In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus
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. Metho...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Shiraz University of Medical Sciences
2016-09-01
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| Series: | Iranian Journal of Medical Sciences |
| Online Access: | http://ijms.sums.ac.ir/index.php/IJMS/article/view/2225 |
| _version_ | 1811325180423700480 |
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| author | Cambyz Irajie Milad Mohkam Navid Nezafat Saeed Hosseinzadeh Mahmood Aminlari Younes Ghasemi |
| author_facet | Cambyz Irajie Milad Mohkam Navid Nezafat Saeed Hosseinzadeh Mahmood Aminlari Younes Ghasemi |
| author_sort | Cambyz Irajie |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T14:28:38Z |
| format | Article |
| id | doaj.art-85503a7a542c40a2b5c0004b847479f1 |
| institution | Directory Open Access Journal |
| issn | 0253-0716 1735-3688 |
| language | English |
| last_indexed | 2024-04-13T14:28:38Z |
| publishDate | 2016-09-01 |
| publisher | Shiraz University of Medical Sciences |
| record_format | Article |
| series | Iranian Journal of Medical Sciences |
| spelling | doaj.art-85503a7a542c40a2b5c0004b847479f12022-12-22T02:43:15ZengShiraz University of Medical SciencesIranian Journal of Medical Sciences0253-07161735-36882016-09-01415406414In Silico Analysis of Glutaminase from Different Species of Escherichia and BacillusCambyz Irajie0Milad Mohkam1Navid Nezafat2Saeed Hosseinzadeh3Mahmood Aminlari4Younes Ghasemi5Department of Public Health and Food Hygiene, School of Veterinary Medicine, Shiraz University, Shiraz, IranPharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran; and Department of Pharmaceutical Biotechnology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, IranPharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, IranDepartment of Public Health and Food Hygiene, School of Veterinary Medicine, Shiraz University, Shiraz, IranDepartment of Biochemistry, School of Veterinary Medicine, Shiraz University, Shiraz, IranPharmaceutical 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; andDepartment of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, IranBackground: 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.http://ijms.sums.ac.ir/index.php/IJMS/article/view/2225 |
| spellingShingle | Cambyz Irajie Milad Mohkam Navid Nezafat Saeed Hosseinzadeh Mahmood Aminlari Younes Ghasemi In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus Iranian Journal of Medical Sciences |
| title | In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus |
| title_full | In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus |
| title_fullStr | In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus |
| title_full_unstemmed | In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus |
| title_short | In Silico Analysis of Glutaminase from Different Species of Escherichia and Bacillus |
| title_sort | in silico analysis of glutaminase from different species of escherichia and bacillus |
| url | http://ijms.sums.ac.ir/index.php/IJMS/article/view/2225 |
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