Article
Characterization of the ATPase activity of topoisomerase II from Leishmania donovani and identification of residues conferring resistance to etoposide.
The Biochemical journal - 1 Sept 2005
Sengupta Tanushri, Mukherjee Mandira, Das Aditi, Mandal Chhabinath, Das Rakhee, Mukherjee Tanmoy, Majumder Hemanta K
Abstract excerpt
We have cloned and expressed the 43 kDa N-terminal domain of Leishmania donovani topoisomerase II. This protein has an intrinsic ATPase activity and obeys Michaelis-Menten kinetics. Cross-linking studies indicate that the N-terminal domain exists as a dimer both in the presence and absence of nucleotides. Etoposide, an effective antitumour drug, traps eukaryotic DNA topoisomerase II in a covalent complex with...
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