Valine 44 and Valine 45 of Human Glutiathione Sythetase are Key for Subunit Stability and Negative Cooperativity

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Article discussing Valine 44 and Valine 45 of human glutathione synthetase as the key for subunit stability and negative cooperativity.

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13 p.

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Slavens, Kerri D.; Brown, Teresa R.; Barakat, Khaldoon A.; Cundari, Thomas R., 1964- & Anderson, Mary E. Creation Date: Unknown.

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Article discussing Valine 44 and Valine 45 of human glutathione synthetase as the key for subunit stability and negative cooperativity.

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13 p.

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This is the accepted manuscript version of the article. Reprinted with permission from Elsevier Science Ltd., all rights reserved. The final definitive version is available here: http://www.sciencedirect.com/science/article/pii/S0006291X11009922

Abstract: It was hypothesized that residues Val44 and Val45 serve as important residues for human glutathione synthetase (hGS) function and stability given their location at the dimer interface of this enzyme. Computational studies suggest that mutation at Val45 has more impact on the structure and stability of hGS than does mutation at Val44. Experimentally, enzymes with mutations at the 44 and or 45 positions of hGS were prepared, purified and assayed for initial activity. Val45 position mutations (either to alanine or tryptophan) have a greater impact on enzyme activity than do mutations at Val44. Differential scanning calorimetry experiments reveal a loss of stability in all mutant enzymes, with V45 mutations being less stable than the corresponding Val44 mutations. The γ-GluABA substrate affinity remains unaltered in V44A and V45A mutant enzymes, but increases when tryptophan is introduced at either of these positions. Hill coefficients trend towards less negative cooperativity with the exception of V45W mutant hGS. These results imply that residues V44 and V45 are located along the allosteric pathway more than it does the active site of hGS, and that these residues (and by extension the dimer interface in which they are located) are integral to the stability of human glutathione sythetase.

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  • Biochemical and Biophysical Research Communications, 2011, Amsterdam: Elsevier Science Ltd., pp. 597-601

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  • Publication Title: Biochemical and Biophysical Research Communications
  • Volume: 410
  • Issue: 3
  • Page Start: 597
  • Page End: 601
  • Peer Reviewed: Yes

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  • Unknown

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  • July 8, 2011

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  • Sept. 6, 2013, 3:22 p.m.

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  • May 27, 2014, 4:17 p.m.

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Slavens, Kerri D.; Brown, Teresa R.; Barakat, Khaldoon A.; Cundari, Thomas R., 1964- & Anderson, Mary E. Valine 44 and Valine 45 of Human Glutiathione Sythetase are Key for Subunit Stability and Negative Cooperativity, article, Date Unknown; [Amsterdam, Netherlands]. (digital.library.unt.edu/ark:/67531/metadc180967/: accessed August 21, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT College of Arts and Sciences.