| Project/Area Number |
03660113
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
応用微生物学・発酵学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
MURATA Kousaku Kyoto University Res. Inst. Food Sci. Associate professor, 食糧科学研究所, 助教授 (90142299)
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| Co-Investigator(Kenkyū-buntansha) |
INOUE Yoshiharu Kyoto University Res. Inst. Food Sci. Research Associate, 食糧科学研究所, 助手 (70203263)
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| Project Period (FY) |
1991 – 1993
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| Project Status |
Completed (Fiscal Year 1992)
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| Budget Amount *help |
¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 1992: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1991: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | C-P bond / C-P bond cleavage enzyme / C-P hydrolase / C-P lyase / CーP結合 / CーP結合解裂酵素 / CーP結合加水分解酵素 / CーPリア-ゼ |
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| Research Abstract |
A direct carbon-phosphorus (C-P) bond is highly stable and resistant to chemical hydrolysis, thermal decomposition and photolysis. Therefore, biological cleavage of the C-P bond in natural habitats assumes importance as a mean to prevent the accumulation of phosphonates. Some bacterial cells are known to use various phosphonates for growth. However, all attempts to detect C-P bond cleavage activity in cell-free systems have resulted in failure, and the problem of how and by what means these bacteria can cleave the C-P bond in phosphonates remains unsolved. We have succeeded, for the first time, in the detection of C-P bond cleavage activity in cell-free extracts of a bacterium Enterobacter aerogenes, and isolated an enzyme responsible for the activity. The enzyme catalyzed the C-P bond cleavage and produced inorganic phosphate. Formation of alkane was not observed. The enzyme was then designated C-P hydrolase to descriminate from C-P lyase and phosphonatase. The enzyme required two proteins (E2 and E3) for activity. E2 was 650 kDa in molecular size. The function of E2 is to convert stable C-P bond into unstable one. E3 was a homodimer of a subunit with M.W. of 55 kDa. The function of the protein is to hydrolyze C-P bond being unstabled by E2 protein. The entire gene covering E2 and E3 structural regions was cloned from the organism and its structure was also analyzed.
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