紀要論文 <研究ノート>基質の歪みを利用する酵素の反応触媒機構
<Research Report>Catalytic mechanism of an enzyme utilizing substrate distortion

藤橋, 雅宏

内容記述
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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http://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/228933/1/LTM-31_3.pdf

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