Hydroxynitrile lyase (HNL) plays significant role in plant defence mechanism, through the synthesis of chiral cyanohydrins, which act as antifeedants. Present investigation was undertaken on hydroxynitrile lyase from Manihot esculenta, in order to increase its efficiency through mutagenesis. For this purpose, six amino acid (Trp-128, Leu-149, Leu-158, Leu-179, Ile-210 and Phe-210) residues were selected for ‘in silico ’mutagenesis with hydrophobic amino acids to generate 25single-mutants. These ‘in silico ’mutants were analysed for protein-ligand interactions and binding affinity. Mutants with proper orientation of the substrate were identified. To improve binding affinity, double-point ‘in silico ’mutations were carried out. In addition, stability of these mutants was evaluated through molecular dynamic (MD) simulation studies.
Hydroxynitrile lyase, Manihot esculenta, In silico mutagenesis, Molecular Docking, Molecular Dynamic Simulation
