2011年
ハロアルカン脱ハロゲン酵素DbjAの鏡像異性体選択性機構の解明
日本結晶学会誌
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- 巻
- 53
- 号
- 2
- 開始ページ
- 124
- 終了ページ
- 129
- 記述言語
- 日本語
- 掲載種別
- 記事・総説・解説・論説等(学術雑誌)
- DOI
- 10.5940/jcrsj.53.124
- 出版者・発行元
- The Crystallographic Society of Japan
Enzymes are widely used for the synthesis of pharmaceuticals, agrochemicals, and food additives because they can catalyze high enantioselective transformations. In order to construct selective enzymes by protein engineering, it is important to understand the molecular basis of enzyme-substrate interactions that contribute to enantioselectivity. The haloalkane dehalogenase DbjA showed high enantioselectivity for two racemic mixtures: α-bromoesters and β-bromoalkanes. Thermodynamic analysis, protein crystallography, and computer simulations indicated that DbjA carries two bases for the enantiodiscrimination of each racemic mixture. This study helps us understand the molecular basis of the enantioselectivity and opens up new possibilities for constructing enantiospecific biocatalysts through protein engineering.
- リンク情報
- ID情報
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- DOI : 10.5940/jcrsj.53.124
- ISSN : 0369-4585
- CiNii Articles ID : 10028253974
- CiNii Books ID : AN00188364