Metallo-beta-lactamase IMP-7 (IMP-7)

Metallo-beta-lactamase IMP-7 is a Class B1 carbapenemase that plays a critical role in bacterial resistance to beta-lactam antibiotics. It is an enzyme that utilizes one or two zinc ions in its active site to facilitate the nucleophilic attack and subsequent hydrolysis of the beta-lactam ring, effectively inactivating penicillins, cephalosporins, and carbapenems. IMP-7 is frequently identified in multidrug-resistant Gram-negative pathogens, particularly Pseudomonas aeruginosa, and its presence is associated with high mortality rates in clinical settings due to the lack of effective treatment options. As a therapeutic target, IMP-7 is the focus of drug discovery efforts aimed at developing potent inhibitors that can be administered in combination with existing antibiotics to overcome resistance. While some next-generation inhibitors like taniborbactam struggle with IMP-type enzymes, newer candidates such as xeruborbactam (QPX7728) have demonstrated significant activity against this specific variant.

Other names

Imipenemase 7Carbapenem-hydrolyzing beta-lactamase IMP-7Class B metallo-beta-lactamase IMP-7blaIMP-7

Inhibition of the enzyme's catalytic activity by binding to the active site (e.g., boronate-based inhibitors like xeruborbactam) or by chelating the essential zinc ions (e.g., thiol-based inhibitors or aspergillomarasmine A), thereby preventing the hydrolysis of the beta-lactam ring and restoring antibiotic efficacy.