Development of anti-Trypanosoma drug based on structural and functional analysis of novel L-amino acid dehydrogenase
| Project/Area Number |
24780105
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Tokai University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 酵素化学 / L-スレオニン酸脱水素酵素 / NAD / トリパノソーマ / クローニング / 結晶化 / 脱水素酵素 / L-スレオニン |
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| Research Abstract |
L-Threonine dehydrogenase (ThrDH) gene from the pathogenic parasite Trypanosoma brucei was amplified using the overlapping primers, and ligated with the expression vector pCold TF. Escherichia coli was then transformed with the vector and induced by adding 1.0 mM IPTG to the medium. The gene was overexpressed in E. coli, and its product was purified and characterized. SDS-PAGE showed the subunit molecular mass of T. brucei ThrDH to be about 81 kDa, which was consistent with the molecular weight calculated from the amino acid sequence. The slightly NAD-dependent ThrDH activity was determined.
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Report
(3 results)
Research Products
(24 results)
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[Journal Article] Crystallization and preliminary X-ray analysis of L-serine 3-dehydrogenase complexed with NADP+ from the hyperthermophilic archaeon Pyrobaculum calidifontis,2013
Author(s)
Yoneda, K., Sakuraba, H., Araki, T., Shibata, T., Nikki, T. & Ohshima, T.
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Journal Title
Acta Cryst.
Volume: F69
Issue: 2
Pages: 134-136
DOI
Related Report
Peer Reviewed
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