Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme.

@article{Barna2002CrystalSO,
  title={Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme.},
  author={Ter{\'e}z Barna and Hanan Latif Messiha and Carlo Petosa and Neil C Bruce and Nigel S. Scrutton and Peter C E Moody},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 34},
  pages={30976-83}
}
The crystal structure of the NADH-dependent bacterial flavoenzyme morphinone reductase (MR) has been determined at 2.2-A resolution in complex with the oxidizing substrate codeinone. The structure reveals a dimeric enzyme comprising two 8-fold beta/alpha barrel domains, each bound to FMN, and a subunit folding topology and mode of flavin-binding similar to that found in Old Yellow Enzyme (OYE) and pentaerythritol tetranitrate (PETN) reductase. The subunit interface of MR is formed by… CONTINUE READING

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