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- W2007809174 abstract "Reducing reactions are among the most useful transformations for the generation of chiral compounds in the fine-chemical industry. Because of their exquisite selectivities, enzymatic approaches have emerged as the method of choice for the reduction of CO and activated CC bonds. However, stereoselective enzymatic reduction of CN bonds is still in its infancy—it was only recently described after the discovery of enzymes capable of imine reduction. In our work, we increased the spectrum of imine-reducing enzymes by database analysis. By combining the currently available knowledge about the function of imine reductases with the experimentally uncharacterized diversity stored in protein sequence databases, three novel imine reductases with complementary enantiopreference were identified along with amino acids important for catalysis. Furthermore, their reducing capability was demonstrated by the reduction of the pharmaceutically relevant prochiral imine 2-methylpyrroline. These novel enzymes exhibited comparable to higher catalytic efficiencies than previously described enzymes, and their biosynthetic potential is highlighted by the full conversion of 2-methylpyrroline in whole cells with excellent selectivities." @default.
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- W2007809174 date "2014-08-27" @default.
- W2007809174 modified "2023-09-23" @default.
- W2007809174 title "Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases" @default.
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- W2007809174 doi "https://doi.org/10.1002/cbic.201402213" @default.
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