Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp.

@article{Bannwarth2004CrystalSO,
  title={Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp.},
  author={Michael Bannwarth and Sabine Bastian and Doroth{\'e}e M. Heckmann-Pohl and Friedrich Giffhorn and Georg E. Schulz},
  journal={Biochemistry},
  year={2004},
  volume={43 37},
  pages={11683-90}
}
Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates using dioxygen. The enzyme forms a D(2) symmetric homotetramer and contains one covalently bound FAD per subunit. The structure of the enzyme from Peniophora sp. was determined by multiwavelength anomalous diffraction (MAD) based on 96 selenium sites per crystallographic asymmetric unit and subsequently refined to good-quality indices. According to its chain fold, the enzyme belongs to the large glutathione reductase family… CONTINUE READING

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