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. 2016 Sep;41(5):406-14.

In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus

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In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus

Cambyz Irajie Md et al. Iran J Med Sci. 2016 Sep.

Abstract

Background: Glutaminase (EC 3.5.1.2) catalyzes the hydrolytic degradation of L-glutamine to L-glutamic acid and has been introduced for cancer therapy in recent years. The present study was an in silico analysis of glutaminase to further elucidate its structure and physicochemical properties.

Methods: Forty glutaminase protein sequences from different species of Escherichia and Bacillus obtained from the UniProt Protein Database were characterized for homology search, physiochemical properties, phylogenetic tree construction, motif, superfamily search, and multiple sequence alignment.

Results: The sequence level homology was obtained among different groups of glutaminase enzymes, which belonged to superfamily serine-dependent β-lactamases and penicillin-binding proteins. The phylogenetic tree constructed indicated 2 main clusters for the glutaminases. The distribution of common β-lactamase motifs was also observed; however, various non-common motifs were also observed.

Conclusion: Our results showed that the existence of a conserved motif with a signature amino-acid sequence of β-lactamases could be considered for the genetic engineering of glutaminases in view of their potential application in cancer therapy. Nonetheless, further research is needed to improve the stability of glutaminases and decrease their immunogenicity in both medical and food industrial applications.

Keywords: Bacillus; Computer simulation; Escherichia; Glutaminase.

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Figures

Figure 1
Figure 1
Multiple sequence alignment of glutaminase protein sequences shows maximum homology from amino-acid residues 60–120. The represented accession numbers of the bacteria and their complete details are provided in table 1.
Figure 2
Figure 2
Phylogenetic tree constructed using the neighbor-joining (NJ) method based on the glutaminase protein sequences from different species of Escherichia and Bacillus is depicted here. The represented accession numbers of the bacteria and their comprehensive details are provided in table 1.

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