| Project/Area Number |
08680683
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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 |
YOSHIMURA Tohru Kyoto University・Institute for Chemical Research, Associate Professor, 化学研究所, 助教授 (70182821)
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| Co-Investigator(Kenkyū-buntansha) |
ESAKI Nobuyoshi Kyoto University・Institute for Chemical Research, Professor, 化学研究所, 教授 (50135597)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1997: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1996: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | coenzyme / molecular evolution / pyridoxal phosphate / stereochemistry / aminotransafearse / lyase / glutamate racemase |
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| Research Abstract |
The stereospecificities for the hydrogen transfer between C-4' of the cofactor and substrate in the transamination catalyzed by various pyridoxal 5'-phosphate (PLP)-dependent enzymes have been studied. The stereospecificities reflect the active-site structures of the enzymes, especially the topographical situation of a coenzyme-substrate Schiff base and a catalytic base for the hydrogen transfer. We found that three types of enzymes catalyzing the reaction stereospecifically on either si-or re-face of the planar intermediate, and alternatively non-stereospecifically on both faces. The classification of PLP-enzymes based on the stereospecificcity for the hydrogen transfer coincident with that based on their primary and three dimensional structures. These suggest that PLP-enzymes have been evolved from at least three different ancestral proteins. These studies lead us the speculation that enzymes requiring coenzymes were created by the combination of the inherently active coenzymes and protein offering the place of the reactions. We attempted to produce a new enzyme by combining a hemin and glutamate recemase showing a significant similarity with mammalian myoglobins in their primary structures.
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