2011 Fiscal Year Final Research Report
Investigation of the reaction mechanism of orotidine monophosphate decarboxylase using the distortion of the substrate
Project/Area Number |
22770102
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | Kyoto University |
Principal Investigator |
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Co-Investigator(Renkei-kenkyūsha) |
ISHIDA Toyokazu 産業技術総合研究所, 計算科学, 研究員 (70443166)
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Research Collaborator |
KOTRA P. lakshmi トロント総合研究所
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Project Period (FY) |
2010 – 2011
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Keywords | X線結晶解析 |
Research Abstract |
Orotidine 5'-monophosphate decarboxylase(ODCase) accelerates the decarboxylation of orotidine 5'-monophosphate(OMP) to uridine 5'-monophosphate(UMP) by 17 orders of magnitude. We have determined several crystal structures with ligand analogues and performed computer simulations of the enzyme's short-lived intermediates. The results show that ODCase catalyzes the decarboxylation reaction utilizing both ground state destabilization and transition state stabilization.
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