| Project/Area Number |
09660074
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
|
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| Research Institution | The University of Tokyo |
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Principal Investigator |
WAKAGI Takayoshi Graduate School of Agricultural and Life Sciences, The University of Tokyo, Associate Professor, 大学院・農学生命科学研究科, 助教授 (70175058)
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| Project Period (FY) |
1997 – 1999
|
| Project Status |
Completed (Fiscal Year 1999)
|
| Budget Amount *help |
¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 1999: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1998: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1997: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | archaea / thermophile / oxidoreductase / ferredoxin / 2-オキソ酸 / 耐熱性酵素 / 遺伝子発現 |
|---|
| Research Abstract |
2-Oxoacid : ferredoxin oxidoreductase (OFOR) catalyzes oxidative decarboxylation of 2-oxoacids, using ferredoxin as an electron acceptor. The OFOR is found among all archaea, certain eubacteria, and certain eukaryotes. The structure-function relationship of OFOR is not clearly elucidated. This is partly because of the difficulty in constructing gene expression system that produces stable enzyme, or of the intrinsic oxygen-sensitivity of most OFORS from anaerobic organisms. In the present study, we first constructed the OFOR gene expression system from Sulfolobus sp. strain 7, compared the characteristics of recombinant enzyme with natural one. The two OFORs were indistinguishable by the criteria so far investigated. Based on the gene expression system, a series of mutants that is implicated as catalytic sites were designed. Some of them lost activity, and the other were found to change its substrate specificity.
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