| Budget Amount *help |
¥17,810,000 (Direct Cost: ¥13,700,000、Indirect Cost: ¥4,110,000)
Fiscal Year 2012: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2011: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2010: ¥9,360,000 (Direct Cost: ¥7,200,000、Indirect Cost: ¥2,160,000)
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| Research Abstract |
In these studies, we examined the role of zinc in the D-serine dehydratase of Saccharomycescerevisiae. We also studied the reaction mechanism of serine racemase of a slime cellularmold, Dictyostelium discoidium, and found that the enzyme reaction proceeds through thetwo-base mechanism with Lys56 and Ser81. In order to clarify the role of D-aspartatein mammals, we cloned the gene of mouse GOT1L1, which was suggested to be an asparateracemase, and attempted to purify the protein. We also studied the D-serine metabolismin D. discoidium to understand the role of D-serine in development. We constructed themutant D. discoidium cells lacking D-serine dehydratase, which is responsible for theD-serine degradation. The mutant cells contained D-serine at their multicellular stageand showed the defects in fruiting body formation. We also constructed the polyethyleneglycol-modified D-serine dehydratase, which can be a tool for the in vivo D-serinedegradation. The modified enzyme exhibited a decreased immunogenicity.
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