In Silico analysis of a novel glutaminase from moderately halophilic bacterium Nesterenkonia Sp. strain F

L-Glutaminase (L-glutamine amidohydrolase, EC 3.5.1.2) is the important enzyme that catalyzes the deamination of L-glutamine to L-glutamic acid and ammonium ions. Recently, L-glutaminase has received much attention with respect to its therapeutic and industrial applications. It acts as a potent antileukemic agent and shows flavor-enhancing capacity in the production of fermented foods. The present study was an in silico analysis of a novel glutaminase from Nesterenkonia Sp. Strain F (a gram-positive and halophilic bacteria of the Micrococcaceae family) to predict its structure and physicochemical properties By utilizing bioinformatics tools, such as NCBI blast,SignalP4.1 server, Genomics %G~C content calculator, ProtParam and Phyre2. Accroding to the results, nucleotide sequence of the selected glutaminase from Nesterenkonia Sp. F has 1230 bp, 71.79% G~C content, and was similar to Nocardioides dokdonensis FR1436, complete genome(with 65% coverage);its protein sequence has 409 amino acide , and was similar to Glutaminase from Micrococcus luteus K-3 (id%:52). its secondary structure contain 47% alpha-helix ,and 12% beta-sheet. Moreover,The instability index (II) of the protein is computed to be 28.08 ,this classifies the protein as stable,and its half-life in mammalian reticulocytes(in vitro)and Escherichia coli(in vivo) has been estimated:30 hour, > 10 hours, respectively. In Conclusion, the selected glutaminase from Nesterenkonia Sp. F was predicted as a salt- tolerant glutaminase which could be employed in fermented food industries.

Keywords:

Nesterenkonia Sp.strain F , halophilic bacteria , glutaminase , In Silico analysis , salt-tolerant ,