In silico characterization and molecular docking of the MIOX gene in Nile tilapia (Oreochromis niloticus)

Myo-inositol oxygenase (MIOX) plays an essential role in metabolic pathways and cell processes, controls oxidative stress response mechanisms, and balances osmotic stress in aquatic organisms. Molecular docking and structural analysis of the MIOX gene have been accomplished in this work. The MIOX gene has a length of 3608 bp, which encodes 286 amino acids (AA). The secondary structure revealed α-helical and random coils containing 40.56% alpha helices, 38.81% random coils, 14.69% extended strands, and 5.94% beta turns. The subcellular localization results showed that 56% of the MIOX gene is found in cytoplasm and then 10% in lysosome. The Ramachandran plot analysis showed that 90.2% of residues fall in the most favored region and 9.8% in the additional allowed region. Virtual screening of ligands and molecular docking of inositol (CID-892) and D-glucuronic acid (CID-94715) showed the highest docking score values of - 4.015 and - 3.563, respectively. The Potential Energy OPLS3e was - 1632.608 and - 1545.687. Inositol and D-glucuronic acid interacted with different residues of MIOX protein. However, a greater binding affinity of MIOX was observed with inositol than with D-glucuronic acid. This signifies the biochemical role of inositol that helps in determining the enzymatic efficiency. So, this study offers insights into protein modeling, molecular docking, and virtual screening of ligands against the MIOX receptor, revealing aspects of drug design and preventive approaches for fish salinity tolerance.