Fluoroquinolones stimulate the DNA cleavage activity of topoisomerase IV by promoting the binding of Mg(2+) to the second metal binding site.

Citation data:

Biochimica et biophysica acta, ISSN: 0006-3002, Vol: 1860, Issue: 3, Page: 569-75

Publication Year:
2016
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PMID:
26723176
DOI:
10.1016/j.bbagen.2015.12.019
PMCID:
PMC4720527
Author(s):
Oppegard, Lisa M, Schwanz, Heidi A, Towle, Tyrell R, Kerns, Robert J, Hiasa, Hiroshi
Publisher(s):
Elsevier BV
Tags:
Biochemistry, Genetics and Molecular Biology
article description
Fluoroquinolones target bacterial type IIA topoisomerases, DNA gyrase and topoisomerase IV (Topo IV). Fluoroquinolones trap a topoisomerase-DNA covalent complex as a topoisomerase-fluoroquinolone-DNA ternary complex and ternary complex formation is critical for their cytotoxicity. A divalent metal ion is required for type IIA topoisomerase-catalyzed strand breakage and religation reactions. Recent studies have suggested that type IIA topoisomerases use two metal ions, one structural and one catalytic, to carry out the strand breakage reaction.

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