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PMID:20074363
| Citation |
Greetham, D, Vickerstaff, J, Shenton, D, Perrone, GG, Dawes, IW and Grant, CM (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem. 11:3 |
|---|---|
| Abstract |
Protein-SH groups are amongst the most easily oxidized residues in proteins, but irreversible oxidation can be prevented by protein glutathionylation, in which protein-SH groups form mixed disulphides with glutathione. Glutaredoxins and thioredoxins are key oxidoreductases which have been implicated in regulating glutathionylation/deglutathionylation in diverse organisms. Glutaredoxins have been proposed to be the predominant deglutathionylase enzymes in many plant and mammalian species, whereas, thioredoxins have generally been thought to be relatively inefficient in deglutathionylation. |
| Links |
PubMed PMC2836980 Online version:10.1186/1471-2091-11-3 |
| Keywords |
Glutaredoxins/metabolism; Glutathione/metabolism; Mutation; Oxidation-Reduction; Reactive Oxygen Species/metabolism; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/growth & development; Thioredoxins/genetics; Thioredoxins/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0080058: protein deglutathionylation |
ECO:0000314: direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0080058: protein deglutathionylation |
ECO:0000316: genetic interaction evidence used in manual assertion |
SGD:S000004033 |
P |
Seeded From UniProt |
complete | ||
See also
References
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