Steps in reductive activation of the disulfide-generating enzyme Ero1p.

@article{Heldman2010StepsIR,
  title={Steps in reductive activation of the disulfide-generating enzyme Ero1p.},
  author={Nimrod Heldman and Ohad Vonshak and Carolyn S Sevier and Elvira Vitu and Tevie Mehlman and Deborah Fass},
  journal={Protein science : a publication of the Protein Society},
  year={2010},
  volume={19 10},
  pages={1863-76}
}
Ero1p is the primary catalyst of disulfide bond formation in the yeast endoplasmic reticulum (ER). Ero1p contains a pair of essential disulfide bonds that participate directly in the electron transfer pathway from substrate thiol groups to oxygen. Remarkably, elimination of certain other Ero1p disulfides by mutation enhances enzyme activity. In particular, the C150A/C295A Ero1p mutant exhibits increased thiol oxidation in vitro and in vivo and interferes with redox homeostasis in yeast cells by… CONTINUE READING
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