Loading...
*  GPX4
... glutathione disulfide), which is generated during the reduction of hydroperoxides by GPx4, is recycled by glutathione reductase ... The antioxidant enzyme glutathione peroxidase 4 (GPx4) belongs to the family of glutathione peroxidases, which consists of 8 ... GPx4 catalyzes the following reaction: 2 glutathione + lipid-hydroperoxide → glutathione disulfide + lipid-alcohol + H2O This ... GPx4 is eventually reactivated by a second glutathione molecule, releasing glutathione disulfide (GS-SG). In mouse and rat, ...
*  Thioredoxin reductase
This TxR is related to glutathione reductase, trypanothione reductase, mercuric reductase and lipoamide dehydrogenase. A low ... Humans express three thioredoxin reductase isozymes: thioredoxin reductase 1 (TrxR1, cytosolic), thioredoxin reductase 2 (TrxR2 ... Each domain individually is very similar to the analogous domains in glutathione reductase, and lipoamide dehydrogenase but ... of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase ...
*  Glutathione reductase
... (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the ... In particular, glutathione reductase appears to be a good target for anti-malarials, as the glutathione reductase of the ... Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione ( ... The mechanism of Glutathione Reductase in sustaining the oxidative burst is still unknown. Glutathione reductase deficiency is ...
*  CoA-glutathione reductase
NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione ... In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction CoA + glutathione + ... Ondarza RN, Abney R, Lopez-Colome AM (1969). "Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from ... Carlberg I, Mannervik B (1977). "Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible ...
*  Glutathione amide reductase
... (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This ... glutathione amide disulfide + NADH + H+ Glutathione amide reductase is a dimeric flavoprotein (FAD). Vergauwen, B.; Pauwels, F ... Glutathione amide reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... "Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) ...
*  Protein-disulfide reductase (glutathione)
... insulin reductase, reductase, protein disulfide (glutathione), protein disulfide transhydrogenase, glutathione-protein ... In enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction 2 ... glutathione disulfide + protein-dithiol Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas ... This enzyme participates in glutathione metabolism. As of late 2007, only one structure has been solved for this class of ...
*  Adenylyl-sulfate reductase (glutathione)
... (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction AMP + sulfite + ... adenylylsulfate reductase (also used for, internal_xref(ec_num(1,8,99,2))), AMP,sulfite:oxidized-glutathione oxidoreductase, ( ... and glutathione disulfide, whereas its two products are adenylyl sulfate and glutathione. This enzyme belongs to the family of ... glutathione disulfide ⇌ {\displaystyle \rightleftharpoons } adenylyl sulfate + 2 glutathione The 3 substrates of this enzyme ...
*  Oncomodulin 2
Palmer EJ, MacManus JP, Mutus B (1990). "Inhibition of glutathione reductase by oncomodulin". Arch. Biochem. Biophys. 277 (1): ...
*  Lactoylglutathione lyase
"Glyoxalase 1 and glutathione reductase 1 regulate anxiety in mice". Nature. 438 (7068): 662-6. doi:10.1038/nature04250. PMID ... Glyoxalase II hydrolyzes the product to re-form the glutathione and produce D-lactate. Thus, glutathione acts unusually as a ... Although aldose reductase can also detoxify methylgloxal, the glyoxalase system is more efficient and seems to be the most ... The attack of the glutathione would leave a charged O- and the aldehyde hydrogen bound to C1. If the carbonyl oxygen of C2 can ...
*  Trypanothione
... spermidine cofactor for glutathione reductase in trypanosomatids". Science. 227 (4693): 1485-1487. Bibcode:1985Sci...227.1485F ... Trypanothione (Mr = 721.86 g/mol) is an unusual form of glutathione containing two molecules of glutathione joined by a ... Since the trypanosomatids also lack an equivalent of thioredoxin reductase, trypanothione reductase is the sole path that ... Trypanothione-disulfide reductase (TryR) was the first trypanothione-dependent enzyme to be discovered (EC 1.8.1.12). It is an ...
*  Richard Perham
Scrutton, Nigel Shaun (1988). Mechanistic and structural studies on glutathione reductase by protein engineering (PhD thesis). ...
*  Nigel Scrutton
Scrutton, Nigel Shaun (1988). Mechanistic and structural studies on glutathione reductase by protein engineering (PhD thesis). ... Hare, Victoria (2012). PETN reductase as a versatile biocatalyst for the reduction of nitroalkenes (PhD thesis). University of ... Lou, Xiao (2010). Biochemical and structural studies of human methionine synthase reductase (PhD thesis). University of ...
*  Ferredoxin-NADP(+) reductase
The glutathione-reductase-type FNRs are seen in the mitochondria of eukaryotes. In the plant-like family of FNRs, selective ... Other names in common use include: adrenodoxin reductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+ oxidoreductase, ... reductase, and TPNH-ferredoxin reductase During photosynthesis, electrons are removed from water and transferred to the single ... reductase ferredoxin-TPN reductase, NADP+:ferredoxin oxidoreductase, NADPH:ferredoxin oxidoreductase, reduced nicotinamide ...
*  Chorthippus brunneus
Exposure to dimethoate also decreases glutathione peroxidase, glutathione reductase, and carboxylesterases activity. Because C ... Individuals from heavily polluted sites have increased glutathione concentrations and decreased glutathione S-transferase ... In the lab, individuals exposed to zinc during diapause have lower glutathione concentrations. Dimethoate exposure enhances the ... A study of glutathione-dependent enzymes in grasshopper nymphs". Insect Science. 16 (1): 33-42. doi:10.1111/j.1744-7917.2009. ...
*  Alan Fairlamb
... spermidine cofactor for glutathione reductase in trypanosomatids". Science. 227 (4693): 1485-7. Bibcode:1985Sci...227.1485F. ... This thiol metabolite is quite different from its human equivalent, glutathione. Trypanothione allows the parasites to fend off ... "Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress". Mol. Microbiol ...
*  Glutaredoxin
Oxidized glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system. ... Glutaredoxins are 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 ... Rouhier N, Lemaire SD, Jacquot JP (2008). "The role of glutathione in photosynthetic organisms: emerging functions for ...
*  Flavin adenine dinucleotide
Glutathione reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) to glutathione (GSH). GR requires FAD and ... The reductase of the microsomal P450 systems, Cytochrome P-450 reductase (CPR) contains both an FMN and FAD. Electrons are ... The reductase of the mitochondrial P450 systems Adrenodoxin reductase contains FAD that is embedded in the FAD-binding domain ... The structures of the reductase of the microsomal versus reductase of the mitochondrial P450 systems are completely different ...
*  Schistosoma mansoni
Targeting of this pathway with different inhibitors of the central antioxidant enzyme thioredoxin glutathione reductase (TGR) ... 2012). "Identification of thioredoxin glutathione reductase inhibitors that kill cestode and trematode parasites". PLoS ONE. 7 ...
*  Arsenic poisoning
Arsenite inhibits members of the disulfide oxidoreductase family like glutathione reductase and thioredoxin reductase. The ... March 2005). "Glutathione reductase inhibition and methylated arsenic distribution in Cd1 mice brain and liver". Toxicological ... "The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex ... mechanistic implications of altered cellular glutathione and glutathione S-transferase". Toxicology and Applied Pharmacology. ...
*  Centenarian
Researchers in Denmark have also found that centenarians exhibit a high activity of glutathione reductase in red blood cells. ... "Low activity of superoxide dismutase and high activity of glutathione reductase in erythrocytes from centenarians". Age Ageing ... centenarians living in Upper Silesia had significantly higher red blood cell glutathione reductase and catalase activities, ...
*  Pentose phosphate pathway
It reduces glutathione via glutathione reductase, which converts reactive H2O2 into H2O by glutathione peroxidase. If absent, ... generate a large amount of NADPH through the pentose phosphate pathway to use in the reduction of glutathione. Hydrogen ...
*  Thiol oxidoreductase
Examples of such proteins include thioredoxin, thioredoxin reductase, glutathione reductase, glutaredoxin, glutathione ... For example, thioredoxin reductase provides reducing equivalents to thioredoxin, which in turn reduces peroxiredoxin. Fomenko, ...
*  Glutathione
... glutathione. Once oxidized, glutathione can be reduced back by glutathione reductase, using NADPH as an electron donor. The ... The role of glutathione as a skin whitener was discovered as a side effect of large doses of glutathione. Glutathione utilizes ... Halprin KM, Ohkawara A (1967). "The measurement of glutathione in human epidermis using glutathione reductase". The Journal of ... Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S-D-lactoyl-glutathione to glutathione and D-lactic acid. Glutathione, ...
*  Catalase
Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ (October 2009). "Characterization of glutathione reductase and catalase in the ... Xi S, Chen LH (2000). "Effects of dietary fish oil on tissue glutathione and antioxidant defense enzymes in mice with murine ...
*  Glutathione peroxidase
RSeH Glutathione reductase then reduces the oxidized glutathione to complete the cycle: GS-SG + NADPH + H+ → 2 GSH + NADP+. ... Glutathione reductase Selenium deficiency PDB: 1GP1​; Epp O, Ladenstein R, Wendel A (Jun 1983). "The refined structure of the ... Glutathione peroxidase was discovered in 1957 by Gordon C. Mills. It has been shown that low levels of glutathione peroxidase ... Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially ...
*  Metabolism
This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to reduce their ... These damaging oxidants are removed by antioxidant metabolites such as glutathione and enzymes such as catalases and ... Sheehan D, Meade G, Foley V, Dowd C (November 2001). "Structure, function and evolution of glutathione transferases: ... In humans, these include cytochrome P450 oxidases, UDP-glucuronosyltransferases, and glutathione S-transferases. This system of ...
*  Protein moonlighting
Blakytny R, Harding JJ (1996). "Prevention of the fructation-induced inactivation of glutathione reductase by bovine alpha- ... a protein that functions as an oxidase in copper metabolism and moonlights as a copper-independent glutathione peroxidase. ...