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dc.contributor.author藤橋, 雅宏
dc.contributor.alternativeFujihashi, Masahiro
dc.contributor.transcriptionフジハシ, マサヒロ
dc.date.accessioned2018-01-19T00:29:38Z-
dc.date.available2018-01-19T00:29:38Z-
dc.date.issued2017-12
dc.identifier.issn2432-0587
dc.identifier.urihttp://hdl.handle.net/2433/228933-
dc.description.abstractLife 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.
dc.format.mimetypeapplication/pdf
dc.language.isojpn
dc.publisher京都大学物性科学センター
dc.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
dc.title.alternative<Research Report>Catalytic mechanism of an enzyme utilizing substrate distortion
dc.type.niitypeDepartmental Bulletin Paper
dc.identifier.ncidAA11853306
dc.identifier.jtitle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)
dc.identifier.volume31
dc.identifier.spage3
dc.identifier.epage8
dc.textversionpublisher
dc.sortkey01
dc.address京都大学大学院理学研究科 化学専攻
dc.address.alternativeDepartment of Chemistry, Graduate School of Science, Kyoto University
dc.relation.urlhttp://www.ltm.kyoto-u.ac.jp/centershi/
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