Structure and activity of NADPH-dependent reductase Q1EQE0 from Streptomyces kanamyceticus, which catalyses the R-selective reduction of an imine substrate.

@article{RodrguezMata2013StructureAA,
  title={Structure and activity of NADPH-dependent reductase Q1EQE0 from Streptomyces kanamyceticus, which catalyses the R-selective reduction of an imine substrate.},
  author={Mar{\'i}a Rodr{\'i}guez-Mata and Annika Frank and Elizabeth K. Wells and Friedemann Leipold and Nicholas J. Turner and Sam J. Hart and Johan P Turkenburg and Gideon Grogan},
  journal={Chembiochem : a European journal of chemical biology},
  year={2013},
  volume={14 11},
  pages={1372-9}
}
NADPH-dependent oxidoreductase Q1EQE0 from Streptomyces kanamyceticus catalyzes the asymmetric reduction of the prochiral monocyclic imine 2-methyl-1-pyrroline to the chiral amine (R)-2-methylpyrrolidine with >99% ee, and is thus of interest as a potential biocatalyst for the production of optically active amines. The structures of Q1EQE0 in native form, and in complex with the nicotinamide cofactor NADPH have been solved and refined to a resolution of 2.7 Å. Q1EQE0 functions as a dimer in… CONTINUE READING
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