| Project/Area Number |
17380060
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
KIMURA Atsuo Hokkaido University, Research Faculty of Agriculture, Professor (90186312)
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| Co-Investigator(Kenkyū-buntansha) |
MORI Haruhide Hokkaido University, Research Faculty of Agriculture, Associate Professor (80241363)
OKUYAMA Masayuki Hokkaido University, Research Faculty of Agriculture, Assistant Professor (00344490)
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| Project Period (FY) |
2005 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥15,890,000 (Direct Cost: ¥14,600,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2007: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2006: ¥5,000,000 (Direct Cost: ¥5,000,000)
Fiscal Year 2005: ¥5,300,000 (Direct Cost: ¥5,300,000)
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| Keywords | Enzyme reaction / Sugar / Protein engineering |
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| Research Abstract |
This project is about the enzymes having the structure similar to α-glucosidase; i.e. α-xylosidase, glucan lyase, cyclic-tetrasaccharide-forming enzyme, and α-glucosidase, each of which catalyzes the different reaction. Three-dimensional structure available recently allows us to analyze the molecular mechanism of reactions exhibited by four enzymes. The purposes of research are 1) to elucidate the relationship between substrate and amino acid residue(s) in the catalytic site; 2) to analyze the function of catalytic residues; 3) to elucidate the structural element(s) to display the above-described different reactions; 4) to synthesize the useful enzyme. Results are as follows.
(1) We analyzed the amino acid residues in the catalytic site of α-xylosidase to recognize α-xyloside-structure, and succeeded in conversion of α-xylosidase into α-glucosidase by the mutagenesis of its structural elements. (2) The catalytic residues were identified and their functions were investigated. (3) Amino acid replacement of α-glucosidase (a hydrolyzing enzyme) lost its hydrolytic activity and enhanced the transglucosidation ability, meaning the conversion of hydrolyzing enzyme into transferring enzyme. (4) We have succeed in change of transferring products.
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