In Silico Structural and Functional Analysis of Bacillus megaterium Asparaginase

Abstract

L-Asparaginase, which catalyzes L-asparagine, an essential amino acid for leukemic cells, into L-aspartic acid and ammonia, is used as a chemotherapeutic agent for the treatment of acute lymphoblast leukemia (ALL). Commercially available L-asparaginases from Escherichia coli and Erwinia chrysanthemi have a short half-life and several side effects on the administration to the patient. Therefore, there is a need for stable, more specific L-asparaginase with no or minimal side effects. This study aims to conduct an in silico structural and functional analysis of B. megaterium asparaginase (BmA) to explore its physicochemical properties using various computational tools. This study is an effort to find its potential as an alternative to commercially available asparaginases. In silico investigation of BmA suggests that the enzyme’s homo-tetramer is thermostable due to higher aliphatic indices (i.e. 98.95). Its monomeric unit has a molecular weight of 35.15 kDa. The stability of the protein is due to the presence of a high percentage of α-helices and β strands. In silico studies primarily suggest that BmA has all the desired properties for being used as a chemotherapeutic which further needs to be validated experimentally.