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.
Synonyms: 0 Glutaredoxin 2 Glutaredoxin 3 Thioltransferase-1 Glutaredoxin 5 Glutaredoxins Glutaredoxin 1 Glutaredoxin TTase-1 Thioltransferase TTase 1 Thioltransferase 1
Term information
2008(1980); use PROTEINS 1979
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