2012 Fiscal Year Final Research Report
Characterization of the catalytic mechanism of DyP which is a representative novel peroxidase family.
| Project/Area Number |
22570136
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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 | Japan Women's University (2011-2012)
Tokyo Institute of Technology (2010) |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
TSUGE Hideaki 京都産業大学, 総合生命科学部, 教授 (40299342)
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| Project Period (FY) |
2010 – 2012
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| Keywords | DyP / 触媒メカニズム / X線結晶構造解析 |
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| Research Abstract |
So far, the catalytic mechanism of DyP was unknown. In this study, we have proved that aspartic acid 171 is the catalytic residue because the mutant of aspartic acid to asparagine has lost the activity completely. We’ve also proposed that the catalytic mechanism depends on the swinging movement of the aspartic acid. Throughout the whole research, DyP has been assigned a new EC number (EC 1.11.1.19) and has been taken notice over the world.
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