The mechanism underlying the regulation of biosynthesis and degradation of NADP(H) in Saccharomyces cerevisiae
Project/Area Number |
21780069
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Single-year Grants |
Research Field |
Applied microbiology
|
Research Institution | Kyoto University |
Principal Investigator |
KAWAI Shigeyuki Kyoto University, 農学研究科, 助教 (00303909)
|
Project Period (FY) |
2009 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2009: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
|
Keywords | NADP(H) / NAD(H) / NADキナーゼ / NADHキナーゼ / リン酸化 / NADP(H)フォスファターゼ / 結核菌 / ミトコンドリア / NADPH / NADH / 出芽酵母 / 真菌 / グルコース-6-リン酸脱水素酵素 / 環元型補酵素 / NADP(H)ase / アルファ・ファクター |
Research Abstract |
Due to the difference of the physiological roles between NAD(H) and NADP(H) as well as the significant impacts of them on the cellular metabolism, it is important to elucidate the mechanism underlying the regulation of biosynthesis and degradation of NADP(H). In this study, the tertiary structure of budding yeast NADPH-biosynthetic enzyme (NADH kinase ; Pos5) complexed with NADH was determined at 2.0Å. Detailed analysis including the comparison of the tertiary structure of Pos5 with those of human and bacterial NADP^+-biosynthetic enzymes (NAD kinases) revealed that the Pos5 Arg293 is at least one of the structural determinants of Pos5 for high NADH kinase activity and for discriminating NADH from NAD^+.
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Report
(3 results)
Research Products
(27 results)