Haloemodin as Novel Antibacterial Agent Inhibiting DNA Gyrase and Bacterial Topoisomerase I

2014 ◽  
Vol 57 (9) ◽  
pp. 3707-3714 ◽  
Author(s):  
Feixia Duan ◽  
Xiaohong Li ◽  
Suping Cai ◽  
Guang Xin ◽  
Yanyan Wang ◽  
...  
Keyword(s):  
Antibacterial Agent ◽  
Topoisomerase I ◽  
Dna Gyrase

Prediction Mechanism of Nevadensin as Antibacterial Agent against S. sanguinis: In vitro and In silico Studies

2021 ◽  
Vol 24 ◽  
Author(s):  
Aldina Amalia Nur Shadrina ◽  
Yetty Herdiyati ◽  
Ika Wiani ◽  
Mieke Hemiawati Satari ◽  
Dikdik Kurnia
Keyword(s):  
Antibacterial Activity ◽  
Molecular Docking ◽  
Dental Caries ◽  
Binding Affinity ◽  
In Silico ◽  
Antibacterial Agent ◽  
In Silico Analysis ◽  
Dna Gyrase ◽  
Silico Analysis

Background: Streptococcus sanguinis can contribute to tooth demineralization, which can lead to dental caries. Antibiotics used indefinitely to treat dental caries can lead to bacterial resistance. Discovering new antibacterial agents from natural products like Ocimum basilicum will help combat antibiotic resistance. In silico analysis (molecular docking) can help determine the lead compound by studying the molecular interaction between the drug and the target receptor (MurA enzyme and DNA gyrase). It is a potential candidate for antibacterial drug development. Objective: The research objective is to isolate the secondary metabolite of O. basilicum extract that has activity against S. sanguinis through in vitro and in silico analysis. Methods: n-Hexane extract of O. basilicum was purified by combining column chromatography with bioactivity-guided. The in vitro antibacterial activity against S. sanguinis was determined using the disc diffusion and microdilution method, while molecular docking simulation of nevadensin (1) with MurA enzyme and DNA gyrase was performed used PyRx 0.8 program. Results: Nevadensin from O. basilicum was successfully isolated and characterized by spectroscopic methods. This compound showed antibacterial activity against S. sanguinis with MIC and MBC values of 3750 and 15000 μg/mL, respectively. In silico analysis showed that the binding affinity to MurA was -8.5 Kcal/mol, and the binding affinity to DNA gyrase was -6.7 Kcal/mol. The binding of nevadensin-MurA is greater than fosfomycin-MurA. Otherwise, Nevadensin-DNA gyrase has a weaker binding affinity than fluoroquinolone-DNA gyrase and chlorhexidine-DNA gyrase. Conclusion: Nevadensin showed potential as a new natural antibacterial agent by inhibiting the MurA enzyme rather than DNA gyrase.

scholarly journals Transcription facilitated genome-wide recruitment of topoisomerase I and DNA gyrase

PLoS Genetics ◽  
2017 ◽  
Vol 13 (5) ◽  
pp. e1006754 ◽  
Author(s):  
Wareed Ahmed ◽  
Claudia Sala ◽  
Shubhada R. Hegde ◽  
Rajiv Kumar Jha ◽  
Stewart T. Cole ◽  
...  
Keyword(s):  
Topoisomerase I ◽  
Dna Gyrase ◽  
Genome Wide

Escherichia coli DNA Topoisomerase I Mutants Have Compensatory Mutations at or near DNA Gyrase Genes

1983 ◽  
Vol 47 (0) ◽  
pp. 779-784 ◽  
Author(s):  
S. DiNardo ◽  
K.A. Voelkel ◽  
R. Sternglanz ◽  
A.E. Reynolds ◽  
A. Wright
Keyword(s):  
Escherichia Coli ◽  
Topoisomerase I ◽  
Dna Gyrase ◽  
Dna Topoisomerase I ◽  
Dna Topoisomerase ◽  
Compensatory Mutations

scholarly journals DNA supercoiling in Escherichia coli is under tight and subtle homeostatic control, involving gene-expression and metabolic regulation of both topoisomerase I and DNA gyrase

2002 ◽  
Vol 269 (6) ◽  
pp. 1662-1669 ◽  
Author(s):  
Jacky L. Snoep ◽  
Coen C. van der Weijden ◽  
Heidi W. Andersen ◽  
Hans V. Westerhoff ◽  
Peter Ruhdal Jensen
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Topoisomerase I ◽  
Metabolic Regulation ◽  
Dna Gyrase ◽  
Dna Supercoiling ◽  
Homeostatic Control

scholarly journals Effects of DNA gyrase inhibitors in Escherichia coli topoisomerase I mutants.

1986 ◽  
Vol 168 (1) ◽  
pp. 276-282 ◽  
Author(s):  
G J Pruss ◽  
R J Franco ◽  
S G Chevalier ◽  
S H Manes ◽  
K Drlica
Keyword(s):  
Escherichia Coli ◽  
Topoisomerase I ◽  
Dna Gyrase ◽  
Gyrase Inhibitors

scholarly journals Metabolic Engineering for l-Glutamine Overproduction by Using DNA Gyrase Mutations in Escherichia coli

2013 ◽  
Vol 79 (9) ◽  
pp. 3033-3039 ◽  
Author(s):  
Mikiro Hayashi ◽  
Kazuhiko Tabata
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Topoisomerase I ◽  
Dna Gyrase ◽  
Chromosomal Dna ◽  
Topoisomerase Iv ◽  
Α Subunit ◽  
Content Type ◽  
Genome Wide ◽  
K 12

ABSTRACTAnl-glutamine-overproducing mutant of anEscherichia coliK-12-derived strain was selected from randomly mutagenized cells in the course ofl-alanyl-l-glutamine strain development. Genome-wide mutation analysis unveiled a novel mechanism forl-glutamine overproduction in this mutant. Three mutations were identified that are related to thel-glutamine overproduction phenotype, namely, an intergenic mutation in the 5′-flanking region ofyeiGand two nonsynonymous mutations ingyrA(Gly821Ser and Asp830Asn). Expression ofyeiG, which encodes a putative esterase, was enhanced by the intergenic mutation. The nonsynonymous mutations ingyrA, a gene that encodes the DNA gyrase α subunit, affected the DNA topology of the cells. Gyrase is a type II topoisomerase that adds negative supercoils to double-stranded DNA. When the opposing DNA-relaxing activity was enhanced by overexpressing topoisomerase I (topA) and topoisomerase IV (parCandparE), an increase inl-glutamine production was observed. These results indicate that a reduction of chromosomal DNA supercoils in the mutant caused an increase inl-glutamine accumulation. The mechanism underlying this finding is discussed in this paper. We also constructed anl-glutamine-hyperproducing strain by attenuating cellularl-glutamine degradation activity. Although the reconstituted mutant (withyeiGtogether withgyrA) produced 200 mMl-glutamine, metabolic engineering finally enabled construction of a mutant that accumulated more than 500 mMl-glutamine.

scholarly journals Escherichia coli DNA Topoisomerase I and Suppression of Killing by Tn5 Transposase Overproduction: Topoisomerase I Modulates Tn5 Transposition

1998 ◽  
Vol 180 (22) ◽  
pp. 5866-5874 ◽  
Author(s):  
Hesna Yigit ◽  
William S. Reznikoff
Keyword(s):  
Escherichia Coli ◽  
Chromosome Segregation ◽  
Topoisomerase I ◽  
Dna Gyrase ◽  
Wild Type ◽  
Dna Topoisomerase ◽  
Dna Relaxation ◽  
Tn5 Transposase ◽  
Lines Of Evidence

ABSTRACT Tn5 transposase (Tnp) overproduction is lethal toEscherichia coli. The overproduction causes cell filamentation and abnormal chromosome segregation. Here we present three lines of evidence strongly suggesting that Tnp overproduction killing is due to titration of topoisomerase I. First, a suppressor mutation of transposase overproduction killing, stkD10, is localized in topA (the gene for topoisomerase I). ThestkD10 mutant has the following characteristics: first, it has an increased abundance of topoisomerase I protein, the topoisomerase I is defective for the DNA relaxation activity, and DNA gyrase activity is reduced; second, the suppressor phenotype of a second mutation localized in rpoH, stkA14 (H. Yigit and W. S. Reznikoff, J. Bacteriol. 179:1704–1713, 1997), can be explained by an increase in topA expression; and third, overexpression of wild-type topA partially suppresses the killing. Finally, topoisomerase I was found to enhance Tn5 transposition up to 30-fold in vivo.

Novel Benzotriazole acetamide derivatives as Benzo-Fused Five-Membered Nitrogen-Containing Heterocycle- Insilico Screening, Molecular Docking, and Synthesis

2021 ◽  
Vol 18 ◽  
Author(s):  
Patil Tejaswini D. ◽  
Amrutkar Sunil V.
Keyword(s):  
Staphylococcus Aureus ◽  
Molecular Docking ◽  
Active Site ◽  
Antibacterial Agent ◽  
Antibacterial Properties ◽  
Dna Gyrase ◽  
Antibacterial Drug ◽  
E Coli ◽  
Fast Development ◽  
Subunit B

Background: DNA gyrase subunit B (1KZN) is an attractive target for antibacterial drug development because of its role in DNA replication. The fast development of antimicrobial medication resistance necessitates the quick discovery of new antimicrobial medicines. Objective: The goal of this research is to design, synthesize, and discover benzo-fused five-membered nitrogen-containing heterocycles that bind to DNA gyrase subunit B via molecular docking (1KZN). Methods: Based on literature research, 2-(1H-1,2,3-Benzotriazol-1-yl)-N-substituted acetamide was synthesized using an efficient method. All synthesized compounds were evaluated for antibacterial activity against three distinct organisms: E. coli, Pseudomonas aeruginosa, Staphylococcus aureus. In a docking investigation, the chemical interacts with the active site of DNA gyrase subunit B (1KZN), indicating that it might have antibacterial action. Conclusion: According to the findings of this research, the compounds 3d and 3f show antibacterial properties. For Staphylococcus aureus, 3c has the potential to be an antibacterial agent.

gyrB-225, a mutation of DNA gyrase that compensates for topoisomerase I deficiency: investigation of its low activity and quinolone hypersensitivity

2001 ◽  
Vol 309 (5) ◽  
pp. 1219-1231 ◽  
Author(s):  
Jonathan G Heddle ◽  
Tao Lu ◽  
Xilin Zhao ◽  
Karl Drlica ◽  
Anthony Maxwell
Keyword(s):  
Topoisomerase I ◽  
Dna Gyrase ◽  
Low Activity
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