Beta-lactamase enzyme (bacterial) (β-lactamase)

Beta-lactamase enzymes are bacterial hydrolases that confer resistance to β-lactam antibiotics by hydrolyzing the β-lactam ring, the core structure essential for antibiotic activity[1][2]. Classified into four major molecular classes (A-D), these enzymes can be serine-based or require metal ions (zinc) at their active sites, and their occurrence is a principal mechanism of clinical antibiotic resistance in both Gram-positive and Gram-negative bacteria[3][5]. Beta-lactamases are widespread among pathogenic bacteria, are often transmissible via plasmids, and their presence correlates closely with reduced efficacy of key antibiotic classes[1][5][8]. Several β-lactamase inhibitors have been developed and are clinically co-administered with β-lactam antibiotics to restore treatment effectiveness, but continual evolution and spread of new β-lactamase variants remain a significant challenge to infectious disease management and public health[6][8].

Other names

Beta-lactamaseβ-lactamaseBeta-lactam antibiotic hydrolaseAntibiotic resistance enzyme

Hydrolysis of the β-lactam ring, rendering the antibiotic molecule inactive[1][2][8] Resistance inhibition by specific inhibitors (e.g., clavulanic acid acts as a "suicide inhibitor" by binding irreversibly to the active site serine of class A enzymes)[3][5][8]