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Glutaredoxin has been sequenced in a variety of viruses. On the basis of extensive sequence similarity, it has been proposed [9] that Vaccinia virus protein O2L is, it seems, a glutaredoxin. Bacteriophage T4 thioredoxin seems to be evolution-related. In position 5 of the pattern T4, thioredoxin has Val instead of Pro.
In molecular biology, the glutaredoxin 2 family is a family of bacterial glutaredoxins. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase . Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. [ 1 ]
Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction arsenate + glutaredoxin arsenite + glutaredoxin disulfide + H 2 O. Thus, the two substrates of this enzyme are arsenate and glutaredoxin, whereas its 3 products are arsenite, glutaredoxin disulfide, and water.
Glutaredoxin 2 (GLRX2) is an enzyme that in humans encoded by the GLRX2 gene. GLRX2, also known as GRX2, is a glutaredoxin family protein and a thiol - disulfide oxidoreductase that maintains cellular thiol homeostasis.
Glutaredoxin 5, also known as GLRX5, is a protein which in humans is encoded by the GLRX5 gene located on chromosome 14. [5] This gene encodes a mitochondrial protein, which is evolutionarily conserved. It is involved in the biogenesis of iron- sulfur clusters, which are required for normal iron homeostasis.
Glutaredoxin-1 is a protein that in humans is encoded by the GLRX gene. [5] [6] Interactions. GLRX has been shown to interact with Wilson disease protein [7] and ...
Glutaredoxin-3 is a protein that in humans is encoded by the GLRX3 gene. [5] [6] [7] Interactions. GLRX3 has been shown to interact with PRKCQ. [5] References
Thioredoxin belongs to a structural family that includes glutaredoxin, glutathione peroxidase, bacterial protein disulfide isomerase DsbA, and the N-terminal domain of glutathione transferase. [4] Thioredoxins have a beta-alpha unit preceding the motif common to all these proteins.