Abstract
Fumarase enzyme is known to catalyse the stereo specific inter conversion of fumarate to L-malate which is a part of the Krebs cycle. Despite the biological significance and importance of this enzyme, the reaction mechanism of fumarase is not completely understood or known. In this context an experiment on molecular dynamics simulation was carried out for at least 10 nanoseconds molecular dynamics simulation run using Nano Scale Molecular Dynamics program implemented in Discovery Studio 4.0. The trajectory analysis of various energy parameters revealed the thermo dynamical stability of the enzyme. The present findings may aid in understanding the biological significance of this enzyme.
Highlights
Fumarase enzyme catalyses the stereo specific inter conversion of fumarate to L-malate as part of the metabolic citric acid or Krebs cycle [1]
In an attempt to understand the actual mechanism of the enzyme, a molecular dynamics simulation experiment was designed which may provide the insights of the thermo dynamical behaviour
The molecular dynamics simulation (MD) was performed to understand the stability of the enzyme in various energy related behaviors to understand its thermodynamic behaviours which might contribute in the stability of the enzyme [8]
Summary
Fumarase enzyme catalyses the stereo specific inter conversion of fumarate to L-malate as part of the metabolic citric acid or Krebs cycle [1]. The recent three-dimensional structure of the fumarase C of Escherichia coli has identified a binding site for anions which is generated by side chains from three of the four subunits within the tetramer [2].
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