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Class A and C beta-lactamases are bacterial enzymes responsible for resistance to a wide range of beta-lactam antibiotics by hydrolyzing the four-membered beta-lactam ring. Class A enzymes (serine beta-lactamases) are common in Gram-negative bacteria and include well-known types such as TEM, SHV, CTX-M, and KPC, with the ability to hydrolyze penicillins, cephalosporins, and sometimes carbapenems. Class C enzymes (AmpC beta-lactamases) preferentially inactivate cephalosporins and are less susceptible to inhibition by traditional beta-lactamase inhibitors. Both are major contributors to hospital- and community-acquired bacterial resistance, posing critical challenges in infectious disease management. Detection of their activity or genes is a key biomarker for guiding appropriate antibiotic therapy.
Enzymatic hydrolysis of the beta-lactam ring, rendering beta-lactam antibiotics inactive
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