Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).

@article{Arunachalam2000EnzymaticRO,
  title={Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).},
  author={B. Arunachalam and U. Phan and H. Geuze and P. Cresswell},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 2},
  pages={
          745-50
        }
}
Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin, but the mechanism of lysosomal reduction is unknown. We describe here a lysosomal thiol reductase optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. The active site… Expand
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Molecular cloning and expression analysis of interferon-γ-inducible-lysosomal thiol reductase gene in orange-spotted grouper, Epinephelus coioides
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