Structure/function analysis of a critical disulfide bond in the active site of l-xylulose reductase

@article{Zhao2009StructurefunctionAO,
  title={Structure/function analysis of a critical disulfide bond in the active site of l-xylulose reductase},
  author={H.-T. Zhao and Shinya Endo and Syuhei Ishikura and Roland P-T Chung and Philip J Hogg and Akira Hara and Ossama El-Kabbani},
  journal={Cellular and Molecular Life Sciences},
  year={2009},
  volume={66},
  pages={1570-1579}
}
l-Xylulose reductase (XR) is involved in water re-absorption and cellular osmoregulation. The crystal structure of human XR complemented with site-directed mutagenesis (Cys138Ala) indicated that the disulfide bond in the active site between Cys138 and Cys150 is unstable and may affect the reactivity of the enzyme. The effects of reducing agents on the activities of the wild-type and mutant enzymes indicated the reversibility of disulfide-bond formation, which resulted in three-fold decrease in… CONTINUE READING

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