ArticleBiotechnology and applied biochemistry2026
In Silico Characterization and Molecular Docking of the L-Arginase Gene From Alcaligenes aquatilis BC2.
Article in Biotechnology and applied biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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
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