Uracil phosphoribosyltransferase from the extreme thermoacidophilic archaebacterium Sulfolobus shibatae is an allosteric enzyme, activated by GTP and inhibited by CTP.

@article{Linde1996UracilPF,
  title={Uracil phosphoribosyltransferase from the extreme thermoacidophilic archaebacterium Sulfolobus shibatae is an allosteric enzyme, activated by GTP and inhibited by CTP.},
  author={Louis P. Linde and Kaj Jensen},
  journal={Biochimica et biophysica acta},
  year={1996},
  volume={1296 1},
  pages={16-22}
}
Uracil phosphoribosyltransferase, which catalyses the formation of UMP and pyrophosphate from uracil and 5-phosphoribosyl alpha-1-pyrophosphate (PRPP), was partly purified from the extreme thermophilic archaebacterium Sulfolobus shibatae. The enzyme required divalent metal ions for activity and it showed the highest activity at pH 6.4. The specific activity of the enzyme was 50-times higher at 95 degrees C than at 37 degrees C, but the functional half-life was short at 95 degrees C. The… CONTINUE READING

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