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New Delhi metallo-β-lactamase 1 (NDM-1) is a metallo-β-lactamase enzyme that confers resistance to a broad range of β-lactam antibiotics, including carbapenems, in Gram-negative bacteria such as Enterobacteriaceae (notably *Klebsiella pneumoniae* and *Escherichia coli*)[2][3][4][5]. NDM-1 has a highly flexible and hydrophobic active site, enabling it to accommodate and hydrolyze various β-lactam substrates[3][5]. The enzyme’s active site coordinates two zinc ions, which facilitate hydrolysis of the antibiotic’s β-lactam ring[1][3][5]. NDM-1 is encoded on mobile genetic elements, promoting rapid dissemination among bacterial strains and leading to multidrug-resistant infections[3]. There are currently no approved clinical inhibitors of NDM-1, and its spread poses a significant threat to the effectiveness of current antibiotic therapies[3][5].
Drug hydrolysis: NDM-1 hydrolyzes the β-lactam ring of antibiotics, abolishing their antibacterial activity[3][5]. Broad substrate specificity due to flexible active site[3][5].
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