Active substances: Ciprofloxacin
Furthermore, the pharmacokinetics of levofloxacin are advantageous compared to those of other members of the drug class, and treatment requires only a single pill per day.
Gyrase and topoisomerase IV modulate the topological state of DNA by passing an intact double helix through a transient double-stranded break that they generate in a separate segment of DNA.
Progression through the catalytic cycle is driven by ATP binding and hydrolysis. Despite their mechanistic and structural similarities, gyrase and topoisomerase IV have separate physiological functions.
In addition, gyrase is primarily responsible for removing the torsional stress that accumulates in front of replication forks and transcription complexes. Its major function is removing knots that accumulate in the bacterial chromosome as a result of fundamental cellular processes and decatenating daughter chromosomes following replication.
GyrA and the equivalent topoisomerase IV subunit contains the active site tyrosine residue. Despite the strong sequence similarity between gyrase and topoisomerase IV, the C-termini of the A subunits are not well conserved. This portion of the protein is involved in topology recognition and allows gyrase, but not topoisomerase IV, to generate supercoils in DNA.
Domain structures of type II topoisomerases. Gyrase and topoisomerase IV are heterotetrameric enzymes consisting of two A subunits and two B subunits.
However, during the course of evolution, the A and B subunits fused into a single polypeptide chain. Therefore, eukaryotic type II topoisomerases function as homodimers.
A representation of the three-dimensional structure of type II topoisomerases is shown at the bottom.
However, during the course of evolution, the genes encoding the A and B subunits have fused, resulting in a single polypeptide chain Figure 2. Stop aches and pains before they start with Aleve!
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