Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum

Endoglucanase is one of the three enzymes required to synergistically hydrolyze cellulose to sugar monomers which can be fermented into ethanol. Hence efforts to improve the efficiency of this enzyme, using experimental and computational approaches have been continuing vigorously. An endoglucanase,...

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Main Authors:	Ibrahim Ali, Noorbatcha, Hamzah, Mohd. Salleh
Format:	Article
Language:	English English
Published:	Journal of Pure and Applied Microbiology 2014
Subjects:	TP Chemical technology TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/38311/ http://irep.iium.edu.my/38311/ http://irep.iium.edu.my/38311/1/Molec_Dock_Endogulc_JPAM_791-796_2014.pdf http://irep.iium.edu.my/38311/3/38311_Molecular%20docking%20of%20cellobiose%20and%20cellotetraose_SCOPUS.pdf

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recordtype	eprints
spelling	iium-383112017-09-25T10:16:33Z http://irep.iium.edu.my/38311/ Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum Ibrahim Ali, Noorbatcha Hamzah, Mohd. Salleh TP Chemical technology TP248.13 Biotechnology Endoglucanase is one of the three enzymes required to synergistically hydrolyze cellulose to sugar monomers which can be fermented into ethanol. Hence efforts to improve the efficiency of this enzyme, using experimental and computational approaches have been continuing vigorously. An endoglucanase, FOegI, which is same as the wellcharacterized endoglucanase I from Fusarium oxysporum (PDB ID: 3OVW) has been cloned into an appropriate expression vector, except for two mutations. As an attempt to improve the substrate binding characteristics of FOegI, computational molecular docking studies to understand the interactions in the active site regions and to suggest mutations to improve the binding characteristics was carried out in this study. The docking of ligands into active site was carried out using Lamarkian Genetic Algorithm with a fast, simplified potential of mean force (PMF) to evaluate the docking efficiency. The two substrate used in this study are cellobiose and cellotetraose. The active site is confirmed by comparing the docked structure with the available experimental structures. Cellotetraose was found to have stronger binding than cellobiose. Among the three in silico mutants tested, T224E is found to have the strongest binding energy of -530.72 +0.85with cellotetraose. Journal of Pure and Applied Microbiology 2014-05 Article PeerReviewed application/pdf en http://irep.iium.edu.my/38311/1/Molec_Dock_Endogulc_JPAM_791-796_2014.pdf application/pdf en http://irep.iium.edu.my/38311/3/38311_Molecular%20docking%20of%20cellobiose%20and%20cellotetraose_SCOPUS.pdf Ibrahim Ali, Noorbatcha and Hamzah, Mohd. Salleh (2014) Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum. Journal of Pure and Applied Microbiology, 8 (s.ed 1). pp. 791-796. ISSN 0973-7510 http://www.miocrobiologyjournals.org
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English
topic	TP Chemical technology TP248.13 Biotechnology
spellingShingle	TP Chemical technology TP248.13 Biotechnology Ibrahim Ali, Noorbatcha Hamzah, Mohd. Salleh Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
description	Endoglucanase is one of the three enzymes required to synergistically hydrolyze cellulose to sugar monomers which can be fermented into ethanol. Hence efforts to improve the efficiency of this enzyme, using experimental and computational approaches have been continuing vigorously. An endoglucanase, FOegI, which is same as the wellcharacterized endoglucanase I from Fusarium oxysporum (PDB ID: 3OVW) has been cloned into an appropriate expression vector, except for two mutations. As an attempt to improve the substrate binding characteristics of FOegI, computational molecular docking studies to understand the interactions in the active site regions and to suggest mutations to improve the binding characteristics was carried out in this study. The docking of ligands into active site was carried out using Lamarkian Genetic Algorithm with a fast, simplified potential of mean force (PMF) to evaluate the docking efficiency. The two substrate used in this study are cellobiose and cellotetraose. The active site is confirmed by comparing the docked structure with the available experimental structures. Cellotetraose was found to have stronger binding than cellobiose. Among the three in silico mutants tested, T224E is found to have the strongest binding energy of -530.72 +0.85with cellotetraose.
format	Article
author	Ibrahim Ali, Noorbatcha Hamzah, Mohd. Salleh
author_facet	Ibrahim Ali, Noorbatcha Hamzah, Mohd. Salleh
author_sort	Ibrahim Ali, Noorbatcha
title	Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
title_short	Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
title_full	Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
title_fullStr	Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
title_full_unstemmed	Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
title_sort	molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum
publisher	Journal of Pure and Applied Microbiology
publishDate	2014
url	http://irep.iium.edu.my/38311/ http://irep.iium.edu.my/38311/ http://irep.iium.edu.my/38311/1/Molec_Dock_Endogulc_JPAM_791-796_2014.pdf http://irep.iium.edu.my/38311/3/38311_Molecular%20docking%20of%20cellobiose%20and%20cellotetraose_SCOPUS.pdf
first_indexed	2023-09-18T20:55:01Z
last_indexed	2023-09-18T20:55:01Z
_version_	1777410246654820352

Molecular docking of cellobiose and cellotetraose into an endoglucanase from fusarium oxysporum

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