| Project/Area Number |
01044016
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research |
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| Research Institution | Tohoku University |
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Principal Investigator |
HATANO Masahiro Chemical Research Institute of Non-aqueous Solutions, Tohoku University, Professor, 非水溶液化学研究所, 教授 (50006293)
籏野 昌弘 東北大, 非水溶液化学研究所, 教授
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| Co-Investigator(Kenkyū-buntansha) |
SHIMIZU Toru Chemical Research Institute of Non-aqueous Solutions, Tohoku Univ., 非水溶液化学研究所, 助教授 (40118956)
FUJII-KURIYAMA Yoshiaki Department of Chemistry, Faculty of Science, Tohoku University, 理学部 化学第二学科, 教授 (00098146)
THOMAS L Pou メリーランド大学, 生化学科, 教授
HATANO Masahiro Chemical Research Institute of Non-aqueous Solutions, Tohoku Univ.
POULOS Thomas L. Center for Advanced Research in Biotechnology of the Maryland Biotechnology Inst
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| Project Period (FY) |
1989
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| Project Status |
Completed (Fiscal Year 1989)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 1989: ¥3,600,000 (Direct Cost: ¥3,600,000)
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| Keywords | Cytochrome P-450 / X-ray crystallography / Site-directed mutagenesis / Computer graphics / Fuction-structure relationship / Heme-protein / Amino acid substitutions / Recombinant DNA |
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| Research Abstract |
A family of protoheme-containing enzymes, collectively called cytochrome P-450(P-450), are involved in a variety of oxidative reactions. Eukaryotic P-450 is a membranebound enzyme, and thus its tertiary structure may differ somewhat from the crystal structure of the soluble bacterial P-450_<cam> decided by Poulos. We had previously developed an efficient expression system for rat liver P-450_d in the Saccharomyces cerevisiae. With site-directed mutageneses, the roles of each amino acids were clarified.
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