DNA topoisomerase 4 subunit B (ParE)

DNA topoisomerase 4 subunit B (ParE) is an essential bacterial enzyme subunit, forming part of the heterotetrameric topoisomerase IV complex alongside ParC. It is a type II topoisomerase that utilizes ATP hydrolysis (the ATPase activity resides in ParE) to drive the passage of one DNA double helix through another, a process critical for resolving intertwined (catenated) daughter chromosomes following DNA replication. This allows for proper segregation of chromosomes during bacterial cell division. ParE is functionally and structurally similar to the GyrB subunit of DNA gyrase, though topoisomerase IV (ParC/ParE) primarily decatenates DNA rather than introducing negative supercoils. It is the principal target for several clinically important antibiotics, including fluoroquinolones such as ciprofloxacin and the coumarin antibiotic novobiocin, which target its ATP binding site or stabilize intermediate cleavage complexes[1][2][4][5][6]. Resistance mutations in ParE can significantly affect drug potency, and its inhibition is a validated antibacterial strategy.

Other names

Topoisomerase IV subunit ParETopoisomerase IV subunit BparEnfxD

ATPase inhibitors, Topoisomerase II inhibitors, Blocking ATP binding/hydrolysis, Stabilization of DNA-topoisomerase cleavage complexes