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A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
Entry Term(s)
Glutaredoxin
Glutaredoxin 1
Glutaredoxin 2
Glutaredoxin 3
Glutaredoxin 5
TTase-1
Thioltransferase
Thioltransferase-1
Registry Numbers
0
Public MeSH Note
2008; GLUTAREDOXINS were indexed under OXIDOREDUCTASES 2005-2007 & under PROTEINS 1979-2004; THIOLTRANSFERASE was indexed under SULFHYDRYL COMPOUNDS 1978-1981; under OXIDOREDUCTASES 1982-2004 & under PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE) 2005-2007
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.