Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae.

@article{Brevet1991IsolationAC,
  title={Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae.},
  author={A. Brevet and J. Chen and M. Fromant and S. Blanquet and P. Plateau},
  journal={Journal of bacteriology},
  year={1991},
  volume={173 17},
  pages={
          5275-9
        }
}
An enzyme able to cleave dinucleoside triphosphates has been purified 3,750-fold from Saccharomyces cerevisiae. Contrary to the enzymes previously shown to catabolize Ap4A in yeast, this enzyme is a hydrolase rather than a phosphorylase. The dinucleoside triphosphatase molecular ratio estimated by gel filtration is 55,000. Dinucleoside triphosphatase activity is strongly stimulated by the presence of divalent cations. Mn2+ displays the strongest stimulating effect, followed by Mg2+, Co2+, Cd2… Expand
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