WEKO3
アイテム
{"_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": ["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": [{"nameIdentifier": "112127", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Ono, Toshio"}], "nameIdentifiers": [{"nameIdentifier": "112128", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Kobayakawa, Takeshi"}], "nameIdentifiers": [{"nameIdentifier": "112129", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Ohara-Nemoto, Yuko"}], "nameIdentifiers": [{"nameIdentifier": "112130", "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": "2020-12-25"}], "displaytype": "detail", "download_preview_message": "", "file_order": 0, "filename": "Biochimie163_50.pdf", "filesize": [{"value": "2.0 MB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_free", "mimetype": "application/pdf", "size": 2000000.0, "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"], "permalink_uri": "http://hdl.handle.net/10069/39181", "pubdate": {"attribute_name": "公開日", "attribute_value": "2020-09-01"}, "publish_date": "2020-09-01", "publish_status": "0", "recid": "1893", "relation": {}, "relation_version_is_last": true, "title": ["Characterization of bacterial acylpeptidyl-oligopeptidase"], "weko_shared_id": -1}
Characterization of bacterial acylpeptidyl-oligopeptidase
http://hdl.handle.net/10069/39181
http://hdl.handle.net/10069/39181003d5acc-9fb4-46da-ab65-105453073db9
名前 / ファイル | ライセンス | アクション |
---|---|---|
Biochimie163_50.pdf (2.0 MB)
|
|
Item type | 学術雑誌論文 / Journal Article(1) | |||||
---|---|---|---|---|---|---|
公開日 | 2020-09-01 | |||||
タイトル | ||||||
タイトル | Characterization of bacterial acylpeptidyl-oligopeptidase | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Acylaminoacyl-peptidase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | acylpeptidyl-oligopeptidase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Bacteroides dorei | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Lysinibacillus sphaericus | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Porphyromonas gingivalis | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Nemoto, Takayuki K.
× Nemoto, Takayuki K.× Ono, Toshio× Kobayakawa, Takeshi× Ohara-Nemoto, Yuko |
|||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Acylpeptidyl-oligopeptidase (AOP), which has been recently identified as a novel enzyme in a periodontopathic bacterium, Porphyromonas gingivalis, removes di- and tri-peptides from N-terminally acylated polypeptides, with a preference for hydrophobic P1-position amino acid residues. To validate enzymatic properties of AOP, characteristics of two bacterial orthologues from Bacteroides dorei (BdAOP), a Gramnegative intestinal rod, and Lysinibacillus sphaericus (LsAOP), a Gram-positive soil rod, were determined. Like P. gingivalis AOP (PgAOP), two orthologues more efficiently hydrolyzed N-terminal acylated peptidyl substrates than non-acylated ones. Optimal pH was shifted from 7.0 ? 8.9 for N-acylated to 8.5 ? 9.5 for non-acylated substrates, indicating preference for non-charged hydrophobic N-terminal residues. Hydrophobic P1- and P2-position preferences were common in the three AOPs, although PgAOP preferred Leu and the others preferred Phe at the P1 position. In vitro mutagenesis demonstrated that Phe647 in PgAOP was responsible for the P1 Leu preference. In addition, bacterial AOPs commonly liberated acetyl-Ser1-Tyr2 from amelanocyte- stimulating hormone. Taken together, although these three bacterial AOPs exhibited some variations in biochemical properties, the present study demonstrated the existence of a group of exopeptidases that preferentially liberates mainly dipeptides from N-terminally acylated polypeptides with a preference for hydrophobic P1 and P2- position residues. |
|||||
書誌情報 |
Biochimie 巻 163, p. 50-57, 発行日 2019-08 |
|||||
出版者 | ||||||
出版者 | Elsevier B.V. | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 03009084 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1016/j.biochi.2019.05.007 | |||||
権利 | ||||||
権利情報 | 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/ | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Biochimie, 163, pp.50-27; 2019 |