Deciphering the Flexibility and Dynamics of Geobacillus zalihae Strain T1 Lipase at High Temperatures by Molecular Dynamics Simulation

Title: Deciphering the Flexibility and Dynamics of Geobacillus zalihae Strain T1 Lipase at High Temperatures by Molecular Dynamics Simulation

Volume: 16 Issue: 11

Author(s): Mohd Basyaruddin Abdul Rahman, Roghayeh Abedi Karjiban, Abu Bakar Salleh, Donald Jacobs, Mahiran Basri, Adam Leow Thean Chor, Habibah Abdul Wahab and Raja Noor Zaliha Raja Abd Rahman

Affiliation:

Keywords: Thermostability, thermoalkalophilic enzyme, lipase, protein dynamics, flexibility

Abstract: 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 α3 and α5, strands β1 and β2, and connecting loops) and the main catalytic domain or core domain (consisting of helices α6- α9 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.

Cite this article as:

Abdul Rahman Basyaruddin Mohd, Karjiban Abedi Roghayeh, Salleh Bakar Abu, Jacobs Donald, Basri Mahiran, Thean Chor Leow Adam, Wahab Abdul Habibah and Abd Rahman Zaliha Raja Raja Noor, Deciphering the Flexibility and Dynamics of Geobacillus zalihae Strain T1 Lipase at High Temperatures by Molecular Dynamics Simulation, Protein & Peptide Letters 2009; 16 (11) . https://dx.doi.org/10.2174/092986609789353763