Quinolone-Resistant E. Coli Mutants Overproduce a 60 kDa Protein Highly Homologous to GroEL View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1990

AUTHORS

P. Hallett , A. Mehlert , A. Maxwell

ABSTRACT

DNA gyrase is a member of a group of enzymes known as topoisomerases which are responsible for the control and modification of the topological state of DNA in vivo. E. coli DNA gyrase is composed of two A subunits and two B subunits of molecular masses 97 kDa and 90 kDa, coded for by the gyrA and gyrB genes respectively. DNA gyrase has been established as the likely target of the quinolone group of synthetic antibacterial drugs, which include nalidixic acid (NAL), oxolinic acid (OXO), norfloxacin (NFX) and ciprofloxacin (CFX). The quinolones have been found to be particularly useful in the treatment of urinary tract and enteric infections. Due to their success, there has been an extensive search for derivatives with broader spectra of bactericidal activities and improved pharmacological properties. Although it was previously thought that quinolone drugs bind to the A subunit, mutants conferring quinolone resistance have been mapped to both the gyrA and gyrB genes (Yamagishi et al. 1986; Yoshida et al. 1988). Other evidence has suggested that the drugs may preferentially bind to the gyrase-DNA complex (Shen et al. 1989). More... »

PAGES

269-273

Book

TITLE

The 4-Quinolones: Anti Bacterial Agents in Vitro

ISBN

978-1-4471-3451-0
978-1-4471-3449-7

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4471-3449-7_19

DOI

http://dx.doi.org/10.1007/978-1-4471-3449-7_19

DIMENSIONS

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