Glutaredoxins [1, 2, 3], also known as thioltransferases (disulphide reductases, are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [4].

Glutaredoxin functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active centre disulphide bond [5]. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulphide bond.

Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed [6] that Vaccinia virus protein O2L is most probably a glutaredoxin. Finally, it must be noted that Bacteriophage T4 thioredoxin seems also to be evolutionary related. In position 5 of the pattern T4 thioredoxin has Val instead of Pro.

This entry represents Glutaredoxin.

1. Thioredoxin and related proteins in procaryotes. FEMS Microbiol. Rev. 4, 271-97
2. Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds. Biochem. Soc. Trans. 16, 95-6
3. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264, 13963-6
4. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6, 63-74
5. The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues. Structure 12, 289-300
6. Vaccinia virus encodes a protein with similarity to glutaredoxins. Virology 181, 378-81

Glutaredoxins [1, 2, Show more...

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