Glutaredoxin

Pfam_box
Symbol = Glutaredoxin
Name = Glutaredoxin


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caption =
Pfam= PF00462
InterPro= IPR002109
SMART=
PROSITE= PDOC00173
SCOP = 1kte
TCDB =
OPM family= 139
OPM protein= 1z9h
PDB=PDB3|1ykaA:17-81 PDB3|1wikA:250-314 PDB3|2cq9A:69-131PDB3|2flsA:69-131 PDB3|1jhb :15-80 PDB3|1b4qA:15-80PDB3|1kte :15-80 PDB3|1nm3B:172-230 PDB3|3grx :4-63PDB3|1ilbA:4-63 PDB3|1fovA:4-63 PDB3|1ego :3-69PDB3|1egr :3-69 PDB3|1grx :3-69 PDB3|1qfnA:3-69PDB3|1aazB:2-76 PDB3|1de2A:2-76 PDB3|1de1A:2-76PDB3|1aba :2-76 PDB3|1nhoA:5-66 PDB3|1fo5A:6-67PDB3|1j08A:138-162 PDB3|1a8l :138-162 PDB3|1r7hB:3-61PDB3|1h75A:3-61 PDB3|1z9hB:102-152 PDB3|1hyuA:155-181PDB3|1zypB:155-181 PDB3|1zynB:155-181

Glutaredoxinscite journal |author=Holmgren A, Gleason FK |title=Thioredoxin and related proteins in procaryotes |journal=FEMS Microbiol. Rev. |volume=4 |issue=4 |pages=271–297 |year=1988 |pmid=3152490] cite journal |author=Holmgren A |title=Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulfide bonds |journal=Biochem. Soc. Trans. |volume=16 |issue=2 |pages=95–96 |year=1988 |pmid=3286320] cite journal |author=Holmgren A |title=Thioredoxin and glutaredoxin systems |journal=J. Biol. Chem. |volume=264 |issue=24 |pages=13963–13966 |year=1989 |pmid=2668278] are small redox enzymes of approximately one hundred amino-acid residues which use glutathione as a cofactor. Glutaredoxins are oxidised 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, oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione systemcite journal |author=Holmgren A, Fernandes AP |title=Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system |journal=Antioxid. Redox. Signal. |volume=6 |issue=1 |pages=63–74 |year=2004 |pmid=14713336 |doi=10.1089/152308604771978354] .

Glutaredoxins function as electron carriers 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 disulfide bondcite journal |author=Nilsson L, Foloppe N |title=The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues |journal=Structure |volume=12 |issue=2 |pages=289–300 |year=2004 |pmid=14962389] . It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulfide bond.

Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposedcite journal |author=Johnson GP, Goebel SJ, Perkus ME, Davis SW, Winslow JP, Paoletti E |title=Vaccinia virus encodes a protein with similarity to glutaredoxins |journal=Virology |volume=181 |issue=1 |pages=378–381 |year=1991 |pmid=1994586 |doi=10.1016/0042-6822(91)90508-9] 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.

ubfamilies

*Glutaredoxin subgroup InterPro|IPR014025

Human proteins containing this domain

GLRX; GLRX2; GLRX3; GLRX5; PTGES2; TXNL3;

References

External links

[http://www.expasy.org/enzyme/1.20.4.1 Enzyme database entry]