The project aims to address the escalating threat of antimicrobial resistance by investigating the structural and functional mechanisms of L1 and L2 beta-lactamases, particularly those produced by the opportunistic pathogen Stenotrophomonas maltophilia. Unlike most bacteria, which employ a single resistance pathway, this pathogen uses both L1 metallo-beta-lactamases and L2 serine-beta-lactamases, making it exceptionally difficult to treat with traditional antibiotics. Alongside this work, I am developing novel boronate inhibitors targeting a broad range of beta-lactamases, including Class A carbapenemases such as SME and other prevalent variants. These boronates act as transition-state analogs, mimicking the tetrahedral intermediate formed during beta-lactam hydrolysis and thereby blocking enzyme activity. By combining high-resolution X-ray crystallography with enzyme kinetics and biophysical assays, I aim to understand these enzyme-inhibitor interactions at the molecular level to support the rational design of effective, broad-spectrum therapeutics.