An insight into the complete biophysical and biochemical characterization of novel class A beta-lactamase (Bla1) from Bacillus anthracis.

Affiliation

Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee 247667, India; Centre of Nanotechnology, Indian Institute of Technology Roorkee, Roorkee 247667, India. Electronic address: [Email]

Abstract

Bacillus anthracis, a potent pathogen of anthrax is becoming resistant to many beta-lactam antibiotics because of the expression of two chromosomally encoded beta-lactamases Bla1 and Bla2. Bla1 is a class A beta-lactamase whereas Bla2 is a Metallo beta-lactamase. In the current study, we have attempted in-detailed characterization of Bla1 beta-lactamase by taking interdisciplinary approaches. Our study includes structure and sequence comparison of this enzyme with other members of the class, to know the conservation pattern that includes active site residues, secondary structure, conserved fold, evolutionary relationships, etc. Dynamic characterizations of the enzyme, unfolding kinetics were determined with the help of Molecular dynamics simulation. Detailed enzyme stability and catalytic activity towards various physical (Temperature and pH), and chemical parameters (Urea, GnHCl) were performed. Together, our study helps to develop a proper understanding of this beta-lactamase by characterizing its biochemical, biophysical, dynamic, kinetic and thermodynamic properties. This would help contribute towards a better understanding of beta-lactamase based AMR emergence.

Keywords

Antimicrobial resistance,Biochemical studies,Biophysical characterization,Catalytic divergence,Minimum inhibitory concentration,Molecular docking,Molecular dynamics simulation,Spectrophotometry techniques,

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