Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases
Homology modeling is a powerful tool in predicting the three dimensional (3D) structure of a protein using a solved structure within the same family as template. Compared to other methods such as X-ray crystallography and NMR, homology modelling has the advantage of being a fast yet reliable techniq...
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| Format: | Article |
| Language: | English |
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Research Journal of Chemistry and Environment
2010
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| Online Access: | http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/1/Homology_Modelling_and_Struct_318-323.pdf |
| _version_ | 1848775996967223296 |
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| author | Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah |
| author_facet | Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah |
| author_sort | Noorbatcha, Ibrahim Ali |
| building | IIUM Repository |
| collection | Online Access |
| description | Homology modeling is a powerful tool in predicting the three dimensional (3D) structure of a protein using a solved structure within the same family as template. Compared to other methods such as X-ray crystallography and NMR, homology modelling has the advantage of being a fast yet reliable technique in solving proteins’ 3D structures,
starting from their amino acid sequences. In this study, homology modelling was used to obtain the 3D structure of two different phytases using only their amino acid sequence; phyFAUIA1_H which belongs to the histidine acid phosphatases and Bacillus subtilis ASUIA243 which belongs to the β-propeller phytases. E. coli phytase (PDB code 1dkm) was used as a template for phyFAUIA1_H model with 99.512% sequence identity.
On the other hand, Bacillus amyloliquefaciens (PDB code 2poo) was used as a template for B. subtilis ASUIA243 model with 71.268% sequence identity. Both models were evaluated and found to be quite satisfactory without being manually modified. These models can now be used in protein structural
studies to improve properties such as specific activity,
pH tolerance and thermostability. |
| first_indexed | 2025-11-14T14:23:05Z |
| format | Article |
| id | iium-2365 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T14:23:05Z |
| publishDate | 2010 |
| publisher | Research Journal of Chemistry and Environment |
| recordtype | eprints |
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| spelling | iium-23652021-07-06T02:01:40Z http://irep.iium.edu.my/2365/ Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah QD Chemistry Homology modeling is a powerful tool in predicting the three dimensional (3D) structure of a protein using a solved structure within the same family as template. Compared to other methods such as X-ray crystallography and NMR, homology modelling has the advantage of being a fast yet reliable technique in solving proteins’ 3D structures, starting from their amino acid sequences. In this study, homology modelling was used to obtain the 3D structure of two different phytases using only their amino acid sequence; phyFAUIA1_H which belongs to the histidine acid phosphatases and Bacillus subtilis ASUIA243 which belongs to the β-propeller phytases. E. coli phytase (PDB code 1dkm) was used as a template for phyFAUIA1_H model with 99.512% sequence identity. On the other hand, Bacillus amyloliquefaciens (PDB code 2poo) was used as a template for B. subtilis ASUIA243 model with 71.268% sequence identity. Both models were evaluated and found to be quite satisfactory without being manually modified. These models can now be used in protein structural studies to improve properties such as specific activity, pH tolerance and thermostability. Research Journal of Chemistry and Environment 2010-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/2365/1/Homology_Modelling_and_Struct_318-323.pdf Noorbatcha, Ibrahim Ali and Sultan, Anas Mufid Nasri and Amid, Azura and Mohd. Salleh, Hamzah (2010) Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases. Research Journal of Chemistry and Environment, Specil (issue). pp. 318-323. ISSN 0972-0626 http://www.chemenviron.net/RJCE/RJCE/right.htm |
| spellingShingle | QD Chemistry Noorbatcha, Ibrahim Ali Sultan, Anas Mufid Nasri Amid, Azura Mohd. Salleh, Hamzah Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases |
| title | Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases |
| title_full | Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases |
| title_fullStr | Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases |
| title_full_unstemmed | Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases |
| title_short | Homology modelling and structural analysis of phyFAUIA1_H and Bacillus subtilis ASUIA243 phytases |
| title_sort | homology modelling and structural analysis of phyfauia1_h and bacillus subtilis asuia243 phytases |
| topic | QD Chemistry |
| url | http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/ http://irep.iium.edu.my/2365/1/Homology_Modelling_and_Struct_318-323.pdf |