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Beta-lactamase enzymes, specifically those belonging to Ambler Class A, are bacterial enzymes that hydrolyze and inactivate beta-lactam antibiotics, leading to antibiotic resistance. They are serine-based enzymes that utilize a conserved serine residue (Ser70) at their active site to cleave the beta-lactam ring. These enzymes are commonly found in pathogens like *Klebsiella pneumoniae* and *Escherichia coli*, contributing to the spread of multidrug-resistant infections. Notable examples include TEM, SHV, CTX-M, and GES variants. Classical inhibitors like clavulanic acid can inhibit many, but not all, class A β-lactamases. Some variants show inhibitor resistance or expanded substrate profiles.
Hydrolyzes beta-lactam ring of antibiotics, rendering them inactive.
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