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

Pub. Date : 2002 Sep 1

PMID : 12176051






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 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. Disulfides quiescin sulfhydryl oxidase 1 Homo sapiens
2 Mixtures of avian QSOX and protein disulfide isomerase catalyze the rapid insertion of the correct disulfide pairings in reduced RNase. Disulfides quiescin sulfhydryl oxidase 1 Homo sapiens
3 Consistent with this role in the formation of disulfide bonds, QSOX is typically found in the cell in the endoplasmic reticulum and Golgi and outside the cell. Disulfides quiescin sulfhydryl oxidase 1 Homo sapiens