Acinetobacter-derived cephalosporinase 7 (ADC-7) (ADC-7)

Acinetobacter-derived cephalosporinase 7 (ADC-7) is a Class C beta-lactamase (AmpC) enzyme predominantly found in the opportunistic pathogen Acinetobacter baumannii (UniProt: P0C1B4). This enzyme plays a critical role in bacterial resistance by catalyzing the hydrolysis of the beta-lactam ring in various antibiotics, including penicillins and extended-spectrum cephalosporins (PubMed: 23478961). ADC-7 is a major factor in the multi-drug resistant (MDR) phenotype of Acinetobacter, which is a leading cause of healthcare-associated infections such as ventilator-associated pneumonia and bloodstream infections (NIH: PMC6411113). Because ADC-7 effectively neutralizes many standard treatments, it has become a primary target for novel beta-lactamase inhibitors. Drugs like durlobactam are designed to specifically inhibit ADC-type enzymes, thereby restoring the clinical utility of antibiotics like sulbactam against resistant Acinetobacter strains (FDA: Xacduro Prescribing Information).

Other names

AmpC beta-lactamase ADC-7Class C beta-lactamase ADC-7blaADC-7 gene productAcinetobacter baumannii cephalosporinase

Inhibition of the beta-lactamase enzyme through covalent binding to the active-site serine residue, preventing the degradation of beta-lactam antibiotics.