The kinetic properties of the carboxy terminal domain of the Bacillus licheniformis 749/I BlaR penicillin-receptor shed a new light on the derepression of β-lactamase synthesis-Reference-Cited by-同舟云学术

The kinetic properties of the carboxy terminal domain of the Bacillus licheniformis 749/I BlaR penicillin-receptor shed a new light on the derepression of β-lactamase synthesis

Published:2003-05-19 Issue:6 Volume:48 Page:1553-1564
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:

Author:

Duval Valérie,Swinnen Marc,Lepage Sophie,Brans Alain,Granier Benoît,Franssen Christine,Frère Jean-Marie,Joris Bernard

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.2003.03520.x/fullpdf

Reference28 articles.

1. Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose;Cartwright;Biochem J,1984

2. The fate of BlaI repressor during the induction of the Bacillus licheniformis BlaP β-lactamase;Filée;Mol Microbiol,2002

3. Beta-lactamase and bacterial resistance to antibiotics;Frère;Mol Microbiol,1995

4. Mode of action: interaction with the penicillin binding proteins

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