scholarly journals Mode of action of closthioamide: the first member of the polythioamide class of bacterial DNA gyrase inhibitors

2015 ◽  
Vol 70 (9) ◽  
pp. 2576-2588 ◽  
Author(s):  
Alina Iulia Chiriac ◽  
Florian Kloss ◽  
Jonas Krämer ◽  
Cuong Vuong ◽  
Christian Hertweck ◽  
...  
Keyword(s):  
Mode Of Action ◽  
Dna Gyrase ◽  
Bacterial Dna ◽  
Gyrase Inhibitors

scholarly journals An assay for the detection of bacterial DNA gyrase inhibitors.

1993 ◽  
Vol 46 (11) ◽  
pp. 1764-1766 ◽  
Author(s):  
MARCIA S. OSBURNE ◽  
WILLIAM M. MAIESE ◽  
MICHAEL GREENSTEIN
Keyword(s):  
Dna Gyrase ◽  
Bacterial Dna ◽  
Gyrase Inhibitors

Discovering new DNA gyrase inhibitors using machine learning approaches

RSC Advances ◽  
2015 ◽  
Vol 5 (128) ◽  
pp. 105600-105608 ◽  
Author(s):  
Long Li ◽  
Xiu Le ◽  
Ling Wang ◽  
Qiong Gu ◽  
Huihao Zhou ◽  
...  
Keyword(s):  
Machine Learning ◽  
Dna Gyrase ◽  
Learning Approaches ◽  
Bacterial Dna ◽  
Gyrase Inhibitors

Bacterial DNA gyrase is not expressed in eukaryotes.

Testing Potential Gyrase Inhibitors of Bacterial DNA Gyrase: A Comparison of the Supercoiling Inhibition Assay and "Cleavable Complex" Assay

1993 ◽  
Vol 214 (1) ◽  
pp. 313-317 ◽  
Author(s):  
J.F. Barrett ◽  
J.I. Bernstein ◽  
H.M. Krause ◽  
J.J. Hilliard ◽  
K.A. Ohemeng
Keyword(s):  
Dna Gyrase ◽  
Inhibition Assay ◽  
Bacterial Dna ◽  
Gyrase A ◽  
Testing Potential ◽  
Gyrase Inhibitors ◽  
Cleavable Complex

scholarly journals Simocyclinone D8, an Inhibitor of DNA Gyrase with a Novel Mode of Action

2005 ◽  
Vol 49 (3) ◽  
pp. 1093-1100 ◽  
Author(s):  
Ruth H. Flatman ◽  
Alison J. Howells ◽  
Lutz Heide ◽  
Hans-Peter Fiedler ◽  
Anthony Maxwell
Keyword(s):  
Complex Formation ◽  
Dna Gyrase ◽  
Antibacterial Drug ◽  
Binding Studies ◽  
Bacterial Dna ◽  
New Class ◽  
Atpase Reaction ◽  
Cleavage Complex ◽  
Simocyclinone D8 ◽  
Gyrase Inhibitors

ABSTRACT We have characterized the interaction of a new class of antibiotics, simocyclinones, with bacterial DNA gyrase. Even though their structures include an aminocoumarin moiety, a key feature of novobiocin, coumermycin A1, and clorobiocin, which also target gyrase, simocyclinones behave strikingly differently from these compounds. Simocyclinone D8 is a potent inhibitor of gyrase supercoiling, with a 50% inhibitory concentration lower than that of novobiocin. However, it does not competitively inhibit the DNA-independent ATPase reaction of GyrB, which is characteristic of other aminocoumarins. Simocyclinone D8 also inhibits DNA relaxation by gyrase but does not stimulate cleavage complex formation, unlike quinolones, the other major class of gyrase inhibitors; instead, it abrogates both Ca2+- and quinolone-induced cleavage complex formation. Binding studies suggest that simocyclinone D8 interacts with the N-terminal domain of GyrA. Taken together, our results demonstrate that simocyclinones inhibit an early step of the gyrase catalytic cycle by preventing binding of the enzyme to DNA. This is a novel mechanism for a gyrase inhibitor and presents new possibilities for antibacterial drug development.

scholarly journals N-Benzyl-3-sulfonamidopyrrolidines Are a New Class of Bacterial DNA Gyrase Inhibitors

2011 ◽  
Vol 2 (4) ◽  
pp. 289-292 ◽  
Author(s):  
Marie H. Foss ◽  
Katherine A. Hurley ◽  
Nohemy A. Sorto ◽  
Laura L. Lackner ◽  
Kelsey M. Thornton ◽  
...  
Keyword(s):  
Dna Gyrase ◽  
Bacterial Dna ◽  
New Class ◽  
Gyrase Inhibitors

scholarly journals Mode of action of GR122222X, a novel inhibitor of bacterial DNA gyrase.

1996 ◽  
Vol 40 (2) ◽  
pp. 473-476 ◽  
Author(s):  
M Oram ◽  
B Dosanjh ◽  
N A Gormley ◽  
C V Smith ◽  
L M Fisher ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Mode Of Action ◽  
Potent Inhibitor ◽  
Dna Gyrase ◽  
Bacterial Dna ◽  
B Subunit ◽  
Terminal Fragment

GR122222X is a potent inhibitor of the supercoiling reaction of bacterial DNA gyrase. We show that this compound binds stoichiometrically to inactivate the ATPase activity of a 43-kDa N-terminal fragment of the B subunit and competitively inhibits the binding of a radiolabelled coumarin drug to N-terminal fragments of GyrB. These and other data suggest that GR122222X has a mode of action similar, but not identical, to that of coumarin antibiotics.

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