AI Article Synopsis
- GstO1 is an enzyme that helps regulate the glutathionylation cycle in cells and has four key cysteine residues that, when mutated, are linked to diseases.
- The study found that the wild-type GstO1 is sensitive to hydrogen peroxide, leading to denaturation, but glutathione can protect it from this damage.
- Cysteine mutations C32A and C236A demonstrated different enzyme activities and stability, highlighting their critical roles in sensing cellular redox conditions and contributing to disease pathology.
Article Abstract
Glutathione -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 (HO), which caused precipitation and denaturation at a physiological temperature. However, glutathione efficiently inhibited the HO-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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11121155 | PMC |
| http://dx.doi.org/10.3390/ijms25105279 | DOI Listing |
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