Biochemical characterization of functional enzymes involved in L-hydroxyproline metabolism from bacteria
| Project/Area Number |
25440049
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Ehime University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | L-ヒドロキシプロリン / 遺伝子クラスター / 物質代謝 / ヒドロキシプロリン / 微生物の物質代謝 / フラビン依存性脱水素酵素 / プロリン / コラーゲン / 微生物代謝 / 脱水素酵素 / 代謝経路 |
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| Outline of Final Research Achievements |
Biochemical characterization of functional enzymes involved in L-hydroxyproline metabolism from bacteria were carried out. D-Hydroxyproline dehydrogenase consisted of α-,β- and γ-subunits, in which the β-subunit played a role as a catalytic subunit, and the remaining them functioned to maintain the structural folding and/or to improve the catalysis. A lysine residue at the position of 164 formed a Schiff base intermediate under NaBH4. Several bacteria could metabolize not only 4-hydroxyproline but also 3-hydroxyproline, and trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline 2-carboxylate reductase involved in the 3-hydroxyptoline metabolism were identified enzymatically and genetically.
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Report
(4 results)
Research Products
(31 results)
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[Journal Article] An enzymatic method to estimate the content of L-hydroxyproline2015
Author(s)
Watanabe, S., Hiraoka, Y., Endo, S., Tanimoto, Y., Tozawa, Y. and Watanabe, Y.
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Journal Title
Journal of Biotechnology
Volume: 199
Pages: 9-16
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] A bienzyme electrochemical biosensor for the detection of collagen L-hydroxyproline2015
Author(s)
Sakamoto, H., Watanabe, K., Koto, A., Koizumi, G., Satomura, T., Watanabe, S. and Suye, SI.
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Journal Title
Sensing and Bio-sensing Research
Volume: 4
Pages: 37-39
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] Diversity in Guanosine 3′,5′-Bisdiphosphate (ppGpp) Sensitivity Among Guanylate Kinases of Bacteria and Plants.2014
Author(s)
Nomura, Y., Izumi, A., Fukunaga, Y. Kusumi, K., Iba, K., Watanabe, S., Nakahira, Y., Weber, A. P., Nozawa, A., and Tozawa, Y.
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Journal Title
J. Biol. Chem.
Volume: 289
Issue: 22
Pages: 15631-15641
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria.2014
Author(s)
Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S., and Watanabe, Y.
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Journal Title
FEBS Open Bio
Volume: 4
Issue: 1
Pages: 240-250
DOI
Related Report
Peer Reviewed
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