Departmental Bulletin Paper <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

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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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