Project/Area Number |
19380059
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied biochemistry
|
Research Institution | Nagoya University |
Principal Investigator |
YOSHIMURA Tohru Nagoya University, 大学院・生命農学研究科, 教授 (70182821)
|
Co-Investigator(Kenkyū-buntansha) |
HEMMI Hisashi 名古屋大学, 大学院・生命農学研究科, 准教授 (60302189)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥19,760,000 (Direct Cost: ¥15,200,000、Indirect Cost: ¥4,560,000)
Fiscal Year 2009: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2008: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2007: ¥10,010,000 (Direct Cost: ¥7,700,000、Indirect Cost: ¥2,310,000)
|
Keywords | D-アミノ酸 / D-セリンデヒドラターゼ / D-セリン定量 / ピリドキサルリン酸 / スクレイピー / 細胞性粘菌 / Saccharomyces cerevisiae / Escherichia coli / D-セリン / セリンラセマーゼ / カイコ / 出芽酵母 |
Research Abstract |
In this study, we found a novel D-serine dehydratase in Saccharomyces cerevisiae, and studied its properties. With this enzyme exhibiting high substrate specificity for D-serine, we constructed a novel D-serine assay system. We examined the relationship between the concentration of D-amino acids in the various organs of a scrapy-infected hamster and the progress in the disease. We also studied the D-serine metabolism in a slime cellular mold, Dictyostellium discoidium, to understand the role of D-serine in development, and found that the cell contains serine racemase catalyzing D-serine synthesis, and D-serine dehydratase and D-amino acid oxidase catalyzing D-serine degradation. In this study, we also examine the function of E.coli YggS, a homolog of the unknown mammalian protein, PROSC, which exhibits the similarity in the primary structure with the bacterial alanine racemase.
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