Interaction of the novel penem CGP 31 608 and Its enantiomer with type Id beta-lactamase and penicillin-binding proteins

1987 ◽  
Vol 6 (6) ◽  
pp. 674-678 ◽  
Author(s):  
H. Mett ◽  
B. Schacher ◽  
P. Schneider ◽  
O. Zak
Keyword(s):  
Binding Proteins ◽  
Beta Lactamase ◽  
The Novel ◽  
Penicillin Binding Proteins

scholarly journals Non-Beta-Lactamase-Producing Penicillin-ResistantEnterococcus faeciumin a Clinical Setting

1990 ◽  
Vol 1 (3) ◽  
pp. 73-76 ◽  
Author(s):  
Daniel Eymard ◽  
Andre Dascal ◽  
John Hiscott ◽  
Sonia Gioseffini ◽  
Janet Stevenson ◽  
...  
Keyword(s):  
Clinical Setting ◽  
Plasmid Dna ◽  
Enterococcus Faecium ◽  
Binding Proteins ◽  
Clinical Isolates ◽  
Beta Lactamase ◽  
Penicillin Binding Proteins ◽  
Mechanism Of Resistance

Six clinical isolates ofEnterococcus faeciumhighly resistant to penicillin are reported. These strains did not produce beta-lactamase and no plasmid DNA could be detected. It is postulated that the mechanism of resistance is one or more chromosomally mediated alterations of penicillin-binding proteins.

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

1997 ◽  
Vol 41 (9) ◽  
pp. 2013-2015 ◽  
Author(s):  
C C Sanders ◽  
P A Bradford ◽  
A F Ehrhardt ◽  
K Bush ◽  
K D Young ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Beta Lactamase ◽  
Penicillin Binding Proteins ◽  
Very High ◽  
Competition Assays

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.

scholarly journals Draft Genome Sequences of Extended-Spectrum-Beta-Lactamase-Producing Morganella morganii Strains AA1 and AV1, Isolated from a Freshwater Lake and Eicchorniacrassipes Roots

2017 ◽  
Vol 5 (24) ◽  
Author(s):  
Pushpa Lata ◽  
Subramaniam S. Govindarajan ◽  
Feng Qi ◽  
Jian-Liang Li ◽  
Santosh K. Maurya ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Draft Genome ◽  
Beta Lactamase ◽  
Genome Sequences ◽  
Morganella Morganii ◽  
Coding Sequences ◽  
Content Type ◽  
Beta Lactamases ◽  
Penicillin Binding Proteins ◽  
Extended Spectrum Beta Lactamase

ABSTRACT Two strains of Morganella morganii, AA1 and AV1, were isolated from freshwater and Eicchornia crassipes roots, respectively. Here, we report their draft genome sequences, which are ~3.6 Mb and have 51% G+C content. The predicted coding sequences (3,259 for strain AA1 and 3,345 for strain AV1) encode beta-lactamases, transpeptidases, and penicillin-binding proteins.

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