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Irajie, Cambyz, Mohkam, Milad, Nezafat, Navid, Hosseinzadeh, Saeed, Aminlari, Mahmood, Ghasemi, Younes. (1395). In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus. سامانه مدیریت نشریات علمی, 41(5), 406-414.
Cambyz Irajie; Milad Mohkam; Navid Nezafat; Saeed Hosseinzadeh; Mahmood Aminlari; Younes Ghasemi. "In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus". سامانه مدیریت نشریات علمی, 41, 5, 1395, 406-414.
Irajie, Cambyz, Mohkam, Milad, Nezafat, Navid, Hosseinzadeh, Saeed, Aminlari, Mahmood, Ghasemi, Younes. (1395). 'In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus', سامانه مدیریت نشریات علمی, 41(5), pp. 406-414.
Irajie, Cambyz, Mohkam, Milad, Nezafat, Navid, Hosseinzadeh, Saeed, Aminlari, Mahmood, Ghasemi, Younes. In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus. سامانه مدیریت نشریات علمی, 1395; 41(5): 406-414.

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

Iranian Journal of Medical Sciences
مقاله 6، دوره 41، شماره 5، آذر 2016، صفحه 406-414    اصل مقاله (2.81 M)
نوع مقاله: Original Article(s)
نویسندگان
Cambyz Irajie1؛ Milad Mohkam2؛ Navid Nezafat3؛ Saeed Hosseinzadeh1؛ Mahmood Aminlari4؛ Younes Ghasemi* 5
1Department of Public Health and Food Hygiene, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
2Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran; and Department of Pharmaceutical Biotechnology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran
3Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
4Department of Biochemistry, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
5Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran; and Department of Pharmaceutical Biotechnology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran; and Department of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, Iran
چکیده
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.
کلیدواژه‌ها
Escherichia؛ Bacillus؛ Glutaminase؛ Computer simulation
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