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IMP-10 is a variant of the IMP-type metallo-beta-lactamase (MBL), a class of enzymes that confer high-level resistance to a wide range of beta-lactam antibiotics, including carbapenems, which are often considered last-resort treatments. As an Ambler Class B enzyme, IMP-10 utilizes zinc ions in its active site to catalyze the hydrolysis of the beta-lactam ring, thereby inactivating the drug. It is primarily found in Gram-negative pathogens such as Pseudomonas aeruginosa and members of the Enterobacteriaceae family. The presence of IMP-10 significantly complicates the treatment of hospital-acquired infections, as it is not inhibited by traditional beta-lactamase inhibitors like clavulanic acid or avibactam. Current therapeutic strategies focus on developing novel MBL inhibitors or using antibiotics like cefiderocol and aztreonam, which exhibit relative stability against these enzymes.
Hydrolysis of the beta-lactam ring of antibiotics using zinc-coordinated water as a nucleophile.
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