2012 Fiscal Year Final Research Report
Function and regulation of D-amino acid biosystem in eukaryote
| Project/Area Number |
22380058
|
|---|
| 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 |
|
|---|
| 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) |
2010 – 2012
|
| Keywords | D-アミノ酸 / D-セリン / D-アスパラギン酸 / Dictyostelium discoidium / D-セリンデヒドラターゼ / セリンラセマーゼ |
|---|
| 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.
|
