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Literature summary extracted from

  • Singh, G.; Thakur, M.; Chakraborti, P.K.; Dey, C.S.
    Evidence for the presence of R250G mutation at the ATPase domain of topoisomerase II in an arsenite-resistant Leishmania donovani exhibiting a differential drug inhibition profile (2009), Int. J. Antimicrob. Agents, 33, 80-85.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.6.2.2 R250G point mutation in the ATPase domain of topo II leading to arsenite resistance Leishmania donovani

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.6.2.2 actinomycin D
-
 Leishmania donovani
5.6.2.2 arsenite
-
 Leishmania donovani
5.6.2.2 doxorubicin
-
 Leishmania donovani
5.6.2.2 novobiocin
-
 Leishmania donovani
5.6.2.2 Pentamidine
-
 Leishmania donovani

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.2 Leishmania donovani Q9XZN0
-
-
5.6.2.2 Leishmania donovani MHOM/80/IN/Dd8 Q9XZN0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.2.2 partially purified Leishmania donovani

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.2 supercoiled DNA + ATP + H2O
-
 Leishmania donovani catenated DNA networks + ADP + phosphate
-
 ?
5.6.2.2 supercoiled DNA + ATP + H2O
-
 Leishmania donovani MHOM/80/IN/Dd8 catenated DNA networks + ADP + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.6.2.2 topo II
-
 Leishmania donovani
5.6.2.2 Topoisomerase II
-
 Leishmania donovani

Cofactor

EC Number Cofactor Comment Organism Structure
5.6.2.2 ATP
-
 Leishmania donovani