Glutaredoxin family

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Last update: 2021-12-02 (Bruno Savelli)


Glutaredoxin family  4CxxC Grx, CGFS Grx, CGYC Grx, CPF Grx, ROXY Grx

Description

Glutaredoxinsare small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. 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. Oxidized glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system. Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active centre disulfide bond. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulfide bond.
Glutaredoxins function as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Moreover, GRX/GLR act in antioxidant defence by reducing dehydroascorbate, peroxiredoxins, and methionine sulfoxide reductase.
Beside their function in antioxidant defence, bacterial and plant GRX/GLR were shown to bind iron-sulfur clusters and to deliver the cluster to enzymes on demand.


Profiles

Glutaredoxin :
Pfam: PF00462
Glutaredoxin:  IPR002109
Thioredoxin-like fold: IPR012336
Glutaredoxin subgroup: IPR014025
Glutaredoxin PICOT-like: IPR033658

Literature

Holmgren A, Gleason FK (1988). Thioredoxin and related proteins in procaryotes. FEMS Microbiol. Rev. 4 (4): 271-297.PMID 3152490.
Holmgren A (1988). Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulfide bonds. Biochem. Soc. Trans. 16 (2): 95-96. PMID 3286320.
Holmgren A (1989). Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264 (24): 13963-13966. PMID 2668278.
Holmgren A, Fernandes AP (2004). Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6 (1): 63-74. PMID 14713336.
Nilsson L, Foloppe N (2004). The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues. Structure 12 (2): 289-300. PMID 14962389.
Rouhier N, Lemaire SD, Jacquot JP (2008). The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annu Rev Plant Biol 59: 143-66. PMID 18444899.
Johnson GP, Goebel SJ, Perkus ME, Davis SW, Winslow JP, Paoletti E (1991). Vaccinia virus encodes a protein with similarity to glutaredoxins. Virology 181 (1): 378-381. PMID 1994586.