Elucidation of physiological role of Laeverin, a novel aminopeptidase.
Project/Area Number |
20790088
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Biological pharmacy
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Research Institution | Kansai Medical University |
Principal Investigator |
MARUYAMA Masato Kansai Medical University, 医学部, 助教 (00399445)
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Project Period (FY) |
2008 – 2009
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Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2008: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | Laeverin / 絨毛外栄養膜細胞 / エキソペプチダーゼモチーフ / M1アミノペプチダーゼ / 胎盤形成 |
Research Abstract |
Here, we evaluated the roles of His^<379>, comprising the exopeptidase motif, in the enzymatic properties of human Laeverin. Our results indicate that His^<379> plays essential roles in its distinctive enzymatic properties and contributes to maintaining the appropriate structure of the catalytic cavity of the enzyme.
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Report
(3 results)
Research Products
(8 results)
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[Presentation] Histidine-379 of human laeverin/aminopeptidase Q, a non-conserved residue within the exopeptidase motif, defines its distinctive enzymatic properties2009
Author(s)
Hattori A, Maruyama M, Arisaka N, Goto Y, Osawa Y, Inoue H, Fujiwara H, Tsujimoto M
Organizer
6th General Meeting of the International Proteolysis Society
Place of Presentation
Surfers Paradise, Australia
Related Report
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