Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase.

@article{OLeary2009BiochemicalCO,
  title={Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase.},
  author={Se{\'a}n E O'Leary and Katherine A Hicks and Steven E. Ealick and Tadhg P Begley},
  journal={Biochemistry},
  year={2009},
  volume={48 14},
  pages={3033-5}
}
The HpxO enzyme from Klebsiella pneumoniae was recently proposed, on the basis of genetic studies, to catalyze the hydroxylation of uric acid to 5-hydroxyisourate as part of the purine catabolic pathway. Its primary sequence suggests that the HpxO catalytic activity depends on a flavin cofactor (FAD), contrasting with all previously studied urate oxidase enzymes, which have no cofactor requirement. Here we demonstrate biochemically that HpxO is an FAD-dependent urate oxidase. Our data are… CONTINUE READING