Serine-type beta-lactamase

Serine-type beta-lactamase is an enzyme produced by various bacteria that confers resistance to beta-lactam antibiotics by hydrolyzing the beta-lactam ring of these drugs. This family includes Class A, C, and D beta-lactamases, which utilize a catalytic serine residue in their active site to attack and deactivate antibiotics such as penicillins, cephalosporins, and carbapenems. These enzymes play a major role in bacterial antimicrobial resistance and are major clinical targets for inhibition in infectious disease management. Serine-type beta-lactamases are structurally and mechanistically distinct from metallo-beta-lactamases (Class B), which use zinc rather than serine for catalysis. Their rapid diversification and prevalence among pathogenic bacteria present a significant therapeutic challenge in contemporary medicine[2][4][5][6].

Other names

Serine beta-lactamaseSerine-based beta-lactamaseClass A beta-lactamaseClass C beta-lactamaseClass D beta-lactamaseSBL

Hydrolysis of the beta-lactam ring of antibiotics via nucleophilic attack by an active site serine, leading to antibiotic inactivation[5][6] Two-step process: acylation (covalent linkage to active site serine) followed by deacylation, releasing an inactive product[5]