DNA gyrase gene in Neisseria gonorrhoeae as indicator for resistance to ciprofloxacin and species verification.
(1a) have E-value of -268.36 Kcal/mol for
DNA gyrase, showed hydrogen bonds through Glu139, Arg176, and non-bonding interactions through His150, Phe160, Tyr141, Try76, Glu72, Lys73 and Trp76, while (2b) have E-value of -322.89 Kcal/mol for
DNA gyrase, showing hydrogen bonding through Asn54, and non-bonding interactions through Glu58, Gly85, Arg144, Arg84, Pro87, IIe86, IIe102, IIe51, Glu50, Val130, Val131, Ser128, Ser131.
Synthesis, Characterization, Antioxidant, Antimicrobial, Cytotoxic, Anticancer, Leishmanicidal, Anti-inflammatory Activities and Docking Studies of Heterocyclic 1,3,4-oxadiazoles and 4-amino-1,2,4-triazoles Derivatives Delarue et al., "Structural insights into the quinolone resistance mechanism of Mycobacterium tuberculosis
DNA gyrase," PLoS ONE, vol.
High-level fluoroquinolone resistance in Pseudomonas aeruginosa due to interplay of the MexAB-OprM efflux pump and the
DNA gyrase mutation.
Fluoroquinolone resistance is caused mainly by chromosomal mutations in the quinolone resistance-determining region (QRDR) of gyrA and gyrB, which encode
DNA gyrase subunits, and parC and parE, which encode topoisomerase IV subunits (9).
The results of
DNA gyrase sensitivity testing of this mutant revealed that the development of fluoroquinolone resistance is not the result of mutation in
DNA gyrase.
The superhelical state of intracellular DNA is regulated by the actions of
DNA gyrase and topoisomerase I, which removes DNA super helical twists but is not inhibited by quinolones.
Renaudin, "Alterations in topoisomerase IV and
DNA gyrase in quinolone-resistant mutants of Mycoplasma hominis obtained in vitro," Antimicrobial Agents and Chemotherapy, vol.
Whitehead et al., "Clinically relevant mutant
DNA gyrase alters supercoiling, changes the transcriptome, and confers multidrug resistance," mBio, vol.
The compound under research, diospyrin, binds to a novel site on a well-known enzyme, called
DNA gyrase, and inactivates the enzyme.
Pernet, "Mechanism of inhibition of
DNA gyrase by quinolone antibacterials: specificity and cooperativity of drug binding to DNA," Biochemistry, vol.
Reduced susceptibility to the fluoroquinolones group of antibiotics is usually linked with point mutations in the bacterial target genes gyrA, gyrB encoding
DNA gyrase and/or parC, parE encoding DNA topoisomerase IV.
