2010 Fiscal Year Final Research Report
Molecular mechanism for the catalysis by sphingomyelinase
| Project/Area Number |
20590075
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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 |
Biological pharmacy
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| Research Institution | Osaka University of Pharmaceutical Sciences |
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Principal Investigator |
FUJII Shinobu Osaka University of Pharmaceutical Sciences, 薬学部, 講師 (80218966)
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| Project Period (FY) |
2008 – 2010
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| Keywords | スフィンゴミエリナーゼ / 触媒機構 / 基質認識 |
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| Research Abstract |
We found that Bacillus cereus SMase has at least two bind sites for substrate, one at the active site and the other at the allosteric site (surface recognition site). The cooperative binding of substrate to the allosteric site induced the structure change for the activation of SMase. Pro 26, Trp 28, and Asp 100 of B. cereus SMase were found to be participate the surface recognition. Furthermore, we found that a thiophosphate analog of SM, in which the phosphate oxygen was replaced by sulfur atom, can be used for the substrate of the measurement of SMase activity.
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