Biochemical Research of Novel Carbohydrate Metabolic Pathway for Development of Efficient Conversion of Biornass
| Project/Area Number |
18570126
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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 |
Functional biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
KODAKI Tsutomu Kyoto University, Institute of Advanced Energy, Bioenerv Researth Safiun, Associate Professor (70170264)
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| Co-Investigator(Kenkyū-buntansha) |
MAKINO Keisuke KYOTO UNIVERSITY, Institute of Advanced Energy, Bioenerv Researth Safiun, Professor (50159141)
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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 |
¥4,010,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥510,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2006: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | Carbohydrate Metabolism / Biomass / Arabinose / Enzyme / Efficient Conversion |
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| Research Abstract |
L-Arabinose is a major constituent of some plant materials, and L-arabinose catabolism is therefore relevant for microorganisms using plant material as a carbon source. The metabolic pathway from L-arabinose to D-xylulose 5-phosphate in bacterium has been investigated extensively. It is believed that there are two alternative pathways for bacterial L-arabinose metabolism, which do not involve a phosphorylation reaction, in contrast to the known bacterial pathway. In the first pathway, L-arabinose is oxidized to L-arabino-γ-lactone by NAD(P)+-dependent dehydrogenase. The lactone is cleaved by a lactonase to L-arabonate, followed by two successive dehydration reactions forming L-2-keto-3-deoxyarabonate (L-KDA) and α-ketoglutaric semialdehyde. The last step is the NAD(P)+-dependent dehydrogenation of the semialdehyde to α-ketoglutaric acid. The second pathway has the same initial three steps, but L-KDA is cleaved through an aldolase reaction to glycoaldehyde and pyruvate. No gene-encoding enzyme involved in these alternative pathways of L-arabinose metabolism had been identified so far. In this study, L-arabinose 1-dehydrogenase catalyzing the conversion of L-arabinose to L-arabino-γ-lactone was characterized as an enzyme responsible for the first step of this alternative pathway of L-arabinose metabolism. The gene encoding L-arabinose 1-dehydrogenase was cloned using a partial peptide sequence of the purified enzyme and was overexpressed in Escherichia coli as a fully active enzyme. This is the first identification of a gene involved in an alternative pathway of L-arabinose metabolism in bacterium. Furthermore, the four other enzymes and the relevant genes were also characterized as L-arabinonolactonase, L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase, and α-ketogoutaric semialdehyde dehydrogease by biochemical analysis.
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Report
(3 results)
Research Products
(45 results)
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[Journal Article] Ethanol production from xylose by recombinant Saccharomyces cerevisiae expressing protein engineered NADP+-dependent xylitol dehydrogenase2007
Author(s)
S., Watanabe, A.A., Saleh, S.P., Pack, N., Annaluru, T., Kodaki, K., Makino
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Journal Title
J. Biotechnol 130
Pages: 316-319
Description
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Related Report
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[Journal Article] Ethanol production from xylose by recombinant Saccharomyces cerevisiae expressing protein-engineered NADH-preferring xylose reductase from Pichia stipitis2007
Author(s)
S., Watanabe, A.A., Saleh, S.P., Pack, N., Annaluru, T., Kodaki, K., Makino
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Journal Title
Microbiology 153
Pages: 3044-3054
Description
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[Journal Article] The positive effect of the decreased NADPH-preferring activity of xylose reductase from Pichia stipitis on ethanol production using xylose-fermenting recombinant Saccharomyces cerevisiae2007
Author(s)
S., Watanabe, S.P., Pack, A.A., Saleh, N., Annaluru, T., Kodaki, K., Makino
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Journal Title
Biosci. Biotechnol. Biochem 71
Pages: 1365-1369
NAID
Description
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[Presentation] Crystallization and preliminary X-ray diffraction studies of xylitol dehydrogenase, a key enzyme for bioethanol production using yeast2006
Author(s)
J., Matsui, S., Watanabe, T., Kodaki, B., Mikami, K., Makino
Organizer
20th IUBMB International Congress of Biochemistry and Molecular Biology
Place of Presentation
Kyoto Japan
Year and Date
2006-06-19
Description
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Related Report
