Structural studies for the refined reaction mechanism of copper amine oxidase.
| Project/Area Number |
23770127
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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 | Osaka Medical College |
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Principal Investigator |
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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 |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | トパキノン / 高分解能X線結晶解析 / 中性子線結晶構造解析 / 超高分解能X腺結晶構造解析 / TPQ / アミン酸化酵素 / 高分解能 / 中性子線 / X線 |
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| Research Abstract |
Copper amine oxidases (CAOs) catalyse the oxidation of various aliphatic amines to the corresponding aldehydes, ammonia and hydrogen peroxide. I focused on the structural insights into the catalytic mechanism of a CAO from Arthrobacter globiformis (AGAO) using an ultra-high resolution X-ray crystallography and neutron crystallography method. For the ultra-high resolution X-ray crystallography, the crystal structure of AGAO was determined at 1.08 A resolution in the substrate-free form. Based on the structure, the oxygen pathway to the active site was estimated. On the other hand, on the basis of the structure of the AGAO complexed with irreversible inhibitors, structural insights of the substrate specificity were obtained. Furthermore, a large crystal of AGAO for a neutron crystallography was prepared.
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Report
(4 results)
Research Products
(14 results)
