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・ Glyceria borealis
・ Glyceria fluitans
・ Glyceria grandis
・ Glyceria leptostachya
・ Glyceria maxima
・ Glyceria notata
・ Glutaminyl-tRNA synthase (glutamine-hydrolysing)
・ Glutamyl aminopeptidase
・ Glutamyl endopeptidase
・ Glutamyl endopeptidase II
・ Glutamyl-tRNA reductase
・ Glutaraldehyde
・ Glutarate-semialdehyde dehydrogenase
・ Glutarate—CoA ligase
・ Glutaredoxin
Glutaredoxin 2 (bacterial)
・ Glutaric acid
・ Glutaric acidemia type 2
・ Glutaric aciduria type 1
・ Glutarimide
・ Glutaronitrile
・ Glutaryl-7-aminocephalosporanic-acid acylase
・ Glutaryl-CoA
・ Glutaryl-CoA dehydrogenase
・ Glutaryl-CoA dehydrogenase (non-decarboxylating)
・ Glutathione
・ Glutathione amide reductase
・ Glutathione amide-dependent peroxidase
・ Glutathione dehydrogenase (ascorbate)
・ Glutathione disulfide


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Glutaredoxin 2 (bacterial) : ウィキペディア英語版
Glutaredoxin 2 (bacterial)

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. The active site residues (Cys9-Pro10-Tyr11-Cys12, in ''Escherichia coli'' Grx2, which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyse reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.
These enzymes are not related to GLRX2.
==References==


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