| Project/Area Number |
18380061
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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 microbiology
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| Research Institution | Toyama Prefectural University |
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Principal Investigator |
ASANO Yasuhisa Toyama Prefectural University, Department of Biotechnology, Professor (00222589)
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| Co-Investigator(Kenkyū-buntansha) |
KOMEDA Hidenobu Toyama Prefectural University, Faculty of Engineering, Lecturer (50285160)
YAMANE Takashi Nagoya University, Faculty of Engineering, Professor (80030055)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥12,650,000 (Direct Cost: ¥11,300,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2007: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2006: ¥6,800,000 (Direct Cost: ¥6,800,000)
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| Keywords | amino acid amide / racemase / amidase / D-aminooeptidase / aloha-amino-ensilon-canrolactam racemase / D-amino acid |
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| Research Abstract |
1. Amino acid amide racemizing activity was discovered in alpha-amino-epsilon-caprolactam (ACL) racemase from Achromobacter obae.
2. Amino acid amidases acting for various amino mid amides, such as D-aminopeptidase (DAP), D-amino acid amidase (DAA), were isolated from various microbial sources, their primary structures deduced and expression in E. coli were made possible.
3. The enzymatic synthesis of D-alanin from L-alanine amide has been demonstrated by use of D-aminopeptidase (DAP) from Ochrobactrum anthropi C1-38 and ACL racemase. The result of successive enzymatic reaction shows that the combination of ACL racemase and DAP can be applied for dynamic kinetic resolution of DL-amino acid amides to yield D-amino acids.
4. Structure of DAA and directed evolution of ACL racemase: We developed a colorimetric method to measure the activity of ACL racemase with stereospecific amino acid amidase and amino acid oxidase, and 4-aminoantipyrine. The structure of D-amino acid amidase from Ochrobactrum anthropiSV3 was solved at 2.1A resolution.
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