Structural analyses of the high molecular mass peptidases belonging to M1 and S9 families
| Project/Area Number |
23590081
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Kyushu University of Health and Welfare (2012-2013)
Nagasaki University (2011) |
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Principal Investigator |
ITO Kiyoshi 九州保健福祉大学, 薬学部, 教授 (50201926)
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| Research Collaborator |
YOSHIMOTO Tadashi 摂南大学, 理工生命, 教授 (60088870)
NAKAJIMA Yoshitaka 摂南大学, 理工生命, 准教授 (80372770)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | ペプチダーゼ / オリゴペプチダーゼB / アミノペプチダーゼ / S9ファミリー / M1ファミリー / 基質特異性 / 基質阻害 / X線結晶構造解析 / アミノペプチダーゼN / ピューロマイシン感受性 |
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| Research Abstract |
High molecular mass is a characteristic feature of the M1 and S9 family enzymes. Enzymes belonging to M1 family contain many aminopeptidases abundant in brain and those to S9 family contain oligopeptidase B, which is involved in the infection process of trypanosomiasis. These enzymes posess unique structures covering the catalytic center of cleavage activity. In this study, two peptidases, a puromycin-sensitive aminopeptidase from human and oligopeptidase B from some bacteria were used to investigate important amino acid residues for activity. In addition, crystallization conditions for some enzymes were found. It is important to understand phisiological functions of brain aminopeptidases and to develop a new way of chemotherapy against some infectious diseases.
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Report
(4 results)
Research Products
(30 results)
