2011 Fiscal Year Final Research Report
Functions and metabolism of D-serine in eukaryote
| Project/Area Number |
22880014
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
ITO Tomokazu 名古屋大学, 生命農学研究科, 助教 (90584970)
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| Project Period (FY) |
2010 – 2011
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| Keywords | D-セリン / D-アミノ酸 / ピリドキサール5'リン酸 |
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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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