ArticleIranian journal of medical sciences2016
In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus.
Article in Iranian journal of medical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
backgroundGlutaminase (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.
methodsForty 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.
resultsThe 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.
conclusionOur 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.
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27582590PMC4967485W2501452551What OpenQuestion holds
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