Identification of Novel VEB β-Lactamase Enzymes and Their Impact on Avibactam Inhibition
Author:
Affiliation:
1. Infection Innovative Medicines Unit, AstraZeneca R&D Boston, Waltham, Massachusetts, USA
Abstract
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Link
https://journals.asm.org/doi/pdf/10.1128/AAC.00047-16
Reference20 articles.
1. Activity of avibactam against Enterobacter cloacae producing an extended-spectrum class C -lactamase enzyme
2. Kinetics of the interaction between avibactam and the CHE-1 class C -lactamase
3. Structure of the Extended-Spectrum Class C β-Lactamase of Enterobacter cloacae GC1, a Natural Mutant with a Tandem Tripeptide Insertion,
4. Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase
5. A tripeptide deletion in the R2 loop of the class C -lactamase enzyme FOX-4 impairs cefoxitin hydrolysis and slightly increases susceptibility to -lactamase inhibitors
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