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Brazil Klebsiella carbapenemase 1 (BKC-1) is a Class A serine beta-lactamase that confers broad-spectrum resistance to beta-lactam antibiotics, including carbapenems, penicillins, and cephalosporins (Perez-Chaparro et al., 2013). First identified in clinical isolates of Klebsiella pneumoniae in Brazil, the enzyme is characterized by its ability to hydrolyze carbapenems, which are critical last-resort treatments for multidrug-resistant infections (Nicoletti et al., 2015). BKC-1 is typically encoded on highly mobile plasmids, such as IncX3, which facilitates its horizontal transfer and rapid spread among various Enterobacteriaceae species (Ferreira et al., 2019). The enzyme's catalytic mechanism involves a conserved serine residue that mediates the hydrolysis of the antibiotic's beta-lactam ring, effectively neutralizing its antibacterial activity. Clinically, BKC-1-producing pathogens pose a significant threat in healthcare settings due to limited therapeutic options. However, BKC-1 remains susceptible to inhibition by newer non-beta-lactam beta-lactamase inhibitors like avibactam and vaborbactam, which are used in combination with antibiotics to restore clinical efficacy (Cunningham et al., 2019).
Inhibition of the carbapenemase enzyme activity to prevent the hydrolysis of beta-lactam antibiotics, thereby restoring their antibacterial efficacy.
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