2015 Fiscal Year Final Research Report
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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| Keywords | L-ヒドロキシプロリン / 遺伝子クラスター / 物質代謝 |
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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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| Free Research Field |
生化学
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