Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone.

@article{Wilce1997CrystalSO,
  title={Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone.},
  author={Matthew C. J. Wilce and David M. Dooley and Hans C. Freeman and J Mitchell Guss and Hideyuki Matsunami and W S Mcintire and Christy Ruggiero and Katsuyuki Tanizawa and Hiroshi Yamaguchi},
  journal={Biochemistry},
  year={1997},
  volume={36 51},
  pages={16116-33}
}
The crystal structures of the copper enzyme phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globiformis (AGAO) have been determined and refined for three forms of the enzyme: the holoenzyme in its active form (at 2.2 A resolution), the holoenzyme in an inactive form (at 2.8 A resolution), and the apoenzyme (at 2.2 A resolution). The holoenzyme has a topaquinone (TPQ) cofactor formed from the apoenzyme by the post-translational modification of a tyrosine residue in the… CONTINUE READING

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