title":"Biochimie"}]}]},"item_2_description_4":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Acylpeptidyl-oligopeptidase (AOP), which has been recently identified as a novel \nenzyme in a periodontopathic bacterium, Porphyromonas gingivalis, removes di- and \ntri-peptides from N-terminally acylated polypeptides, with a preference for \nhydrophobic P1-position amino acid residues. To validate enzymatic properties of AOP, \ncharacteristics of two bacterial orthologues from Bacteroides dorei (BdAOP), a Gramnegative \nintestinal rod, and Lysinibacillus sphaericus (LsAOP), a Gram-positive soil \nrod, were determined. Like P. gingivalis AOP (PgAOP), two orthologues more \nefficiently hydrolyzed N-terminal acylated peptidyl substrates than non-acylated ones. \nOptimal pH was shifted from 7.0 ? 8.9 for N-acylated to 8.5 ? 9.5 for non-acylated \nsubstrates, indicating preference for non-charged hydrophobic N-terminal residues. \nHydrophobic P1- and P2-position preferences were common in the three AOPs, \nalthough PgAOP preferred Leu and the others preferred Phe at the P1 position. In vitro \nmutagenesis demonstrated that Phe647 in PgAOP was responsible for the P1 Leu \npreference. In addition, bacterial AOPs commonly liberated acetyl-Ser1-Tyr2 from amelanocyte-\nstimulating hormone. Taken together, although these three bacterial AOPs \nexhibited some variations in biochemical properties, the present study demonstrated the \nexistence of a group of exopeptidases that preferentially liberates mainly dipeptides \nfrom N-terminally acylated polypeptides with a preference for hydrophobic P1 and P2-\nposition residues.","subitem_description_type":"Abstract"}]},"item_2_description_63":{"attribute_name":"引用","attribute_value_mlt":[{"subitem_description":"Biochimie, 163, pp.50-27; 2019","subitem_description_type":"Other"}]},"item_2_publisher_33":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Elsevier B.V."}]},"item_2_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1016/j.biochi.2019.05.007","subitem_relation_type_select":"DOI"}}]},"item_2_rights_13":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"c2019, Elsevier. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/"}]},"item_2_source_id_7":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"03009084","subitem_source_identifier_type":"ISSN"}]},"item_2_version_type_16":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Nemoto, Takayuki K."}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Ono, Toshio"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Kobayakawa, Takeshi"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Ohara-Nemoto, Yuko"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2020-12-25"}],"displaytype":"detail","filename":"Biochimie163_50.pdf","filesize":[{"value":"2.0 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"Biochimie163_50.pdf","url":"https://nagasaki-u.repo.nii.ac.jp/record/1893/files/Biochimie163_50.pdf"},"version_id":"869b55c5-cb0d-4507-9d53-17a884e2ef2b"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"Acylaminoacyl-peptidase","subitem_subject_scheme":"Other"},{"subitem_subject":"acylpeptidyl-oligopeptidase","subitem_subject_scheme":"Other"},{"subitem_subject":"Bacteroides dorei","subitem_subject_scheme":"Other"},{"subitem_subject":"Lysinibacillus sphaericus","subitem_subject_scheme":"Other"},{"subitem_subject":"Porphyromonas gingivalis","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":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Characterization of bacterial acylpeptidyl-oligopeptidase","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Characterization of bacterial acylpeptidyl-oligopeptidase"}]},"item_type_id":"2","owner":"2","path":["28"],"pubdate":{"attribute_name":"公開日","attribute_value":"2020-09-01"},"publish_date":"2020-09-01","publish_status":"0","recid":"1893","relation_version_is_last":true,"title":["Characterization of bacterial acylpeptidyl-oligopeptidase"],"weko_creator_id":"2","weko_shared_id":-1},"updated":"2023-05-15T23:01:50.935178+00:00"}