Substrate binding mechanism of a type I extradiol dioxygenase.

@article{Cho2010SubstrateBM,
  title={Substrate binding mechanism of a type I extradiol dioxygenase.},
  author={Hyo Je Cho and Kyungsun Kim and Seo Yean Sohn and Ha Yeon Cho and Kyung Jin Kim and Myung Hee Kim and Dockyu Kim and Eungbin Kim and Beom Sik Kang},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 45},
  pages={34643-52}
}
A meta-cleavage pathway for the aerobic degradation of aromatic hydrocarbons is catalyzed by extradiol dioxygenases via a two-step mechanism: catechol substrate binding and dioxygen incorporation. The binding of substrate triggers the release of water, thereby opening a coordination site for molecular oxygen. The crystal structures of AkbC, a type I extradiol dioxygenase, and the enzyme substrate (3-methylcatechol) complex revealed the substrate binding process of extradiol dioxygenase. AkbC is… CONTINUE READING
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