Structure and function of enzymes involved with the synthesis or the degradation of D-aspartate.
| Project/Area Number |
22770113
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | Toho University |
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Principal Investigator |
GOTO Masaru 東邦大学, 理学部, 講師 (80379289)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 酵素 / 酵素反応 / 立体構造 |
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| Research Abstract |
In the mammalian neuroendocrine system, D-aspartate plays important roles in the regulation of the synthesis and secretion of hormones. PLP-dependent aspartate racemase and FAD-dependent D-aspartate oxidase are the enzymes known to be responsible for the synthesis or the degradation of D-aspartate, respectively. To understand the substrate specificity of these two enzymes we have determined the structures of the following two wild-type enzymes : aspartate racemase from Scapharca broughtonii and D-aspartate oxidase from Yeast Cryptococcus humicola at 2.15 and 2.00Åresolution, respectively.
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Report
(3 results)
Research Products
(6 results)
