Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina

The efficacy of β-1,4-glucosidase enzyme produced by Trichoderma harzianum in disrupting phytopathogenic fungus, Macrophomina phaseolina had been studied and recorded. Meanwhile, the molecular mechanisms underlying the cell wall components of M. phaseolina recognition remain elusive. Molecular docki...

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Main Authors:	Mohammad Hood, Mohammad Hakim, Abdul Wahab, Roswanira, Tengku Abdul Hamid, Tengku Haziyamin, Abdul Hamid, Azzmer Azzar
Format:	Conference or Workshop Item
Language:	English
Published:	2019
Subjects:	QR Microbiology
Online Access:	http://irep.iium.edu.my/72129/ http://irep.iium.edu.my/72129/ http://irep.iium.edu.my/72129/1/72129_Molecular%20Docking%20Analysis%20of%20%CE%B2-1%2C4-Glucosidase.pdf

id	iium-72129
recordtype	eprints
spelling	iium-721292019-05-14T07:28:50Z http://irep.iium.edu.my/72129/ Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina Mohammad Hood, Mohammad Hakim Abdul Wahab, Roswanira Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar QR Microbiology The efficacy of β-1,4-glucosidase enzyme produced by Trichoderma harzianum in disrupting phytopathogenic fungus, Macrophomina phaseolina had been studied and recorded. Meanwhile, the molecular mechanisms underlying the cell wall components of M. phaseolina recognition remain elusive. Molecular docking was done using Autodock Vina 1.1.2 program to determine the binding location, and interactions formed between β-glucan and chitin with the residues of β-glucosidase. Docking simulation was done in two means, blind docking and specific docking which assigned the enzyme to be rigid with flexible ligands. The search space for specific binding was determined from the residues predicted by COACH tool. Respectively, the blind docking of chitin and of β-glucan showed binding affinity of -8.1 kcal/mol and -7.8 kcal/mol while in specific docking showed -7.8 kcal/mol and -7.7 kcal/mol. The low binding affinity indicated the binding between β-glucosidase and the ligands was favourable. Several residues were found in consensus to form up the pocket of active site. These include Ser183, Thr185, Phe186, Asn231, Phe256, Trp345, Glu373, Glu430 and Trp431. Glu373 was found to constantly form hydrogen bond with both ligands as this residue could be the nucleophile for hydrolysis. Hence, this finding provides a fundamental basis for improving biological agent in inhibiting the growth of the phytopathogenic fungus. 2019-04-11 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/72129/1/72129_Molecular%20Docking%20Analysis%20of%20%CE%B2-1%2C4-Glucosidase.pdf Mohammad Hood, Mohammad Hakim and Abdul Wahab, Roswanira and Tengku Abdul Hamid, Tengku Haziyamin and Abdul Hamid, Azzmer Azzar (2019) Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina. In: 2nd International Conference on Biosciences and Medical Engineering (ICBME) 2019, 11th-12th April 2019, Bali, Indonesia. http://icbme.fbme.utm.my/
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	QR Microbiology
spellingShingle	QR Microbiology Mohammad Hood, Mohammad Hakim Abdul Wahab, Roswanira Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
description	The efficacy of β-1,4-glucosidase enzyme produced by Trichoderma harzianum in disrupting phytopathogenic fungus, Macrophomina phaseolina had been studied and recorded. Meanwhile, the molecular mechanisms underlying the cell wall components of M. phaseolina recognition remain elusive. Molecular docking was done using Autodock Vina 1.1.2 program to determine the binding location, and interactions formed between β-glucan and chitin with the residues of β-glucosidase. Docking simulation was done in two means, blind docking and specific docking which assigned the enzyme to be rigid with flexible ligands. The search space for specific binding was determined from the residues predicted by COACH tool. Respectively, the blind docking of chitin and of β-glucan showed binding affinity of -8.1 kcal/mol and -7.8 kcal/mol while in specific docking showed -7.8 kcal/mol and -7.7 kcal/mol. The low binding affinity indicated the binding between β-glucosidase and the ligands was favourable. Several residues were found in consensus to form up the pocket of active site. These include Ser183, Thr185, Phe186, Asn231, Phe256, Trp345, Glu373, Glu430 and Trp431. Glu373 was found to constantly form hydrogen bond with both ligands as this residue could be the nucleophile for hydrolysis. Hence, this finding provides a fundamental basis for improving biological agent in inhibiting the growth of the phytopathogenic fungus.
format	Conference or Workshop Item
author	Mohammad Hood, Mohammad Hakim Abdul Wahab, Roswanira Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar
author_facet	Mohammad Hood, Mohammad Hakim Abdul Wahab, Roswanira Tengku Abdul Hamid, Tengku Haziyamin Abdul Hamid, Azzmer Azzar
author_sort	Mohammad Hood, Mohammad Hakim
title	Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
title_short	Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
title_full	Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
title_fullStr	Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
title_full_unstemmed	Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
title_sort	molecular docking analysis of β-1,4-glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina
publishDate	2019
url	http://irep.iium.edu.my/72129/ http://irep.iium.edu.my/72129/ http://irep.iium.edu.my/72129/1/72129_Molecular%20Docking%20Analysis%20of%20%CE%B2-1%2C4-Glucosidase.pdf
first_indexed	2023-09-18T21:42:15Z
last_indexed	2023-09-18T21:42:15Z
_version_	1777413217897676800

Molecular docking analysis of β-1,4-Glucosidase from trichoderma harzianum against mycelial cell wall components of macrophomina phaseolina

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