Anshika Gupta

Research Area: Structure and Function of Class-C β-lactamase.

Expertise: Protein purification, Circular Dichroism, Steady state Kinetic assay, Protein Modelling, Validation, Molecular Docking

Abstract: Antimicrobial resistance (AMR) has escalated into a global crisis, and Class C β-lactamases are serine-dependent hydrolases that contribute significantly to bacterial resistance against β-lactam antibiotics, particularly higher-generation cephalosporins. Among them, Acinetobacter-derived cephalosporinases (ADC enzymes) represent clinically important and structurally dynamic variants. These enzymes possess an expanded and flexible active site, shaped by key structural elements including the Ω-loop and a spacious R2-binding pocket, which together enable efficient accommodation and hydrolysis of bulky cephalosporin substrates. Catalysis proceeds via a conserved serine-mediated acylation–deacylation mechanism, but distinct loop dynamics and active-site organization differentiate Class C enzymes from other β-lactamase classes.