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Synonyms
atpase, topoisomerase ii, dna gyrase, topo ii, gyrase, top2a, dna topoisomerase ii, topoisomerase iialpha, topo iialpha, topoisomerase ii alpha,
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ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
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ATP + supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
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network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
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decatenation
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supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
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relaxation
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additional information
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supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
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supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
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catenation
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additional information
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for DNA cleavage, the correct positioning of the catalytic tyrosine on the CAP domain with respect to the topoisomerase/primase domain seems to be achieved by a rigid body-domain movement, catalytic mechanism and role of the metal-binding TOPRIM domains in catalysis, overview
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additional information
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for DNA cleavage, the correct positioning of the catalytic tyrosine on the CAP domain with respect to the topoisomerase/primase domain seems to be achieved by a rigid body-domain movement, catalytic mechanism and role of the metal-binding TOPRIM domains in catalysis, overview
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additional information
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for DNA cleavage, the correct positioning of the catalytic tyrosine on the CAP domain with respect to the topoisomerase/primase domain seems to be achieved by a rigid body-domain movement, catalytic mechanism and role of the metal-binding TOPRIM domains in catalysis, overview
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(2R)-2-[(5Z)-5-[[3-(4-fluorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-4-oxo-5-[(3-[[(2Z)-3-phenylprop-2-en-1-yl]oxy]phenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-([3-[(3,4-dichlorophenyl)methyl]phenyl]methylidene)-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[(3',4'-dichloro[1,1'-biphenyl]-3-yl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[(3-benzoylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[(3-benzylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[([1,1'-biphenyl]-3-yl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[[3-(3-chlorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2R)-2-[(5Z)-5-[[3-(4-fluorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-4-oxo-5-[(3-[[(2Z)-3-phenylprop-2-en-1-yl]oxy]phenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-([3-[(3,4-dichlorophenyl)methyl]phenyl]methylidene)-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[(3',4'-dichloro[1,1'-biphenyl]-3-yl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[(3-benzoylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[(3-benzylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[([1,1'-biphenyl]-3-yl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[[3-(3-chlorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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(2S)-2-[(5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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1-(4-nitrobenzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
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3-acetyl-2-(4-methoxyphenyl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole
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3-chloro-4-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] azetidin-2-one
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4-chloro-5-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one
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6-methoxy-4-(2-[4-[([1,3]oxathiolo[5,4-c]pyridin-6-ylmethyl)amino]piperidin-1-yl]ethyl)quinoline-3-carbonitrile
i.e. GSK299423, it shows potent inhibition of supercoiling by DNA gyrase, enzyme binding mode and structure, overview. The inhibitor bridges the DNA and a transient non-catalytic pocket on the 2fold axis at the GyrA dimer interface, and is close to the active sites and luoroquinolone binding sites. In the inhibitor complex the active site seems poised to cleave the DNA, with a single metal ion observed between the topoisomerase/primase domain and the scissile phosphate
ABT-719
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i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000015 mg/ml for strain CiproS, 0.00025 mg/ml for strain CiproR, and 0.001 mg/ml for the methicillin-resistant strain
clinafloxacin
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MIC90 is 0.00003 mg/ml for strain CiproS, 0.001 mg/ml for strain CiproR, and 0.001 mg/ml for the methicillin-resistant strain
sparfloxacin
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MIC90 is 0.00006 mg/ml for strain CiproS, 0.016 mg/ml for strain CiproR, and 0.008 mg/ml for the methicillin-resistant strain
y, Namen korrigieren: 4-chloro-5-(furan-2-yl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one
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additional information
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not inhibited by 1-(benzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide, 3-chloro-4-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]azetidin-2-one, 4-chloro-5-(4-chlorophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 4-chloro-5-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 3-acetyl-2-(furan-2-yl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, 2-(furan-2-yl)-3-[2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxyacetamido]-thiazolidin-4-one, and amphotericin B
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Ciprofloxacin
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MIC90 is 0.0005 mg/ml for strain CiproS, 0.064 mg/ml for strain CiproR, and 0.128 mg/ml for the methicillin-resistant strain
Ciprofloxacin
a fluoroquinolone, enzyme binding mode and structure, overview
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Y123F
site-directed mutagenesis, the Tyr123Phe construct stabilizes a homogenous pre-cleavage conformation trapped by the inhibitor, with a construct that is otherwise demonstrated to be cleavage competent
additional information
the small, flexible Greek key or tail domain, residues 544-579, in the GyrB subunit, which does not make contact with the DNA in the crystal structure at 3.5 A resolution, is deleted and replaced with two amino acids to give a GyrB27-A56(GKdel/Tyr123Phe) construct, crystal structure with bound gyrase. The recombinant construct improves the resolution of the crystal in X-ray diffraction, overview
additional information
the small, flexible Greek key or tail domain, residues 544-579, in the GyrB subunit, which does not make contact with the DNA in the crystal structure at 3.5 A resolution, is deleted and replaced with two amino acids to give a GyrB27-A56(GKdel/Tyr123Phe) construct, crystal structure with bound gyrase. The recombinant construct improves the resolution of the crystal in X-ray diffraction, overview
additional information
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the small, flexible Greek key or tail domain, residues 544-579, in the GyrB subunit, which does not make contact with the DNA in the crystal structure at 3.5 A resolution, is deleted and replaced with two amino acids to give a GyrB27-A56(GKdel/Tyr123Phe) construct, crystal structure with bound gyrase. The recombinant construct improves the resolution of the crystal in X-ray diffraction, overview
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Sutcliffe, J.A.; Gootz, T.D.; Barrett, J.F.
Biochemical characteristics and physiological significance of major DNA topoisomerases
Antimicrob. Agents Chemother.
33
2027-2033
1989
Bacillus subtilis, Bacteria, Citrobacter freundii, Drosophila melanogaster, Escherichia coli, eukaryota, Micrococcus luteus, Staphylococcus aureus, Pseudomonas aeruginosa, Streptomyces niveus
brenda
Flamm, R.K.; Vojtko, C.; Chu, D.T.; Li, Q.; Beyer, J.; Hensey, D.; Ramer, N.; Clement, J.J.; Tanaka, S.K.
In vitro evaluation of ABT-719, a novel DNA gyrase inhibitor
Antimicrob. Agents Chemother.
39
964-970
1995
Acinetobacter calcoaceticus, Bacteroides thetaiotaomicron, Bacteroides fragilis, Moraxella catarrhalis, Citrobacter freundii, Clostridioides difficile, Clostridium perfringens, Corynebacterium sp., Streptococcus pneumoniae, Escherichia coli, Enterococcus faecium, Haemophilus influenzae, Klebsiella sp., Listeria monocytogenes, Staphylococcus aureus, Morganella morganii, Mycobacterium avium, Neisseria gonorrhoeae, Proteus mirabilis, Providencia rettgeri, Providencia stuartii, Pseudomonas aeruginosa, Salmonella sp., Serratia marcescens, Shigella sp., Staphylococcus epidermidis, Streptococcus agalactiae, Streptococcus pyogenes, Enterococcus sp., Streptococcus viridans, Citrobacter spp., Legionella sp., Prevotella bivia, Peptostreptococcus sp., Staphylococcus aureus CiproS, Pseudomonas aeruginosa AC1679-1682
brenda
Carr, S.B.; Makris, G.; Phillips, S.E.; Thomas, C.D.
Crystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus
Acta Crystallogr. Sect. F
62
1164-1167
2006
Staphylococcus aureus (Q6G9K4), Staphylococcus aureus
brenda
Hassan, G.S.; Farag, N.A.; Hegazy, G.H.; Arafa, R.K.
Design and synthesis of novel benzopyran-2-one derivatives of expected antimicrobial activity through DNA gyrase-B inhibition
Arch. Pharm.
341
725-733
2008
Bacillus subtilis, Candida albicans, Micrococcus luteus, Staphylococcus aureus, Escherichia coli (P0AES6)
brenda
Bax, B.D.; Chan, P.F.; Eggleston, D.S.; Fosberry, A.; Gentry, D.R.; Gorrec, F.; Giordano, I.; Hann, M.M.; Hennessy, A.; Hibbs, M.; Huang, J.; Jones, E.; Jones, J.; Brown, K.K.; Lewis, C.J.; May, E.W.; Saunders, M.R.; Singh, O.; Spitzfaden, C.E.; Shen, C.; Shillings, A.; Theobald, A.J.; Wohlkonig, A.; Pearson, N.D.
Type IIA topoisomerase inhibition by a new class of antibacterial agents
Nature
466
935-940
2010
Staphylococcus aureus (P66937), Staphylococcus aureus (Q99XG5), Staphylococcus aureus
brenda
Werner, M.M.; Patel, B.A.; Talele, T.T.; Ashby, C.R.; Li, Z.; Zauhar, R.J.
Dual inhibition of Staphylococcus aureus DNA gyrase and topoisomerase IV activity by phenylalanine-derived (Z)-5-arylmethylidene rhodanines
Bioorg. Med. Chem.
23
6125-6137
2015
Staphylococcus aureus, Staphylococcus aureus (P0A0K8)
brenda