QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.

@article{Alon2010QSOXCA,
  title={QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.},
  author={Assaf Alon and Erin J. Heckler and Colin Thorpe and Deborah Fass},
  journal={FEBS letters},
  year={2010},
  volume={584 8},
  pages={1521-5}
}
Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins. Human QSOX1 is a multi-domain, monomeric enzyme containing a module related to the single-domain sulfhydryl oxidases of the Erv family. A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes. However, one pseudo-dimer "subunit" has lost its cofactor and catalytic activity. In QSOX evolution, a further… CONTINUE READING

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