Molecular Bases of Enantioselectivity of Haloalkane Dehalogenase DbjA
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- SATO Yukari
- Japan Biological Informatics consortium
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- NATSUME Ryo
- Japan Biological Informatics consortium
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- PROKOP Zbynek
- Faculty of Science, Masaryk University
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- BREZOVSKY Jan
- Faculty of Science, Masaryk University
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- CHALOUPKOVA Radka
- Faculty of Science, Masaryk University
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- DAMBORSKY Jiri
- Faculty of Science, Masaryk University
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- NAGATA Yuji
- Graduate School of Life Sciences, Tohoku University
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- SENDA Toshiya
- Biomedicinal Information Research Center, National Institute of Advanced Industrial Science and Technology
Bibliographic Information
- Other Title
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- 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
- ハロアルカン ダツハロゲン コウソ DbjA ノ キョウゾウ イセイタイ センタクセイ キコウ ノ カイメイ
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Description
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.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 53 (2), 124-129, 2011
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679066080384
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- NII Article ID
- 10028253974
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 11112864
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed
