Penicillin-binding proteins and induction of AmpC beta-lactamase

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Penicillin-binding proteins and induction of AmpC beta-lactamase.

In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in diminished inducibility. This suggests that if PBPs are involved in induction of AmpC beta-lactamase, there is probably a redundancy in function among the different PBPs.

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Induction of beta-lactamase and penicillin-binding proteins in Escherichia coli by introduction of Streptomyces DNA.

Introduction of hybrid plasmids, which were constructed by ligation of pCR1 or pMN1 vector plasmid and SalI restriction endonuclease cleaved segments of Streptomyces cacaoi chromosome, resulted in the production of new beta-lactamase and penicillin-binding protein in Escherichia coli. The beta-lactamase and penicillin-binding protein were not from S. cacaoi but rather induced by the plasmids. C...

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Role of penicillin-binding proteins in the initiation of the AmpC beta-lactamase expression in Enterobacter cloacae.

Penicillin-binding proteins (PBPs) are involved in the regulation of beta-lactamase expression by determining the level of anhydromuramylpeptides in the periplasmatic space. It was hypothesized that one or more PBPs act as a sensor in the beta-lactamase induction pathway. We have performed induction studies with Escherichia coli mutants lacking one to four PBPs with DD-carboxypeptidase activity...

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Role of Low-Molecular-Mass Penicillin-Binding Proteins, NagZ and AmpR in AmpC β-lactamase Regulation of Yersinia enterocolitica

Yersinia enterocolitica encodes a chromosomal AmpC β-lactamase under the regulation of the classical ampR-ampC system. To obtain a further understanding to the role of low-molecular-mass penicillin-binding proteins (LMM PBPs) including PBP4, PBP5, PBP6, and PBP7, as well as NagZ and AmpR in ampC regulation of Y. enterocolitica, series of single/multiple mutant strains were systematically constr...

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The deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution.

Beta-lactamases confer bacterial resistance to beta-lactam antibiotics, such as penicillins. The characteristic class C beta-lactamase AmpC catalyzes the reaction with several key residues including Ser64, Tyr150, and Lys67. Here, we describe a 1.07 A X-ray crystallographic structure of AmpC beta-lactamase in complex with a boronic acid deacylation transition-state analogue. The high quality of...

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ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 1997

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.41.9.2013