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Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases
Author(s) -
Scheller Philipp N.,
Fademrecht Silvia,
Hofelzer Sebastian,
Pleiss Jürgen,
Leipold Friedemann,
Turner Nicholas J.,
Nestl Bettina M.,
Hauer Bernhard
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402213
Subject(s) - imine , enzyme , chemistry , combinatorial chemistry , biocatalysis , functional diversity , catalysis , stereoselectivity , artificial enzyme , stereochemistry , biochemistry , reaction mechanism , biology , ecology
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.