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Class A TEM-type beta-lactamase is an enzyme produced by Gram-negative bacteria that confers resistance to beta-lactam antibiotics such as penicillins and early cephalosporins by hydrolyzing the beta-lactam ring, rendering these drugs ineffective[1][3][5]. TEM-1 is the most widespread of these enzymes, plasmid-borne, and highly prevalent in Enterobacteriaceae[3][4]. The catalytic mechanism involves a serine residue at the active site, utilizing a two-step acylation–deacylation process to cleave the antibiotic[1][2][3]. Variants of TEM-type beta-lactamases have adapted to hydrolyze extended-spectrum cephalosporins and resist inhibition by traditional beta-lactamase inhibitors, posing a major clinical challenge in managing infections[1][3][4]. The spread of these enzymes is a leading cause of resistance to commonly used antimicrobials, emphasizing the need for surveillance and novel inhibitors.
Enzymatic hydrolysis of the beta-lactam ring of antibiotics, destroying their antibacterial activity[1][2][3][5] - Resistance to beta-lactamase inhibitors in some TEM variants[1]
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