Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors.

@article{Truppo2012CarbonicAV,
  title={Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors.},
  author={Emanuela Truppo and Claudiu T. Supuran and Annamaria Sandomenico and Daniela Vullo and Alessio Innocenti and Anna Di Fiore and Vincenzo Alterio and Giuseppina De Simone and Simona Maria Monti},
  journal={Bioorganic & medicinal chemistry letters},
  year={2012},
  volume={22 4},
  pages={1560-4}
}
Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic isoform. Cys183 and Cys217 were found to be the residues involved in reaction with glutathione for hCA VII. The two reactive cysteines were then mutated and the corresponding variant (C183S/C217S) expressed. The native enzyme, the variant and the S… CONTINUE READING