Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.

@article{Nakajima1998CrystalSO,
  title={Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.},
  author={Keiji Nakajima and Atsushi Yamashita and Hiroyuki Akama and Toru Nakatsu and Hiroaki Kato and Takashi Hashimoto and J. Oda and Yasuyuki Yamada},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 9},
  pages={4876-81}
}
A pair of tropinone reductases (TRs) share 64% of the same amino acid residues and belong to the short-chain dehydrogenase/reductase family. In the synthesis of tropane alkaloids in several medicinal plants, the TRs reduce a carbonyl group of an alkaloid intermediate, tropinone, to hydroxy groups with different diastereomeric configurations. To clarify the structural basis for their different reaction stereospecificities, we determined the crystal structures of the two enzymes at 2.4- and 2.3-A… CONTINUE READING

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