Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.2.2 extracted from

  • Furet, P.; Schoepfer, J.; Radimerski, T.; Chene, P.
    Discovery of a new class of catalytic topoisomerase II inhibitors targeting the ATP-binding site by structure based design. Part I (2009), Bioorg. Med. Chem. Lett., 19, 4014-4017.
    View publication on PubMed
Search for more literature for 5.6.2.2

Inhibitors

Inhibitors Comment Organism Structure
N2-(1,3-benzothiazol-6-yl)-N6-cyclohexyl-9H-purine-2,6-diamine
-
 Homo sapiens
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-9H-purine-2,6-diamine
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Homo sapiens 5634
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structure-activity relationship, structure modelling and modelling of ligand docking in the ATP binding pocket, binding mechanism, overview Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
More topoisomerase II is an ATPase belonging to the GHKL family Homo sapiens
Topoisomerase II
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP modelling of ligand docking in the ATP binding pocket, involves e.g. Asn91, a residue absolutely conserved in the GHKL ATPase family, binding mechanism, overview Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0017
-
-
 Homo sapiens N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-9H-purine-2,6-diamine
0.0084
-
-
 Homo sapiens N2-(1,3-benzothiazol-6-yl)-N6-cyclohexyl-9H-purine-2,6-diamine