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Identification and Characterization of Prokaryotic Dipeptidyl-Peptidase 5 from Porphyromonas gingivalis
http://hdl.handle.net/10069/34200
http://hdl.handle.net/10069/342003e91f253-38b0-4621-8b49-0e7cef1dfb25
名前 / ファイル | ライセンス | アクション |
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JBC289_5436.pdf (3.1 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2014-03-24 | |||||
タイトル | ||||||
タイトル | Identification and Characterization of Prokaryotic Dipeptidyl-Peptidase 5 from Porphyromonas gingivalis | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | DPP4 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | DPP5 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | DPP7 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | DPP11 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Porphyromonas gingivalis | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | substrate specificity | |||||
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 |
Ohara-Nemoto, Yuko
× Ohara-Nemoto, Yuko× Rouf, Shakh M. A.× Naito, Mariko× Yanase, Amie× Tetsuo, Fumi× Ono, Toshio× Kobayakawa, Takeshi× Shimoyama, Yu× Kimura, Shigenobu× Nakayama, Koji× Saiki, Keitarou× Konishi, Kiyoshi× Nemoto, Takayuki K. |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is one of the major causative organisms of chronic periodontitis. The bacterium utilizes amino acids as energy and carbon sources, and incorporates them mainly as dipeptides. Therefore, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. A DPP7-like activity still remained in a dpp4-7-11 disrupted P. gingivalis ATCC 33277. PGN_0756, currently annotated as a prolyl oligopeptidase, possessed an activity indistinguishable from that of the triple dpp gene-disrupted strain, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with an apparent molecular weight of 66 kDa, while it preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated kcat/Km values for Gly-Phe-MCA and Lys-Ala-MCA of 13.01 and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of dpp- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also distributed in prokaryotes. | |||||
書誌情報 |
Journal of Biological Chemistry 巻 289, 号 9, p. 5436-5448, 発行日 2014-02-28 |
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出版者 | ||||||
出版者 | The American Society for Biochemistry and Molecular Biology | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 00219258 | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1083351X | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1074/jbc.M113.527333 | |||||
権利 | ||||||
権利情報 | This research was originally published in Journal of Biological Chemistry. Ohara-Nemoto, Y. et al. Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis. Journal of Biological Chemistry. 2014; Vol: 289(9), pp.5436-5448. c the American Society for Biochemistry and Molecular Biology. | |||||
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 | Journal of Biological Chemistry, 289(9), pp.5436-5448; 2014 |