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Title: <研究ノート>基質の歪みを利用する酵素の反応触媒機構
Other Titles: <Research Report>Catalytic mechanism of an enzyme utilizing substrate distortion
Authors: 藤橋, 雅宏  KAKEN_name
Author's alias: Fujihashi, Masahiro
Issue Date: Dec-2017
Publisher: 京都大学物性科学センター
Journal title: 京都大学物性科学センター : LTMセンター誌 = Low Temperature and Materials Sciences (Kyoto University)
Volume: 31
Start page: 3
End page: 8
Abstract: Life is an assembly of reactions, and such reactions are controlled by various enzymes. Most of the enzymatic reactions are explained by the transition state stabilization. Here, I summarize the mechanism of orotidine-5’-monophosphate decarboxylase (ODCase), which utilizes an alternative catalytic mechanism, substrate distortion, in addition to the transition state stabilization. The contribution of substrate distribution to catalysis is estimated to be 10-15% of the transition state stabilization.
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