Reversible binding of zinc in Plasmodium falciparum Sir2: structure and activity of the apoenzyme.

@article{Chakrabarty2010ReversibleBO,
  title={Reversible binding of zinc in Plasmodium falciparum Sir2: structure and activity of the apoenzyme.},
  author={Subhra Prakash Chakrabarty and Hemalatha Balaram},
  journal={Biochimica et biophysica acta},
  year={2010},
  volume={1804 9},
  pages={1743-50}
}
Reversible zinc chelation via thiol groups of cysteines leading to modulation of activity in redox regulated proteins forms a basis for switching on-off of various biochemical processes. Silent information regulator 2 (Sir2), a NAD(+) dependent deacetylase, contains a non-catalytic zinc ion coordinated by thiol groups of cysteines. Using Plasmodium falciparum Sir2 (PfSir2), we have examined the effect of zinc removal on the structure and activity of this enzyme. Our studies show that the enzyme… CONTINUE READING

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