Molecular Characterization of Reversible Decarboxylases Catalyzing CO_2 Fixation and Their Application to Molecular Conversion Process
| Project/Area Number |
14560061
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | Gifu University |
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Principal Investigator |
YOSHIDA Toyokazu Gifu University, Faculty of Engineering, Associate Professor, 工学部, 助教授 (90220657)
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| Co-Investigator(Kenkyū-buntansha) |
MITSUKURA Koichi Gifu University, Faculty of Engineering, Research Assistant, 工学部, 助手 (70324283)
NAGASAWA Toru Gifu University, Faculty of Engineering, Professor, 工学部, 教授 (60115904)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2003: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2002: ¥2,800,000 (Direct Cost: ¥2,800,000)
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| Keywords | Decarboxylase / Carbon dioxide fixation / Aromatic carboxylic acids / Cloning / Microbial conversion / 炭酸固定 / 4-ヒドロキシ安息香酸 / レゾルシン酸 / ピロール-2-カルボン酸 / インドール-3-カルボン酸 / ピロール / インドール |
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| Research Abstract |
Generally, decarboxylases can not catalyze the reverse carboxylation reaction. However, we found novel decarboxylases efficiently catalyzing nonoxidative decarboxyation. In the metabolism of phenol in the absence of oxygen, 4-hydroxybenzoate decarboxylase found to catalyze carbon dioxide fixation. In the view point of application to chemical industry, the reversible decarboxylases are useful for the synthesis of aromatic carboxylic acids, because a carboxyl group is regioselectively introduced into aromatic ring. In the present research, we screened novel decarboxylases reversibly catalyzing nonoxidative decarboxylation, revealed physicochemical and molecular characteristics, and evaluated the reverse carboxylation activities.
The primary structures of pyrrole-2-carboxylate decarboxylase and indole-3carboxylate decarboxylase were determined from their gene analysis. These decarboxylases showed similarity to various microbial hypothetical proteins. In the screening of 4-hydroxybenzoate decarboxylase, the enzyme activity was widely detected in various bacteria, actinomycetes and yeasts, contrary to the previous observation. As for 2,6-dihydroxybenzoate decarboxylase, a novel decarboxylase, the efficient regioselecetive carboxylation of 1,3-dihydroxybenzene was confirmed in the presence of KHCO_3. From the analyses for enzymatic properties and structures, various reversible decarboxylase were classified into two subgroups.
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Report
(3 results)
Research Products
(7 results)
