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- Title
Regulation of Glutathione S -Transferase Omega 1 Mediated by Cysteine Residues Sensing the Redox Environment.
- Authors
Kim, Kwonyoung; Choi, Jeongin; Iram, Sana; Kim, Jihoe
- Abstract
Glutathione S-transferase omega 1 (GstO1) catalyzes deglutathionylation and plays an important role in the protein glutathionylation cycle in cells. GstO1 contains four conserved cysteine residues (C32, C90, C191, C236) found to be mutated in patients with associated diseases. In this study, we investigated the effects of cysteine mutations on the structure and function of GstO1 under different redox conditions. Wild-type GstO1 (WT) was highly sensitive to hydrogen peroxide (H2O2), which caused precipitation and denaturation at a physiological temperature. However, glutathione efficiently inhibited the H2O2-induced denaturation of GstO1. Cysteine mutants C32A and C236A exhibited redox-dependent stabilities and enzyme activities significantly different from those of WT. These results indicate that C32 and C236 play critical roles in GstO1 regulation by sensing redox environments and explain the pathological effect of cysteine mutations found in patients with associated diseases.
- Subjects
GLUTATHIONE transferase; CYSTEINE; GLUTATHIONE; ENZYME stability; OXIDATION-reduction reaction; HYDROGEN peroxide
- Publication
International Journal of Molecular Sciences, 2024, Vol 25, Issue 10, p5279
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms25105279