Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization.

@article{Renosto1984Adenosine5K,
  title={Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization.},
  author={Franco Renosto and Peter Seubert and Irwin H. Segel},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 4},
  pages={
          2113-23
        }
}
Adenosine 5'-phosphosulfate (APS) kinase, the second enzyme in the pathway of inorganic sulfate assimilation, was purified to near homogeneity from mycelium of the filamentous fungus, Penicillium chrysogenum. The enzyme has a native molecular weight of 59,000-60,000 and is composed of two 30,000-dalton subunits. At 30 degrees C, pH 8.0 (0.1 M Tris-chloride buffer), 5.5 microM APS, 5 mM MgATP, 5 mM excess MgCl2, and "high" salt (70-150 mM (NH4)2SO4), the most highly purified preparation has a… CONTINUE READING

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