Establishment of a guideline to improve the low-temperature activity of thermophilic enzymes
Project/Area Number |
24560966
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biofunction/Bioprocess
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Research Institution | Tokyo University of Pharmacy and Life Science |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
|
Keywords | 酵素工学 / 好熱菌酵素 / 酵素利用 |
Outline of Final Research Achievements |
Thermophilic enzymes are generally stable and potentially useful for industrial processes. However, a crucial drawback for their use is that they are often nearly inactive at moderate and low temperatures. I previously reported that a small change in side-chain volume of a non-polar residue that interacts with the adenine moiety of the coenzyme NAD enhances the catalytic efficiency of the thermostable 3-isopropylmalate dehydrogenase and lactate dehydrogenase from the extreme thermophile Thermus thermophiles. In this study, I produced mutants of the glucose-1-dehydrogenase from the hyperthermophile Sulfolobus tokodaii in which one of the coenzyme-binding, non-polar residues was replaced by another non-polar residue. Because the mutant showed the improved low-temperature activity, I conclude that a small volume change of a non-polar residue’s side chain that interacts with the adenine of NAD(P) in a dehydrogenase will provide a general method to improve its low temperature activity.
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Report
(4 results)
Research Products
(43 results)
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[Journal Article] Evaluation of the protein interfaces that form an intermolecular four-helix bundle as studied by computer simulation2014
Author(s)
Fukuda, M., Komatsu, Y., Yamada, H., Morikawa, R., Miyakawa, T., Takasu, M., Akanuma, S., Yamagishi, A
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Journal Title
Molecular Simulation
Volume: 40
Issue: 6
Pages: 498-503
DOI
Related Report
Peer Reviewed
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[Journal Article] Preparation of Phi29 DNA polymerase free of amplifiable DNA using ethidium monoazide, an ultraviolet-free light-emitting diode lamp and trehalose2014
Author(s)
Takahashi, H., Yamazaki, H., Akanuma, S., Kanahara, H., Saito, T., Chimuro, T., Kobayashi, T., Ohtani, T., Yamamoto, K., Sugiyama, S., Kobori, T.
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Journal Title
PLoS ONE
Volume: 9
Issue: 2
Pages: e82624-e82624
DOI
Related Report
Peer Reviewed
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[Journal Article] N-terminal Hydrophobic Amino Acids of Activating Transcription Factor 5 (ATF5) Protein Confer Interleukin 1β (IL-1β)-induced Stabilization.2014
Author(s)
Abe T, Kojima M, Akanuma S, Iwashita H, Yamazaki T, Okuyama R, Ichikawa K, Umemura M, Nakano H, Takahashi S, Takahashi Y
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Journal Title
Journal of Biological Chemistry
Volume: 289
Issue: 7
Pages: 3888-3900
DOI
Related Report
Peer Reviewed
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[Journal Article] Characterization of the low-temperature activity of Sulfolobus tokodaii glucose-1-dehydrogenase mutants2014
Author(s)
Sugii, T., Akanuma, S., Yagi, S., Yagyu, K., Shimoda, Y., Yamagishi, A.
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Journal Title
J. Biosci. Bioeng
Volume: ***
Issue: 4
Pages: 16010-16010
DOI
NAID
Related Report
Peer Reviewed
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[Journal Article] The simulation study of protein-protein interfaces based on the 4-helix bundle structure2013
Author(s)
Fukuda, M., Komatsu, Y., Morikawa, R., Miyakawa, T., Takasu, M., Akanuma, S., Yamagishi A.
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Journal Title
AIP Conf. Proc.
Volume: 1518
Pages: 606-609
DOI
Related Report
Peer Reviewed
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