2015 Fiscal Year Final Research Report
Study of a novel enzymatic group of dipeptidyl peptidases and their cellular localization
Project/Area Number |
25462894
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Functional basic dentistry
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Research Institution | Nagasaki University |
Principal Investigator |
OHARA-NEMOTO Yuko 長崎大学, 医歯薬学総合研究科(歯学系), 准教授 (10164667)
|
Co-Investigator(Kenkyū-buntansha) |
NEMOTO Takayuki K. 長崎大学, 医歯薬学総合研究科(歯学系), 教授 (90164665)
KIMURA Shigenobu 岩手医科大学, 歯学部, 教授 (10177917)
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Keywords | Porphyromonas gingivalis / ジペプチジルペプチダーゼ / アミノ酸代謝 / ペリプラズム / 歯周病 |
Outline of Final Research Achievements |
We examined enzymatic activity and cellular localization of a group of dipeptidyl peptidases (DPP) in a periodontopathic bacterium, Porphyromonas gingivalis. This study revealed that DPP5, which had been discovered in fungi, was expressed in the bacterium, and that a novel peptidase, acylpeptidyl oligopeptidase (AOP), was identified. Ortholog search demonstrated wide spreading of the two exopeptidases from bacteria, archea to eukaryote. DPP5 cleaves X-Ala dipeptides from the N-terminus of oligopeptides and AOP liberates di- and tri-peptides from N-terminally blocked ones. Both peptidases were expressed in the periplasmic space of the bacterium. Consequently, we proposed that dipeptide-producing exopeptidases including DPP4, DPP5, DPP7, DPP11 and AOP are crucial for the growth and pathogenicity of P. gingivalis.
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Free Research Field |
口腔生化学
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