Overexpression, Purification, and Biochemical Characterization of the vanC2 d-Ala-d-Ser Ligase from <i>Enterococcus casseliflavus</i> SSK and Its Inhibition by an Oxadiazole Derivative.

ABSTRACT: The bacterial cell wall and enzymes involved in peptidoglycan biosynthesis are prime targets for the discovery of novel antibacterial agents. Among these enzymes, d-alanine-d-alanine ligases (Ddl) are particularly significant due to their utilization of specific substrates (d-amino acids) essential for bacterial viability. Isozymes of Ddl that utilize alternative substrates such as d-lactate or d-serine are found in vancomycin-resistant Gram-positive bacteria, initially identified in Enterococcus species, and now represent a growing concern in clinical settings. In this study, we isolated and identified vancomycin-resistant Enterococcus casseliflavus (E. casseliflavus) strain SSK and used it for amplification, cloning, and purification of the vanC2 type of d-alanine-d-serine

SUBMITTER: Paymal SB 

PROVIDER: S-EPMC12004154 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature