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- W2312373576 abstract "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." @default.
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- W2312373576 date "2011-01-01" @default.
- W2312373576 modified "2023-10-17" @default.
- W2312373576 title "Molecular Bases of Enantioselectivity of Haloalkane Dehalogenase DbjA" @default.
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- W2312373576 doi "https://doi.org/10.5940/jcrsj.53.124" @default.
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