Structural Modelling and Molecular Dynamics Study on Erwinaze towards its substrates

DOI: 10.5176/2251-2489_BioTech15.67

Authors: Erva Rajeswara Reddy, Rajulapati Satish Babu and Chandrasai Potla durthi

Abstract: Acute Lymphocytic Leukemia (ALL) is an Outrageous disease worldwide. L-Asparagine and L-Glutamine deamination plays crucial role in ALL treatment. Role of Erwinaze (L-Asparaginase from Erwinia chrysanthemi) in regulation of L-Asparagine and L-Glutamine has been confirmed by the experimental studies. Therapeutic research against ALL remained elusive with the lack of structural information on Erwinaze enzyme. In this present insilico study, homology model of the Erwinaze was predicted using Modeller and the same was validated by various quality indexing tools. For the apo state enzyme and ligand bound state complexes MD simulations were performed and the trajectory analysis described the conformational changes of structures in the dynamic system. Ligand binding mechanisms were studied using different docking tools to interpret the various ligand-receptor interactions and binding free energies. MD simulation of docked complex with L-Asparagine ligand substrate showed the defined structural folding with stable conformation over the L-Glutamine complex in dynamic environment. Our insilico reports give much more information on structural and functional aspects of Erwinaze with its ligands which may be useful in designing of effective therapeutics for ALL.

Keywords: Erwinaze; Homology; Modelling; Molecular Docking; MD simulations; Acute Lymphocytic Leukemia