TEM-1 β-lactamase (TEM-1)

TEM-1 β-lactamase is a class A serine hydrolase enzyme, most commonly found in Gram-negative bacteria, and responsible for resistance to penicillins and early generation cephalosporins. Engineered versions involve specific mutations, substitutions, or chimeric recombinations to probe enzymatic properties, substrate scope, stability, and inhibitor susceptibility. Its catalytic mechanism involves a nucleophilic serine attacking the β-lactam ring of antibiotics, facilitating hydrolysis and drug inactivation[1][2][3][4][5][6]. Engineered mutants are also critical for studying the molecular evolution and biophysical characterization of β-lactamase function, as well as developing new antibacterial strategies. The clinical significance of TEM-1 and its derivatives rests in their roles in multidrug-resistant infections, which continue to drive the need for novel therapies and diagnostic monitoring.

Other names

TEM β-lactamaseTEM-1 penicillinaseClass A β-lactamase (TEM-type)Engineered TEMLaboratory-engineered TEM-1 β-lactamase

Hydrolysis of the β-lactam ring of antibiotics, leading to inactivation of the antimicrobial agent and ensuing resistance[1][2][3][4][5]. Mutations and engineered alterations can extend substrate specificity or confer resistance to β-lactamase inhibitors[2][4][5].