| Budget Amount *help |
¥3,146,000 (Direct Cost: ¥2,420,000、Indirect Cost: ¥726,000)
Fiscal Year 2011: ¥1,508,000 (Direct Cost: ¥1,160,000、Indirect Cost: ¥348,000)
Fiscal Year 2010: ¥1,638,000 (Direct Cost: ¥1,260,000、Indirect Cost: ¥378,000)
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| Research Abstract |
We examined the properties of the serine racemase from Dictyostelium discoideum. The enzyme was found to be unique in its stimulation by N_a^+in addition to Mg^<2+> and Ca^<2+>, which are well-known activators for the mammalian serine racemase. Mutation of the divalent metal ion binding sites abolished both Mg^<2+-> and Na+-dependent stimulation, indicating that Mg^<2+> and Na^+share the common metal ion-binding site. In addition, we studied the catalytic mechanism of D-serine dehydratase from Saccharomyces cerevisiae. We found that the Zn^<2+> is indispensable for the abstraction of.-hydrogen as well as elimination of hydroxyl group from D-serine. We revealed that both.-hydrogen abstraction and hydroxyl group elimination from D-serine occurs in a concerted fashion.
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