Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
class C beta-lactamase
Overview
Mutational Replacement of Leu-293 in the Class C Enterobacter cloacae P99 beta-lactamase Confers Increased MIC of Cefepime.
The Leu-293-Pro mutation in the class C Enterobacter cloacae P99 beta-lactamase increases the MIC of cefepime and ceftazidime.
Identification of residues critical for catalysis in a class C beta-lactamase by combinatorial scanning mutagenesis.
The study identified several mutations in the class C beta-lactamase P99 that significantly reduce antibiotic resistance, indicating the importance of specific residues in catalytic activity.
Characterisation and clinical features of Enterobacter cloacae bloodstream infections occurring at a tertiary care university hospital in Switzerland: is cefepime adequate therapy?
Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine beta-lactamases by Relieving Steric Strain.
The study demonstrates that replacing the active-site serine with glycine in various serine beta-lactamases enhances their thermal stability by reducing steric strain, although this substitution significantly reduces catalytic efficiency.
QPX7728, An Ultra-Broad-Spectrum B-Lactamase Inhibitor for Intravenous and Oral Therapy: Overview of Biochemical and Microbiological Characteristics.
QPX7728 is a novel beta-lactamase inhibitor with broad-spectrum activity against serine and metallo-beta-lactamases, including Class A, C, D, and B enzymes. It effectively inhibits clinically relevant beta-lactamases such as KPC-2, CTX-M-15, SHV-12, TEM-43, OXA-48, OXA-23, NDM-1, and VIM-1.
β-Lactam Antibiotics and beta-lactamase Enzymes Inhibitors, Part 2: Our Limited Resources.
The paper reviews β-lactam antibiotics and beta-lactamase enzymes inhibitors, focusing on the mechanisms of resistance mediated by beta-lactamases such as TEM-1, SHV-1, KPC-2, OXA-48, and NDM-1, and highlights the need for new inhibitors to combat carbapenem-resistant bacteria.
Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C β-Lactamases.
The study identifies three nanobodies (cAb CMY-2 (250), cAb CMY-2 (254), and cAb CMY-2 (272)) that specifically bind to CMY-2 β-lactamase, with cAb CMY-2 (254) showing the highest stability and affinity. These nanobodies act as noncompetitive inhibitors of CMY-2 activity and are used to develop a highly specific sandwich ELISA for detecting CMY-2-producing bacteria.
In vitro potency of xeruborbactam in combination with multiple β-lactam antibiotics in comparison with other β-lactam/β-lactamase inhibitor (BLI) combinations against carbapenem-resistant and extended-spectrum β-lactamase-producing Enterobacterales.
Xeruborbactam (XER) showed superior in vitro potency against carbapenem-resistant and extended-spectrum β-lactamase-producing Enterobacterales when combined with various β-lactam antibiotics compared to other β-lactam/β-lactamase inhibitor combinations. XER effectively inhibited a wide range of β-lactamases, including metallo-β-lactamases (MBLs) and serine β-lactamases, enhancing the activity of antibiotics such as meropenem, cefepime, ceftolozane, ceftriaxone, aztreonam, piperacillin, and ertapenem.
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