Journal article 709 views
Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione
,
Richard N Armstrong,
Ralf Morgenstern
Archives of Biochemistry and Biophysics, Volume: 487, Issue: 1, Pages: 42 - 48
Swansea University Author:
William Griffiths
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DOI (Published version): 10.1016/j.abb.2009.04.009
Abstract
The trimeric membrane protein microsomal glutathione transferase 1 (MGST1) possesses glutathione transferase and peroxidase activity. Previous data indicated one active site/trimer whereas structural data suggests three GSH-binding sites. Here we have determined ligand interactions of MGST1 by sever...
| Published in: | Archives of Biochemistry and Biophysics |
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| ISSN: | 0003-9861 |
| Published: |
2009
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| Online Access: |
Check full text
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| URI: | https://cronfa.swan.ac.uk/Record/cronfa10949 |
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| Abstract: |
The trimeric membrane protein microsomal glutathione transferase 1 (MGST1) possesses glutathione transferase and peroxidase activity. Previous data indicated one active site/trimer whereas structural data suggests three GSH-binding sites. Here we have determined ligand interactions of MGST1 by several techniques. Nanoelectrospray mass spectrometry of native MGST1 revealed binding of three GSH molecules/trimer and equilibrium dialysis showed three product molecules/trimer (Kd = 320 ± 50 μM). All three product molecules could be competed out with GSH. Reinvestigation of GSH-binding showed one high affinity site per trimer, consistent with earlier data. Using single turnover stopped flow kinetic measurements, Kd could be determined for a low affinity GSH-binding site (2.5 ± 0.5 mM). Thus we can reconcile previous observations and show here that MGST1 contains three active sites with different affinities for GSH and that only the high affinity site is catalytically competent. |
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| College: |
Faculty of Medicine, Health and Life Sciences |
| Issue: |
1 |
| Start Page: |
42 |
| End Page: |
48 |