Construction of D-aminoacyl peptides synthetase
| Project/Area Number |
20780075
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | Tottori University |
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Principal Investigator |
ARIMA Jiro Tottori University, 農学部, 講師 (80393411)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2010: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2008: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | タンパク質工学 / D-アミノペプチダーゼ / アミノリシス / ペプチド合成 / 活性中心セリン残基 / 基質特異性 / キメラ酵素 |
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| Research Abstract |
Peptides incorporating D-amino acids are expected to increase the functional variety and applications of peptides. In this study, we constructed the mutant D-aminopeptidases as a convenient tool for synthesis of peptides incorporating D-amino acids. We obtained a serine D-stereospecific amidohydrolase that exhibit peptide bond formation activity by catalysis of aminolysis reaction. The enzyme utilizes D-Pro derivatives as acyl donor substrate, and exhibit efficient synthesis of cyclo (D-Pro-L-Arg) that has chitinase inhibitory activity in a one-pot reaction manner. In addition, we identified the residue, Asn193, which associates the recognition of side chain of acyl donor, from the mutation analysis.
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Report
(4 results)
Research Products
(17 results)
