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Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F
Author
Source
Issue
Vol. 2014, Issue 2014 (31 Dec. 2014), pp.1-7, 7 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2014-05-20
Country of Publication
Egypt
No. of Pages
7
Main Subjects
Abstract EN
Molecular dynamics (MD) and metadynamics techniques were used to study the cellulase Cel48F-sugar.
Cellulase is enzyme that breaks cellulose fibers into small sugar units and is potentially useful in second generation alcohol production.
In MD simulations, the overall structure of equilibrated Cel48F did not significantly change along the trajectory, retaining root mean square deviation below 0.15 nm.
A set of 15 residues interacting with the sugar chains via hydrogen bonding throughout the simulation was observed.
The free energy of dissociation (ΔGdiss.) of the chains in the catalytic tunnel of Cel48F was determined by metadynamics.
The ΔGdiss.
values of the chains entering and leaving the wild-type Cel48F cavity were 13.9 and 62.1 kcal/mol, respectively.
We also mutated the E542 and Q543 to alanine residue and obtained ΔGdiss.
of 41.8 and 45.9 kcal/mol, respectively.
These mutations were found to facilitate smooth dissociation of the sugar chain across the Cel48F tunnel.
At the entry of the Cel48F tunnel, three residues were mutated to alanine: T110, T213, and L274.
Contrary to the T110A-Cel48F, the mutants T213-Cel48F and L274-Cel48F prevented the sugar chain from passing across the leaving site.
The present results can be a guideline in mutagenesis studies to improve processing by Cel48F.
American Psychological Association (APA)
Vital de Oliveira, Osmair. 2014. Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F. Enzyme Research،Vol. 2014, no. 2014, pp.1-7.
https://search.emarefa.net/detail/BIM-491035
Modern Language Association (MLA)
Vital de Oliveira, Osmair. Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F. Enzyme Research No. 2014 (2014), pp.1-7.
https://search.emarefa.net/detail/BIM-491035
American Medical Association (AMA)
Vital de Oliveira, Osmair. Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F. Enzyme Research. 2014. Vol. 2014, no. 2014, pp.1-7.
https://search.emarefa.net/detail/BIM-491035
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-491035