Dimerization of thiol-specific antioxidant and the essential role of cysteine 47.

@article{Chae1994DimerizationOT,
  title={Dimerization of thiol-specific antioxidant and the essential role of cysteine 47.},
  author={Ho Zoon Chae and Taewoong Uhm and Sue Goo Rhee},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 15},
  pages={7022-6}
}
Thiol-specific antioxidant (TSA) from yeast contains cysteine residues at amino acid positions 47 and 170 but is not associated with obvious redox cofactors. These two cysteines are highly conserved in a family of proteins that exhibit sequence identity of 23-98% with TSA. The roles of Cys-47 and Cys-170 in yeast TSA were investigated by replacing them individually with serine and expressing the mutant TSA proteins (RC47S and RC170S, respectively), as well as wild-type TSA (RWT), in Escherichia… CONTINUE READING

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