Glutathione reductase family

Lll. Loos, H., Roos, D., Weening, R and Houwerzijl, J., Familial deficiency of glutathione reductase in human blood cells. Blood 48,53-62 (1976). GR4... 

In contrast, antioxidant enzymes can efficiently counteract all UV-induced ROS (Aguilera et al. 2002). These enzymes are represented by superoxide dismutase (SOD), catalase and glutathione peroxidase as well as those involved in the ascorbate-glutathione cycle, such as ascorbate peroxidase, mono-dehydroascorbate reductase, dehydroascorbate reductase and glutathione reductase. One of the most important classes of antioxidant enzymes is the SOD family, which eliminate noxious superoxide radical anions. Different metalloforms of SOD exist (Fe, Mn, CuZn and Ni), which due to their intracellular localisation protect different cellular proteins (Lesser and Stochaj 1990). 

Williams, C. H. J., 1992, Lipoamide dehydrogenase, glutathione reductase, diioredoxin reductase and mercuric ion reductase family of flavoenzyme transhy(hogenases, in Chemistry and Biochemistry of Elavoenzymes, volume III (F. Muller, ed.), CRC Press, Boca Raton,... 

Loos et al. (L2) described a leukocytic glutathione reductase deficiency in three children of one family. The PMN glutathione-reductase activity was 10-15% of normal controls. 

Figure 3-7. Sequence alignment of various enzymes in the flavopro-tein disulfide oxidoreductase family. The sequences of the NADP4-dependent enzymes are the glutathione reductase from E. coli (E-GR), human (H-GR), Pseudomonas aeruginosa (P-GR), mercuric reductase from Staphylococcus aureus (S-MR), P. aeruginosa Tn 501 (P-GR), and trypanothione reductase from Trypanosoma congolense (T-TR). The NAD+-dependent enzymes are dihydrolipoamide dehydrogenase from E. coli (E-DD), B. stearothermophilus (B-DD), yeast (Y-DD), and human (H-DD). Residue positions marked with an asterisk correspond to those that were targets of site-directed mutagenesis in the text.

C. H. Williams, Jr., Lipoamide Dehydrogenase, Glutathione Reductase, Thioredoxin Reductase, and Mercuric Reductase - A Family of Flavoenzyme Transhydrogenases. In Chemistry and Biochemistry of Fiavoenzymes F. Muller, Ed. CRC Press Boca Raton, 1992 Vol. III. 

A NADPH-dependent PGF, synthase activity has been partially purified from lung. Structurally, this enzyme is a member of the aldose reductase family of proteins. There is also a glutathione-dependent form of the enzyme [15]. The roles of these proteins in PGF synthesis in vivo remain to be established. 

Figure 5 Comparison of thioredoxin coupled arsenate reductase (pI258 family) and glutaredoxin coupled arsenate reductase (R773 family). GSH reduced glutathione, the tripeptide consisting of y-glutamyl-cysteine-glycine. GSSG S-S bridged oxidized dimer of glutathionine.

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