Mutagenesis of an Asn156 Residue in a Surface Region of S-Selective Hydroxynitrile Lyase from Baliospermum montanum Enhances Catalytic Efficiency and Enantioselectivity.

@article{Kawahara2015MutagenesisOA,
  title={Mutagenesis of an Asn156 Residue in a Surface Region of S-Selective Hydroxynitrile Lyase from Baliospermum montanum Enhances Catalytic Efficiency and Enantioselectivity.},
  author={Nobuhiro Kawahara and Yasuhisa Asano},
  journal={Chembiochem : a European journal of chemical biology},
  year={2015},
  volume={16 13},
  pages={
          1891-1895
        }
}
The S-selective hydroxynitrile lyase from Baliospermum montanum (BmHNL) has broad substrate specificity toward aromatic substrates as well as high temperature stability, although with low enantioselectivity and specific activity. To expand the industrial application of this enzyme, we improved its enantioselectivity and specific activity toward (S… CONTINUE READING