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Modeling wild type and mutant glutathione synthetase.

Glutathione syntethase (GS) is an enzyme that belongs to the ATP-grasp superfamily and catalyzes the second step in the biosynthesis of glutathione. GS has been purified and sequenced from a variety of biological sources; still, its exact mechanism is not fully understood. Four highly conserved residues were identified in the binding site of human GS. Additionally, the G-loop residues that close the active site during catalysis were found to be conserved. Since these residues are important for catalysis, their function was studied computationally by site-directed mutagenesis. Starting from the reported crystal structure of human GS, different conformations for the wild type and mutants were obtained using molecular dynamics technique. The key interactions between residues and ligands were detected and found to be essential for enzyme activity.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc5556
Date08 1900
CreatorsDinescu, Adriana
ContributorsCundari, Thomas R., Wilson, Angela K.
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
FormatText
RightsUse restricted to UNT Community (strictly enforced), Copyright, Dinescu, Adriana, Copyright is held by the author, unless otherwise noted. All rights reserved.

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