Structural basis for chiral substrate recognition by two 2,3‐butanediol dehydrogenases

@article{Otagiri2010StructuralBF,
  title={Structural basis for chiral substrate recognition by two 2,3‐butanediol dehydrogenases},
  author={M. Otagiri and S. Ui and Y. Takusagawa and T. Ohtsuki and G. Kurisu and M. Kusunoki},
  journal={FEBS Letters},
  year={2010},
  volume={584}
}
  • M. Otagiri, S. Ui, +3 authors M. Kusunoki
  • Published 2010
  • Chemistry, Medicine
  • FEBS Letters
  • 2,3‐Butanediol dehydrogenase (BDH) catalyzes the NAD‐dependent redox reaction between acetoin and 2,3‐butanediol. There are three types of homologous BDH, each stereospecific for both substrate and product. To establish how these homologous enzymes possess differential stereospecificities, we determined the crystal structure of l‐BDH with a bound inhibitor at 2.0 Å. Comparison with the inhibitor binding mode of meso‐BDH highlights the role of a hydrogen‐bond from a conserved Trp residue192… CONTINUE READING
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