Tyrosinase folding and copper loading in vivo: a crucial role for calnexin and alpha-glucosidase II.

@article{BranzaNichita1999TyrosinaseFA,
  title={Tyrosinase folding and copper loading in vivo: a crucial role for calnexin and alpha-glucosidase II.},
  author={Norica Branza-Nichita and A J Petrescu and Raymond A. Dwek and Mark R Wormald and Frances M Platt and Stefana Maria Petrescu},
  journal={Biochemical and biophysical research communications},
  year={1999},
  volume={261 3},
  pages={720-5}
}
Tyrosinase is the key enzyme of melanin biosynthesis. It is a multiply glycosylated metalloenzyme, which has a long maturation time making it an ideal in vivo model system to probe protein folding and metal loading events. The use of NB-DNJ, an alpha-glucosidase I and II inhibitor has allowed us to dissect these processes. Here we show that tyrosinase folds through several inactive intermediates, at least two of which are recognised by the ER chaperone, calnexin. If the association with… CONTINUE READING

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