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The role of Arg157Ser in improving the compactness and stability of ARM lipase

Consensus approach is an efficient strategy to identify hot residue important for compactness and stability of protein. Structure of ARM lipase was modeled to explore the possible effect of critical point mutation towards structure and function. The significant difference of amino acid at position 1...

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Main Authors: Salleh, Abu Bakar, Abd Rahim, Arilla Sri Masayu, Raja Abdul Rahman, Raja Noor Zaliha, Leow, Thean Chor, Basri, Mahiran
Format: Article
Language:English
Published: Omics Publishing Group 2012
Online Access:http://psasir.upm.edu.my/id/eprint/22420/1/The%20Role%20of%20Arg157Ser%20in%20Improving%20the%20Compactness%20and%20Stability%20of.pdf
http://psasir.upm.edu.my/id/eprint/22420/
http://www.omicsonline.org/computer-science-systems-biology-abstract.php?abstract_id=5559
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spelling my.upm.eprints.224202016-09-27T01:11:07Z http://psasir.upm.edu.my/id/eprint/22420/ The role of Arg157Ser in improving the compactness and stability of ARM lipase Salleh, Abu Bakar Abd Rahim, Arilla Sri Masayu Raja Abdul Rahman, Raja Noor Zaliha Leow, Thean Chor Basri, Mahiran Consensus approach is an efficient strategy to identify hot residue important for compactness and stability of protein. Structure of ARM lipase was modeled to explore the possible effect of critical point mutation towards structure and function. The significant difference of amino acid at position 157 between ARM lipase (Arg157) and other thermostable lipases (Ser157) was targeted as a critical residue. Using YASARA software, Arg157 was substituted to Ser and subsequently the energy minimized. Both ARM and R157S lipases were analyzed by MD simulations at different temperatures (50ºC,60ºC, and 70ºC). MD simulation result showed that R157S lipase had lower value of RMSD, RMSF, solvent accessible surface area (SASA) and radius of gyration than native ARM lipase. It indicated that R157S lipase had higher compactness in the structure leading to enhanced stability. To validate the computational data, the substitution of Arg157 to Ser has been conducted using site-directed mutagenesis experimentally. The catalytic efficiency (kcat/KM) of R157S lipase was refold better than ARM lipase of 70°C. Circular dichorism study revealed that R157S lipase had increased thermostability with higher Tm value (71.6°C) than its wildtype (63.9°C) indicating a better compactness as revealed by spectrofluorocence study. Thus the rational design of substituting Arg157 with Ser improved the protein folding of mutant lipase as shown in MD simulations and subsequently increased the catalytic effectiveness and thermodynamic stability. Omics Publishing Group 2012-09 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22420/1/The%20Role%20of%20Arg157Ser%20in%20Improving%20the%20Compactness%20and%20Stability%20of.pdf Salleh, Abu Bakar and Abd Rahim, Arilla Sri Masayu and Raja Abdul Rahman, Raja Noor Zaliha and Leow, Thean Chor and Basri, Mahiran (2012) The role of Arg157Ser in improving the compactness and stability of ARM lipase. Journal of Computer Science & Systems Biology, 5 (2). pp. 39-46. ISSN 0974-7230 http://www.omicsonline.org/computer-science-systems-biology-abstract.php?abstract_id=5559 10.4172/jcsb.1000088
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description Consensus approach is an efficient strategy to identify hot residue important for compactness and stability of protein. Structure of ARM lipase was modeled to explore the possible effect of critical point mutation towards structure and function. The significant difference of amino acid at position 157 between ARM lipase (Arg157) and other thermostable lipases (Ser157) was targeted as a critical residue. Using YASARA software, Arg157 was substituted to Ser and subsequently the energy minimized. Both ARM and R157S lipases were analyzed by MD simulations at different temperatures (50ºC,60ºC, and 70ºC). MD simulation result showed that R157S lipase had lower value of RMSD, RMSF, solvent accessible surface area (SASA) and radius of gyration than native ARM lipase. It indicated that R157S lipase had higher compactness in the structure leading to enhanced stability. To validate the computational data, the substitution of Arg157 to Ser has been conducted using site-directed mutagenesis experimentally. The catalytic efficiency (kcat/KM) of R157S lipase was refold better than ARM lipase of 70°C. Circular dichorism study revealed that R157S lipase had increased thermostability with higher Tm value (71.6°C) than its wildtype (63.9°C) indicating a better compactness as revealed by spectrofluorocence study. Thus the rational design of substituting Arg157 with Ser improved the protein folding of mutant lipase as shown in MD simulations and subsequently increased the catalytic effectiveness and thermodynamic stability.
format Article
author Salleh, Abu Bakar
Abd Rahim, Arilla Sri Masayu
Raja Abdul Rahman, Raja Noor Zaliha
Leow, Thean Chor
Basri, Mahiran
spellingShingle Salleh, Abu Bakar
Abd Rahim, Arilla Sri Masayu
Raja Abdul Rahman, Raja Noor Zaliha
Leow, Thean Chor
Basri, Mahiran
The role of Arg157Ser in improving the compactness and stability of ARM lipase
author_facet Salleh, Abu Bakar
Abd Rahim, Arilla Sri Masayu
Raja Abdul Rahman, Raja Noor Zaliha
Leow, Thean Chor
Basri, Mahiran
author_sort Salleh, Abu Bakar
title The role of Arg157Ser in improving the compactness and stability of ARM lipase
title_short The role of Arg157Ser in improving the compactness and stability of ARM lipase
title_full The role of Arg157Ser in improving the compactness and stability of ARM lipase
title_fullStr The role of Arg157Ser in improving the compactness and stability of ARM lipase
title_full_unstemmed The role of Arg157Ser in improving the compactness and stability of ARM lipase
title_sort role of arg157ser in improving the compactness and stability of arm lipase
publisher Omics Publishing Group
publishDate 2012
url http://psasir.upm.edu.my/id/eprint/22420/1/The%20Role%20of%20Arg157Ser%20in%20Improving%20the%20Compactness%20and%20Stability%20of.pdf
http://psasir.upm.edu.my/id/eprint/22420/
http://www.omicsonline.org/computer-science-systems-biology-abstract.php?abstract_id=5559
_version_ 1643827822000603136
score 13.211869

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