In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.

@article{Choi2008InVR,
  title={In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.},
  author={Yoo Seong Choi and Houjin Zhang and Joseph S. Brunzelle and Satish K Nair and Huimin Zhao},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 19},
  pages={
          6858-63
        }
}
p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of the cofactor remains a controversy. Here, we report the in vitro reconstitution of the AurF enzyme… CONTINUE READING

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Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus.

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Nitroaromatic compounds, from synthesis to biodegradation.

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