The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.

@article{Benach2003The2C,
  title={The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.},
  author={Jordi Benach and Insun Lee and William Edstrom and Alexandre P. Kuzin and Yiwen Chiang and Thomas B. Acton and Gaetano T. Montelione and John Francis Hunt},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 21},
  pages={19176-82}
}
We present here the 2.3-A crystal structure of the Escherichia coli YdiB protein, an orthologue of shikimate 5-dehydrogenase. This enzyme catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway, which is absent in mammals but required for the de novo synthesis of aromatic amino acids, quinones, and folate in many other organisms. In this context, the shikimate pathway has been promoted as a target for the development of antimicrobial agents. The crystal… CONTINUE READING
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