Bacteria achieve resistance to beta-lactam antibiotics primarily through the production of beta-lactamase enzymes. These enzymes bind to the antibiotic's characteristic beta-lactam ring and hydrolyze it, breaking the ring structure. This inactivation prevents the antibiotic from inhibiting cell wall synthesis, rendering it ineffective.

Mechanism of Beta-Lactam Resistance

- The Acinetobacter derived cephalosporinase (ADC) enzyme is a beta-lactamase 
- ADC-7 has broad antibiotic properties. 
- It is a target for novel beta-lactamase inhibitors (BLIs). 
- Not a currently targeted beta-lactamase for an inhibitor

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- Beta-lactamase enzymes are enzymes that cleave beta-lactam antibiotics. 
- They are enzymes responsible for beta-lactam antibiotic resistance.
- Their mechanism of action against antibiotics is cleaving the beta-lactam ring in beta-lactam antibiotics which prevents it being effective. 

Beta-lactamases

Powers, R. A., Swanson, H. C., Taracila, M. A., Florek, N. W., Romagnoli, C., Caselli, E., Prati, F., Bonomo, R. A., & Wallar, B. J. (2014). Biochemical and Structural Analysis of Inhibitors Targeting the ADC-7 Cephalosporinase of Acinetobacter baumannii. Biochemistry, 53(48), 7670–7679. https://doi.org/10.1021/bi500887n

Biochemical and Structural Analysis of Inhibitors Targeting the ADC‑7 Cephalosporinase of Acinetobacter baumannii

ADC-7

- They have a characteristic beta-lactam ring that is important in its mechanism of action. 
- These antibiotics inhibit cell wall synthesis in bacteria thus preventing bacterial replication and further bacterial propagation.
- Known antibiotics: Penicillins, cephalosporins, carbapenems
- In recent years, increasing resistance to this type of antibiotic has been a growing concern.

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