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Serine beta-lactamases are bacterial enzymes that hydrolyze beta-lactam antibiotics, conferring resistance. They belong to Ambler classes A, C, and D and utilize a conserved serine residue in their active site for catalysis. They are clinically relevant due to their role in antibiotic resistance and are targeted by beta-lactamase inhibitors.
Acylation-deacylation mechanism: nucleophilic attack on the beta-lactam ring by a serine residue, followed by hydrolysis of the acyl-enzyme intermediate.
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