ABSTRACT L‐arginine is a vital amino acid metabolized by L‐arginase, an enzyme with growing biotechnological and therapeutic significance, particularly in cancer treatment. This study presents a comprehensive in silico characterization of the L‐arginase gene isolated from Alcaligenes aquatilis BC2, a bacterium originating from Ethiopian soda lakes. The analysis identified a 336‐amino‐acid enzyme predicted to be stable, soluble, and extracellular. Homology modeling generated a reliable hexameric 3D structure with high stereochemical quality, validated through multiple structural assessment tools. Phylogenetic and conserved domain analyses confirmed the enzyme's evolutionary placement within the Alcaligenes genus and highlighted preserved functional motifs. Molecular docking predicted a strong binding affinity (−7.1 kcal mol −1 ) for L‐arginine, with ligand enzyme complex stabilized by a dense network of hydrogen bonds and electrostatic interactions within the active site. These findings elucidate the structural basis of the enzyme's function and underscore its potential for future experimental validation and therapeutic applications.
Assega et al. (Sat,) studied this question.