In Silico Structural and Functional Analysis of Bacillus Megaterium Arginase

Abstract

Arginase is a ubiquitously occurring metalloenzyme that shows an anticancer property. It can be isolated from various species of plants, animals, bacteria and fungi. Although several bacterial species have already been explored to get new arginases, they are not up to the mark for application in cancer treatment. As a result, there is a need for a new arginase with a longer half-life, improved stability, and efficacy. Therefore, the present study is aimed to conduct an in silico study of the arginase of Bacillus megaterium to analyze its physicochemical properties and their correlations with their structure. For performing the current study, full-length sequences of Bacillus arginases were procured from the UNIPROT database and then analyzed the physicochemical and secondary structures and active site composition using various online bioinformatics tools. PROTOPARAM is used to analyze physicochemical characteristics. SWISS-Model and I-Tasser server were used for making the 3D structure of the B. megaterium arginase (BmA). The current study suggests that B. megaterium arginase is a thermostable enzyme with a slightly acidic pH. All other properties of Bacillus megaterium arginase are in the line as for from different Bacillus sp. Hence, the current studies suggest that Bacillus megaterium arginase also has similar potential as other arginases of various Bacillus sp. Further experimental validation is needed for the characterization of BmA to establish its potential application in cancer treatment.