Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima

The enzyme β-Glucuronidases (GUS) which belongs to the glycoside hydrolase family of enzymes, can hydrolyze any aglycne conjugated to D-glucuronic acid through a β-O~glycosidic linkage. It is present in almost all tissues of vertebrates and their residentinal flora, including E. coli. However, GUS e...

Full description

Bibliographic Details
Main Authors:	Noorbatcha, Ibrahim Ali, Masrur Khan, Ayesha, Mohd. Salleh, Hamzah
Format:	Article
Language:	English
Published:	Universiti Malaya 2009
Subjects:	QP Physiology
Online Access:	http://irep.iium.edu.my/782/ http://irep.iium.edu.my/782/ http://irep.iium.edu.my/782/1/Homology_Modeling_of_B-Glucuronidases_From_E._Coli_and_T._Maritima.pdf

id	iium-782
recordtype	eprints
spelling	iium-7822011-11-16T02:22:59Z http://irep.iium.edu.my/782/ Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima Noorbatcha, Ibrahim Ali Masrur Khan, Ayesha Mohd. Salleh, Hamzah QP Physiology The enzyme β-Glucuronidases (GUS) which belongs to the glycoside hydrolase family of enzymes, can hydrolyze any aglycne conjugated to D-glucuronic acid through a β-O~glycosidic linkage. It is present in almost all tissues of vertebrates and their residentinal flora, including E. coli. However, GUS enzymes obtained from different sources have different stability towards heat, resistance to detergents and varying catalytic activities. A good understanding or the reasons for this variation can lead to designing new enzymes with desired level of property. having great prospect in the industry. For this purpose, studies on the three-dimensional structure of GUS enzyme can offer insights on the structure-function correlations, and provide information on the distribution or certain residues both in E. coli and T. maritima enzymes. The structures of GUS enzymes from E. coli and T. maritima are not known experimentally. As such in the current work, homology modeling or the three-dimensional structure of both variants of the GUS enzyme was carried out based on the solved crystal structure of Human GUS enzyme. Multiple sequence alignment for both enzyme sequences was carried out in order to locate the most suitable template for homology modeling and the models thus prepared were found to cotain 32-43% sequence identity with the template. Superposition of the model obtained with the template as well as structural alignment were carried out to classify the structural differences. This paper will also present an analysis and verification studies of the model based on various criteria. The current work offers a better understanding of the structural differences between GUS enzymes from different sources, as well as suggests regions for further modification using experimental and computational methods. Universiti Malaya 2009 Article PeerReviewed application/pdf en http://irep.iium.edu.my/782/1/Homology_Modeling_of_B-Glucuronidases_From_E._Coli_and_T._Maritima.pdf Noorbatcha, Ibrahim Ali and Masrur Khan, Ayesha and Mohd. Salleh, Hamzah (2009) Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima. Malaysian Journal os Science, 28. pp. 115-122. ISSN 1394-3065 http://ejum.fsktm.um.edu.my/VolumeListing.aspx?JournalID=11
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	QP Physiology
spellingShingle	QP Physiology Noorbatcha, Ibrahim Ali Masrur Khan, Ayesha Mohd. Salleh, Hamzah Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima
description	The enzyme β-Glucuronidases (GUS) which belongs to the glycoside hydrolase family of enzymes, can hydrolyze any aglycne conjugated to D-glucuronic acid through a β-O~glycosidic linkage. It is present in almost all tissues of vertebrates and their residentinal flora, including E. coli. However, GUS enzymes obtained from different sources have different stability towards heat, resistance to detergents and varying catalytic activities. A good understanding or the reasons for this variation can lead to designing new enzymes with desired level of property. having great prospect in the industry. For this purpose, studies on the three-dimensional structure of GUS enzyme can offer insights on the structure-function correlations, and provide information on the distribution or certain residues both in E. coli and T. maritima enzymes. The structures of GUS enzymes from E. coli and T. maritima are not known experimentally. As such in the current work, homology modeling or the three-dimensional structure of both variants of the GUS enzyme was carried out based on the solved crystal structure of Human GUS enzyme. Multiple sequence alignment for both enzyme sequences was carried out in order to locate the most suitable template for homology modeling and the models thus prepared were found to cotain 32-43% sequence identity with the template. Superposition of the model obtained with the template as well as structural alignment were carried out to classify the structural differences. This paper will also present an analysis and verification studies of the model based on various criteria. The current work offers a better understanding of the structural differences between GUS enzymes from different sources, as well as suggests regions for further modification using experimental and computational methods.
format	Article
author	Noorbatcha, Ibrahim Ali Masrur Khan, Ayesha Mohd. Salleh, Hamzah
author_facet	Noorbatcha, Ibrahim Ali Masrur Khan, Ayesha Mohd. Salleh, Hamzah
author_sort	Noorbatcha, Ibrahim Ali
title	Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima
title_short	Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima
title_full	Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima
title_fullStr	Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima
title_full_unstemmed	Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima
title_sort	homology modeling of β-glucuronidases from e. coli and t. maritima
publisher	Universiti Malaya
publishDate	2009
url	http://irep.iium.edu.my/782/ http://irep.iium.edu.my/782/ http://irep.iium.edu.my/782/1/Homology_Modeling_of_B-Glucuronidases_From_E._Coli_and_T._Maritima.pdf
first_indexed	2023-09-18T20:07:56Z
last_indexed	2023-09-18T20:07:56Z
_version_	1777407283751288832

Homology Modeling Of β-Glucuronidases From E. Coli and T. Maritima

Similar Items