Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes.

@article{Thorpe2002SulfhydrylOE,
  title={Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes.},
  author={Colin Thorpe and Karen L Hoober and Sonali Raje and Nicole M. Glynn and Joan Burnside and George K. Turi and Donald L Coppock},
  journal={Archives of biochemistry and biophysics},
  year={2002},
  volume={405 1},
  pages={1-12}
}
Members of the Quiescin-sulfhydryl oxidase (QSOX) family utilize a thioredoxin domain and a small FAD-binding domain homologous to the yeast ERV1p protein to oxidize sulfhydryl groups to disulfides with the reduction of oxygen to hydrogen peroxide. QSOX enzymes are found in all multicellular organisms for which complete genomes exist and in Trypanosoma brucei, but are not found in yeast. The avian QSOX is the best understood enzymatically: its preferred substrates are peptides and proteins, not… CONTINUE READING