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Bacterial resistance enzymes are a diverse group of proteins produced by bacteria to neutralize or inactivate antimicrobial agents, thereby conferring antibiotic resistance (Bush & Bradford, 2016; Ramirez & Tolmasky, 2010). These enzymes function through various mechanisms, including hydrolysis (e.g., beta-lactamases), group transfer (e.g., aminoglycoside-modifying enzymes), or redox reactions (Munita & Arias, 2016). By degrading or modifying the chemical structure of antibiotics, these enzymes prevent the drugs from reaching or binding to their intended cellular targets, such as the cell wall or ribosomes (Blair et al., 2015). In clinical settings, these enzymes are major drivers of treatment failure in infections caused by Gram-negative and Gram-positive pathogens (WHO, 2023). Therapeutic strategies often involve the use of enzyme inhibitors in combination with antibiotics to restore the drug's efficacy (StatPearls, 2023). Understanding the structural and functional diversity of these enzymes is critical for the development of next-generation antimicrobial therapies and diagnostic tools.
Inhibition of enzyme activity through competitive, non-competitive, or suicide inhibition to prevent the degradation or modification of co-administered antibiotics (StatPearls, 2023; Bush & Bradford, 2016).
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