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|Other Titles:||<Research Report>Catalytic mechanism of an enzyme utilizing substrate distortion|
|Author's alias:||Fujihashi, Masahiro|
|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)|
|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.|
|Appears in Collections:||第31号|
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