Klebsiella pneumoniae carbapenemase 2 (KPC-2)

Klebsiella pneumoniae carbapenemase 2 (KPC-2) is a potent Class A serine beta-lactamase that confers broad-spectrum resistance to nearly all beta-lactam antibiotics, including penicillins, cephalosporins, and carbapenems (Munoz-Price et al., 2013, Lancet Infect Dis). The enzyme functions by utilizing an active-site serine residue to nucleophilically attack and hydrolyze the beta-lactam ring, thereby inactivating the antibiotic before it can reach its bacterial cell wall targets (Papp-Wallace et al., 2011, Antimicrob Agents Chemother). KPC-2 is primarily found in Klebsiella pneumoniae but has spread globally across various Enterobacteriaceae species via highly mobile genetic elements like the Tn4401 transposon (Chen et al., 2014, Future Microbiol). Infections caused by KPC-2-producing organisms are a major public health threat, often associated with high morbidity and limited therapeutic options (Tzouvelekis et al., 2012, Clin Microbiol Rev). Modern clinical management relies on the use of novel beta-lactamase inhibitors, such as avibactam, vaborbactam, and relebactam, which are administered in combination with beta-lactams to neutralize the enzyme and restore antibacterial activity (Galani et al., 2021, Front Med).

Other names

KPC-2 beta-lactamaseClass A carbapenemase KPC-2blaKPC-2Carbapenem-hydrolyzing beta-lactamase KPC-2

Inhibition of the enzyme's catalytic activity through covalent or non-covalent binding to the active site serine residue, preventing the hydrolysis of beta-lactam antibiotics and restoring their efficacy.