Bioinformatic Analysis of L-Asparaginase Structures in Halophilic (Bacillus subtilis), Mesophilic (Kibdelosporangium), and Thermophilic (Thermococcus kodakarensis) Bacteria: New Insights on L-asparaginase as a Potent Antileukemic Agent

Background: The L-asparaginase enzyme is used as an anticancer agent in treating acute lymphoblastic leukemia (ALL). Moreover, it has widespread applications in medicine, food, and pharmaceutical industries. Methods: The nucleotide and amino acid sequences of L-asparaginase derived from Bacillus subtilis BEST7613, Kibdelosporangium sp. MJ126-NF4, and Thermococcus kodakarensis KOD1 have been obtained from the GenBank and the NCBI databases. The EMBOSS Water pairwise sequence alignments were performed using ClustalW 1.83. Prediction of secondary and tertiary protein structures of the different L-asparaginase molecules studied was done using SWISS-MODEL software. In addition, the protein domains of L-asparaginase originating from the three mentioned bacteria were analyzed using PROSITE software. Theoretical isoelectric point (pI), molecular weight, and amino acid composition were predicted using the protein pI calculator (http://isoelectric.ovh.org/). Results: Despite the structural differences in L-asparaginase enzymes in the three bacterial strains, there were no differences in their functional characteristics, including molecular weight, pI, and functional domain. Conclusion: Analyzing structural differences and finding functional similarities can be useful in designing drugs with higher stability and biological half-life. Our analysis showed that proteins with different structures could have similar functional characteristics, which proves the codon usage hypothesis.