Function of Conserved Residues of Human Glutathione Synthetase: Implications for the ATP-grasp Enzymes Metadata

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Title

  • Main Title Function of Conserved Residues of Human Glutathione Synthetase: Implications for the ATP-grasp Enzymes

Creator

  • Author: Dinescu, Adriana
    Creator Type: Personal
    Creator Info: University of North Texas
  • Author: Cundari, Thomas R., 1964-
    Creator Type: Personal
    Creator Info: University of North Texas
  • Author: Bhansali, Vikas S.
    Creator Type: Personal
    Creator Info: University of North Texas
  • Author: Luo, Jia-Li
    Creator Type: Personal
    Creator Info: Hisun Pharmaceutical Co. Ltd.
  • Author: Anderson, Mary E.
    Creator Type: Personal
    Creator Info: Texas Woman's University

Publisher

  • Name: American Society for Biochemistry and Molecular Biology
    Place of Publication: [Rockville, Maryland]

Date

  • Creation: 2004-02-27

Language

  • English

Description

  • Content Description: This article discusses human glutathione synthetase, an enzyme that belongs to the glutathione synthetase ATP-binding domain-like superfamily.
  • Physical Description: 10 p.

Subject

  • Keyword: glutathione synthetase
  • Keyword: enzymes

Source

  • Journal: Journal of Biological Chemistry, 279(21), American Society for Biochemistry and Molecular Biology, February 27, 2004, pp. 1-10

Citation

  • Publication Title: Journal of Biological Chemistry
  • Volume: 279
  • Issue: 21
  • Page Start: 22412
  • Page End: 22421
  • Pages: 10
  • Peer Reviewed: True

Collection

  • Name: UNT Scholarly Works
    Code: UNTSW

Institution

  • Name: UNT College of Arts and Sciences
    Code: UNTCAS

Rights

  • Rights Access: public

Resource Type

  • Article

Format

  • Text

Identifier

  • DOI: 10.1074/jbc.M401334200
  • Archival Resource Key: ark:/67531/metadc75414

Degree

  • Academic Department: Chemistry

Note

  • Display Note: Abstract: Glutathione synthetase is an enzyme that belongs to the glutathione synthetase ATP-binding domain-like superfamily. It catalyzes the second step in the biosynthesis of glutathione from y-glutamylcysteine and glycine in an ATP-dependent manner. Glutathione synthetase has been purified and sequenced from a variety of biological sources; still, its exact mechanism is not fully understood. A variety of structural alignment methods were applied and four highly conserved residues of human glutathione synthetase (Glu-144, Asn-146, Lys-305, and Lys-364) were identified in the binding site. The function of these was studied by experimental and computational site-directed mutagenesis. The three-dimensional coordinates for several human glutathione synthetase mutant enzymes were obtained using molecular mechanics and molecular dynamics simulation techniques, starting from the reported crystal structure of human glutathione synthetase. Consistent with circular dichroism spectroscopy, the authors' results showed no major changes to overall enzyme structure upon residue mutation. However, semiempirical calculations revealed that ligand binding is affected by these mutations. The key interactions between conserved residues and ligands were detected and found to be essential for enzymatic activity. Particularly, the negatively charged Glu-144 residue plays a major role in catalysis.
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