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Deciphering the flexibility and dynamics of Geobacillus zalihae strain T1 lipase at high temperatures by molecular dynamics simulation


Citation

Abdul Rahman, Mohd Basyaruddin and Karjiban, Roghayeh Abedi and Salleh, Abu Bakar and Jacobs, Donald and Basri, Mahiran and Leow, Adam Thean Chor and Abdul Wahab, Habibah and Raja Abdul Rahman, Raja Noor Zaliha (2009) Deciphering the flexibility and dynamics of Geobacillus zalihae strain T1 lipase at high temperatures by molecular dynamics simulation. Protein & Peptide Letters, 16 (11). pp. 1360-1370. ISSN 0929-8665; ESSN: 1875-5305

Abstract / Synopsis

The stability of biocatalysts is an important criterion for a sustainable industrial operation economically. T1 lipase is a thermoalkalophilic enzyme derived from Geobacillus zalihae strain T1 (T1 lipase) that was isolated from palm oil mill effluent (POME) in Malaysia. We report here the results of high temperatures molecular dynamics (MD) simulations of T1 lipase in explicit solvent. We found that the N-terminal moiety of this enzyme was accompanied by a large flexibility and dynamics during temperature-induced unfolding simulations which preceded and followed by clear structural changes in two specific regions; the small domain (consisting of helices alpha3 and alpha5, strands beta1 and beta2, and connecting loops) and the main catalytic domain or core domain (consisting of helices alpha6- alpha9 and connecting loops which located above the active site) of the enzyme. The results suggest that the small domain of model enzyme is a critical region to the thermostability of this organism.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science
Institute of Bioscience
DOI Number: https://doi.org/10.2174/092986609789353763
Publisher: Bentham Science Publishers
Keywords: Thermostability; Thermoalkalophilic enzyme; Lipase; Protein dynamics; Flexibility
Depositing User: Nida Hidayati Ghazali
Date Deposited: 15 Aug 2012 15:25
Last Modified: 02 Sep 2016 12:54
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.2174/092986609789353763
URI: http://psasir.upm.edu.my/id/eprint/13871
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