Glutaredoxin
| Glutaredoxin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| OPM superfamily | 131 | ||||||||
| OPM protein | 1z9h | ||||||||
| CDD | cd02066 | ||||||||
| |||||||||
Glutaredoxins[1][2][3] (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose metabolism.[4][5] Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Instead, glutaredoxins are reduced by the oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system.[6]
Like
In viruses
Glutaredoxin has been sequenced in a variety of
In plants
Approximately 30 GRX isoforms are described in the model plant
Subfamilies
Human proteins containing this domain
References
External links
- Enzyme database entry
- Glutaredoxins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
