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...

Full description

Saved in:

Bibliographic Details
Main Author:	Kusnan, Khalida Ain
Format:	Thesis
Language:	English
Published:	2014
Subjects:	Biology
Online Access:	https://ir.uitm.edu.my/id/eprint/26742/2/26742.pdf
Tags:	Add Tag No Tags, Be the first to tag this record!

id	my-uitm-ir.26742
record_format	uketd_dc
spelling	my-uitm-ir.267422024-06-04T07:15:22Z Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan 2014 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 https://ir.uitm.edu.my/id/eprint/26742/ https://ir.uitm.edu.my/id/eprint/26742/2/26742.pdf text en public masters Universiti Teknologi MARA Faculty of Applied Sciences
institution	Universiti Teknologi MARA
collection	UiTM Institutional Repository
language	English
topic	Biology
spellingShingle	Biology Kusnan, Khalida Ain Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan
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).
format	Thesis
qualification_level	Master's degree
author	Kusnan, Khalida Ain
author_facet	Kusnan, Khalida Ain
author_sort	Kusnan, Khalida Ain
title	Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan
title_short	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_sort	characterization of n-acetylglucosaminidase gene from aureus / khalida ain kusnan
granting_institution	Universiti Teknologi MARA
granting_department	Faculty of Applied Sciences
publishDate	2014
url	https://ir.uitm.edu.my/id/eprint/26742/2/26742.pdf
_version_	1804889597216292864

Characterization of N-acetylglucosaminidase gene from aureus / Khalida Ain Kusnan

Similar Items