Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase.

@article{Delvaux2013StructuralDO,
  title={Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase.},
  author={David Delvaux and Fr{\'e}d{\'e}ric Kerff and M. S. R. Murty and Bernard Lakaye and Jan Czerniecki and Gregory M. Kohn and Pierre Wins and Rapha{\"e}l Herman and Val{\'e}rie Gabelica and Fabien Heuze and Xavier Tordoir and Rapha{\"e}l Mar{\'e}e and Andr{\'e} Matagne and Paulette Charlier and Edwin De Pauw and Lucien Bettendorff},
  journal={Biochimica et biophysica acta},
  year={2013},
  volume={1830 10},
  pages={
          4513-23
        }
}
BACKGROUND Thiamine triphosphate (ThTP) is present in most organisms and might be involved in intracellular signaling. In mammalian cells, the cytosolic ThTP level is controlled by a specific thiamine triphosphatase (ThTPase), belonging to the CYTH superfamily of proteins. CYTH proteins are present in all superkingdoms of life and act on various triphosphorylated substrates. METHODS Using crystallography, mass spectrometry and mutational analysis, we identified the key structural determinants… CONTINUE READING
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