2017年10月31日 · KPC-2 is a β-lactamase that inactivates carbapenems and β-lactamase inhibitors (e.g., clavulanate) and is prevalent around the world, including in the United States. Resistance to the new antibiotic ceftazidime-avibactam, which was designed to overcome KPC resistance, had already emerged within a year.

2022年3月24日 · 2020年发表在《细胞和感染微生物学的前沿》（Front Cell Infect Microbiol）杂志的一项研究显示，在成人和儿童患者中分离的CRE菌株中， bla kpc-2 (51.6%) 是最常见的碳青霉烯酶基因。

2018年8月27日 · Using enhanced sampling computational methods together with site-directed mutagenesis, we report the identification of two “hydrophobic networks” in the KPC-2 enzyme, the integrity of which has...

2017年9月26日 · One key mechanism of resistance is the breakdown of β-lactam antibiotics by β-lactamase enzymes. KPC-2 is a β-lactamase that inactivates carbapenems and β-lactamase inhibitors (e.g., clavulanate) and is prevalent around the world, including in the United States.

Visualize and interact with protein structures with 3-D information available at PDB. Click PDB: 2OV5. KPC-2 is a beta-lactamase found in Klebsiella pneumoniae and Pseudomonas aeruginosa. Smith Moland E, et al. 2003. J Antimicrob Chemother 51 (3): 711-714.

We show that KPC-2 has a 20,000-fold increased deacylation rate compared with the common TEM-1 β-lactamase. Furthermore, kinetic analysis of active site alanine mutants indicates that carbapenem hydrolysis is a concerted effort involving multiple residues.

Carbapenem-resistant Enterobacteriaceae are resistant to most β-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A β-lactamase. Here, we present the first product complex crystal structures of KPC-2 with β-lactam antibiotics containing hydrolyzed cefotaxime and faropenem.

2023年7月25日 · In this study, we compared and analyzed MDR region of the F94_plasmid bearing KPC-2 with those of related plasmids, characterized the KPC-2 core structure of the plasmid, and explored the...

Plasmid transferability assay and phylogenic analysis suggested an evolutionary pathway that KPC-2-NDM-1-CRKP emerged from a KPC-2-CRKP progenitor which acquired another highly transferable bla NDM-1 plasmid later. Further, demographics and stability test revealed that these isolates were stable and had the potential for transmission among ...

The three KPC-2 molecules are depicted in a Cα trace. Active site residues and bicine molecules are shown in stick representation and labeled accordingly. The structure of KPC-2 contains two subdomains generating a cleft resulting in an overall fold that is expectedly similar to that of other class A β-lactamases . One of the subdomains is ...