Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans.

  title={Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans.},
  author={Jochen W A Koetter and Georg E. Schulz},
  journal={Journal of molecular biology},
  volume={352 2},
The crystal structure of 6-hydroxy-d-nicotine oxidase (EC was solved by X-ray diffraction analysis in three crystal forms at resolutions up to 1.9 A. The enzyme is monomeric in solution and also in the mother liquor but formed disulfide-dimers in all crystals. It belongs to the p-cresol methylhydroxylase-vanillyl-alcohol oxidase family and contains an FAD covalently bound to the polypeptide. The covalent bond of this enzyme was the first for which a purely autocatalytic formation had… CONTINUE READING

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