PER-1 beta-lactamase (PER-1)

PER-1 beta-lactamase is a class A serine-based enzyme in the Ambler molecular classification system, belonging to the extended-spectrum beta-lactamase (ESBL) family, and is encoded on plasmids or chromosomes in Gram-negative bacteria such as Pseudomonas aeruginosa, Acinetobacter spp., Escherichia coli, Salmonella enterica, Proteus mirabilis, and others. It efficiently hydrolyzes penicillins, extended-spectrum cephalosporins like ceftazidime, cefotaxime, ceftriaxone, and monobactams such as aztreonam, but does not hydrolyze cephamycins or carbapenems, conferring resistance to these antibiotics while remaining susceptible to inhibition by clavulanate. First identified in Pseudomonas aeruginosa, PER-1 shows low homology (25-27%) to common TEM and SHV ESBLs and shares relatedness with enzymes like PER-2, VEB-1, and TLA-1, often linked to chromosomal beta-lactamases in Bacteroides species. Its prevalence is notable in regions like Turkey, Korea, South America, France, Italy, and Belgium, contributing to nosocomial infections and challenging treatment of multidrug-resistant pathogens prioritized by the WHO. Drugs targeting PER-1 primarily act via beta-lactamase inhibitors combined with beta-lactams, though newer agents like avibactam show reduced efficacy compared to other class A ESBLs, posing therapeutic challenges in combating ESBL-producing Enterobacteriaceae.

Other names

PER beta-lactamasePseudomonas extended resistant beta-lactamase

Beta-lactamase inhibition