Debasmita Chatterjee

Rv0783c of Mycobacterium tuberculosis acts as a proton-motive force dependent multidrug efflux transporter involved in the efflux of structurally unrelated antibiotics and enhancing biofilm formation

This study identifies Rv0783c as a multidrug efflux transporter in Mycobacterium tuberculosis that enhances antibiotic resistance and biofilm formation.

Substitution of a valine to glutamic acid in the omega-like loop of MSMEG_6194 of Mycobacterium smegmatis interchanges its activity from DD-carboxypeptidase to beta-lactamase

This study identifies MSMEG_6194 in Mycobacterium smegmatis as a DD-carboxypeptidase, showing that a single amino acid substitution converts its activity to beta-lactamase.

Putative MFS transporter Rv1250 of Mycobacterium tuberculosis is involved in multidrug efflux activity

This study identifies Rv1250 as a multidrug efflux pump in Mycobacterium tuberculosis that enhances drug resistance by facilitating drug extrusion and biofilm formation.

Conserved ancillary residues situated proximally to the VIM-2 active site affect its metallo β-lactamase activity

The paper investigates the impact of specific amino acid substitutions near the VIM-2 active site on its metallo β-lactamase activity and stability, finding that N210A and D182A reduce catalytic efficiency and thermal stability.

A magnesium transporter CorA of Mycobacterium smegmatis enhances the tolerance of structurally unrelated antibiotics in the host cells

This study shows that the magnesium transporter CorA in Mycobacterium smegmatis and E. coli increases tolerance to structurally unrelated antibiotics and enhances biofilm formation.