X-ray structure analysis of rare sugar producible enzymes aiming for elucidation of novel isomerization mechanism
| Project/Area Number |
23770122
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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 |
Structural biochemistry
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| Research Institution | Kagawa University |
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Principal Investigator |
YOSHIDA Hiromi 香川大学, 総合生命科学研究センター, 准教授 (10313305)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | X 線結晶解析 / 単糖異性化酵素 / L-ラムノースイソメラーゼ / D-タガトースエピメラーゼ / D-アラビノースイソメラーゼ / L-リボースイソメラーゼ / 希少糖 / 放射光 / 部位特異的変異 / X線結晶解析 / 糖異性化酵素 |
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| Research Abstract |
X-ray structure of a novel isomerase, L-ribose isomerase from Acinetobacter sp. (L-RI) was determined. L-RI can catalyze reversible isomerization between L-ribose and L-ribulose, and is a plausible enzyme for rare sugar production. In the structure analysis, L-RI showed the dimer formation. The monomer structure of L-RI is similar to that of D-lyxose isomerase from Escherichia coli O157:H7. L-RI retains a metal ion in the active site with three histidines. Two glutamates are putative catalytic residues.
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Report
(3 results)
Research Products
(18 results)
