Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan
SACOL2666, which is known as an N-acetylmuramoyl-L-alanine in NCBI database is shown to be homologuos with atl of S. aureus, a bifunctional autolysin gene. In this study, in-silico analysis of deduced amino acids sequence SACOL2666 was characterized to confirm the protein from S. aureus SHI000 is an...
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| Format: | Thesis |
| Language: | English |
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2014
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| Online Access: | https://ir.uitm.edu.my/id/eprint/26742/1/TM_KHALIDA%20AIN%20KUSNAN%20AS%2014_5.pdf |
| _version_ | 1796902367788007424 |
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| author | Kusnan, Khalida Ain |
| author_facet | Kusnan, Khalida Ain |
| author_sort | Kusnan, Khalida Ain |
| collection | UITM |
| description | SACOL2666, which is known as an N-acetylmuramoyl-L-alanine in NCBI database is shown to be homologuos with atl of S. aureus, a bifunctional autolysin gene. In this study, in-silico analysis of deduced amino acids sequence SACOL2666 was characterized to confirm the protein from S. aureus SHI000 is an Nacetylglucosaminidase autolysin. Successful transformed gene in pBAD-sScaB and pQE60-xScaQ clones contain 1860 bp of the full gene and 1779 bp of gene without signal peptide sequence. An N-acetylglucosaminidase protein family (PF01832) of Lysozyme like superfamily is found in SACOL2666 domain architecture. The amino acid of SACOL2666 gene demonstrated a high sequence similarity to characterized N-acetylglucosaminidases, AcmB (L. lactis) and Auto (L. monocytogenes) Group B in GH73 rather than bifunctional autolysins in Group A, Atl (S. aureus). SACOL2666 has high relatedness in sequence similarity (46%) and structural alignment with N-acetylglucosaminidases Auto Chain A structure (3FI7 A). Residue E352, G356, E386, F399, Y455 and a tetrad YATD (Y449-D452) at SACOL2666 hypothetical secondary structures are shown to be identical to Auto (3FI7_A) residues. As conclusion, this study reveals SACOL2666 as a novel N-acetylglucosaminidase with high sequence similarity to N-acetylglucosaminidases in Group B of GH73. Moreover, structural similarity suggests the functional and enzymatic activity of SACOL2666 is similar to Auto (3FI7 A). |
| first_indexed | 2024-03-06T02:03:55Z |
| format | Thesis |
| id | uitm.eprints-6742 |
| institution | Universiti Teknologi MARA |
| language | English |
| last_indexed | 2024-03-06T02:03:55Z |
| publishDate | 2014 |
| record_format | dspace |
| spelling | uitm.eprints-67422019-12-04T02:38:02Z https://ir.uitm.edu.my/id/eprint/26742/ Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan Kusnan, Khalida Ain Biology SACOL2666, which is known as an N-acetylmuramoyl-L-alanine in NCBI database is shown to be homologuos with atl of S. aureus, a bifunctional autolysin gene. In this study, in-silico analysis of deduced amino acids sequence SACOL2666 was characterized to confirm the protein from S. aureus SHI000 is an Nacetylglucosaminidase autolysin. Successful transformed gene in pBAD-sScaB and pQE60-xScaQ clones contain 1860 bp of the full gene and 1779 bp of gene without signal peptide sequence. An N-acetylglucosaminidase protein family (PF01832) of Lysozyme like superfamily is found in SACOL2666 domain architecture. The amino acid of SACOL2666 gene demonstrated a high sequence similarity to characterized N-acetylglucosaminidases, AcmB (L. lactis) and Auto (L. monocytogenes) Group B in GH73 rather than bifunctional autolysins in Group A, Atl (S. aureus). SACOL2666 has high relatedness in sequence similarity (46%) and structural alignment with N-acetylglucosaminidases Auto Chain A structure (3FI7 A). Residue E352, G356, E386, F399, Y455 and a tetrad YATD (Y449-D452) at SACOL2666 hypothetical secondary structures are shown to be identical to Auto (3FI7_A) residues. As conclusion, this study reveals SACOL2666 as a novel N-acetylglucosaminidase with high sequence similarity to N-acetylglucosaminidases in Group B of GH73. Moreover, structural similarity suggests the functional and enzymatic activity of SACOL2666 is similar to Auto (3FI7 A). 2014 Thesis NonPeerReviewed text en https://ir.uitm.edu.my/id/eprint/26742/1/TM_KHALIDA%20AIN%20KUSNAN%20AS%2014_5.pdf Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan. (2014) Masters thesis, thesis, Universiti Teknologi MARA. <http://terminalib.uitm.edu.my/26742.pdf> |
| spellingShingle | Biology Kusnan, Khalida Ain Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan |
| title | Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan |
| title_full | Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan |
| title_fullStr | Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan |
| title_full_unstemmed | Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan |
| title_short | Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan |
| title_sort | characterization of n acetylglucosaminidase gene from aureus khalida ain kusnan |
| topic | Biology |
| url | https://ir.uitm.edu.my/id/eprint/26742/1/TM_KHALIDA%20AIN%20KUSNAN%20AS%2014_5.pdf |
| work_keys_str_mv | AT kusnankhalidaain characterizationofnacetylglucosaminidasegenefromaureuskhalidaainkusnan |