Modeling wild type and mutant glutathione synthetase.

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Description:

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.

Creator(s): Dinescu, Adriana
Creation Date: August 2004
Partner(s):
UNT Libraries
Collection(s):
UNT Theses and Dissertations
Usage:
Total Uses: 43
Past 30 days: 2
Yesterday: 0
Creator (Author):
Publisher Info:
Publisher Name: University of North Texas
Place of Publication: Denton, Texas
Date(s):
  • Creation: August 2004
  • Digitized: November 26, 2007
Description:

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.

Degree:
Level: Master's
Discipline: Inorganic Chemistry
Language(s):
Subject(s):
Keyword(s): ATP-grasp proteins | molecular dynamics | computational chemistry | GSH | hGS
Contributor(s):
Partner:
UNT Libraries
Collection:
UNT Theses and Dissertations
Identifier:
  • OCLC: 56612932 |
  • ARK: ark:/67531/metadc5556
Resource Type: Thesis or Dissertation
Format: Text
Rights:
Access: Use restricted to UNT Community (strictly enforced)
License: Copyright
Holder: Dinescu, Adriana
Statement: Copyright is held by the author, unless otherwise noted. All rights reserved.