Corpus ID: 31665633

Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis.

@article{Cacciapuoti2003PurificationAC,
  title={Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis.},
  author={G. Cacciapuoti and C. Bertoldo and A. Brio and V. Zappia and M. Porcelli},
  journal={Extremophiles : life under extreme conditions},
  year={2003},
  volume={7 2},
  pages={
          159-68
        }
}
  • G. Cacciapuoti, C. Bertoldo, +2 authors M. Porcelli
  • Published 2003
  • Medicine
  • Extremophiles : life under extreme conditions
  • 5'-Methylthioadenosine phosphorylase (MTAP) was purified to homogeneity from the hyperthermophilic archaeon Pyrococcus furiosus. The protein is a homoexamer of 180 kDa. The enzyme is highly thermoactive, with an optimum temperature of 125 degrees C, and extremely thermostable, retaining 98% residual activity after 5 h at 100 degrees C and showing a half-life of 43 min at 130 degrees C. In the presence of 100 mM phosphate, the apparent T(m) (137 degrees C) increases to 139 degrees C. The enzyme… CONTINUE READING
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