Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis.

@article{Nomura2013CrystalSO,
  title={Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis.},
  author={Junpei Nomura and Hiroshi Hashimoto and Takehiro Ohta and Yoshiteru Hashimoto and Koichi Wada and Yoshinori Naruta and Ken-ichi Oinuma and Michihiko Kobayashi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 8},
  pages={2810-5}
}
Aldoxime dehydratase (OxdA), which is a unique heme protein, catalyzes the dehydration of an aldoxime to a nitrile even in the presence of water in the reaction mixture. Unlike the utilization of H(2)O(2) or O(2) as a mediator of catalysis by other heme-containing enzymes (e.g., P450), OxdA is notable for the direct binding of a substrate to the heme iron… CONTINUE READING