The Role of the Glycine Triad in Human Glutathione Synthetase

PDF Version Also Available for Download.

Description

Article discussing the role of the glycine triad in human glutathione synthetase.

Physical Description

16 p.

Creation Information

Dinescu, Adriana; Brown, Teresa R.; Barelier, Sarah; Cundari, Thomas R., 1964- & Anderson, Mary E. October 1, 2010.

Context

This article is part of the collection entitled: UNT Scholarly Works and was provided by UNT College of Arts and Sciences to Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 53 times . More information about this article can be viewed below.

Who

People and organizations associated with either the creation of this article or its content.

Authors

Publisher

Provided By

UNT College of Arts and Sciences

The UNT College of Arts and Sciences educates students in traditional liberal arts, performing arts, sciences, professional, and technical academic programs. In addition to its departments, the college includes academic centers, institutes, programs, and offices providing diverse courses of study.

Contact Us

What

Descriptive information to help identify this article. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

Article discussing the role of the glycine triad in human glutathione synthetase.

Physical Description

16 p.

Notes

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/S0006291X10015913

Abstract: Experimental kinetics and computational modeling of human glutathione synthetase (hGS) support the significant role of the G-loop glycine triad (G369, G370, G371) for activity of this ATP-grasp enzyme. Enzyme kinetic experiments indicate that G369V and G370V mutant hGS have little activity (<0.7 and 0.3%, respectively, versus wild-type hGS). However, G371V retains ~13% of the activity of wild-type hGS. With respect to G-loop:A-loop interaction in hGS, mutations at Gly369 and GLy370 decrease ligand binding and prevent active site closure and protection. This research indicates that Gly369 and Gly370 have essential role in hGS, while Gly371 has a lesser involvement. Implications for glycine-rich ensembles in other phosphate-binding enzymes are discussed.

Source

  • Biochemical and Biophysical Research Communications, 2010, Amsterdam: Elsevier Science Ltd., pp. 511-516

Language

Item Type

Identifier

Unique identifying numbers for this article in the Digital Library or other systems.

Publication Information

  • Publication Title: Biochemical and Biophysical Research Communications
  • Volume: 400
  • Issue: 4
  • Page Start: 511
  • Page End: 516
  • Peer Reviewed: Yes

Collections

This article is part of the following collection of related materials.

UNT Scholarly Works

Materials from the UNT community's research, creative, and scholarly activities and UNT's Open Access Repository. Access to some items in this collection may be restricted.

What responsibilities do I have when using this article?

When

Dates and time periods associated with this article.

Creation Date

  • October 1, 2010

Added to The UNT Digital Library

  • Sept. 6, 2013, 3:22 p.m.

Description Last Updated

  • May 28, 2014, 1:59 p.m.

Usage Statistics

When was this article last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 53

Interact With This Article

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

Citations, Rights, Re-Use

Dinescu, Adriana; Brown, Teresa R.; Barelier, Sarah; Cundari, Thomas R., 1964- & Anderson, Mary E. The Role of the Glycine Triad in Human Glutathione Synthetase, article, October 1, 2010; [Amsterdam, Netherlands]. (digital.library.unt.edu/ark:/67531/metadc180966/: accessed August 19, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT College of Arts and Sciences.