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Enzyme
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene. Glutathione reductase
Glutathione_reductase
Ubiquitous antioxidant compound in living organisms
to the reduced state by NADPH. This conversion is catalyzed by glutathione reductase: NADPH + GSSG + H2O → 2 GSH + NADP+ + OH− GSH protects cells by
Glutathione
Enzyme family protecting the organism from oxidative damages
GSH → GS-SeR + H2O GS-SeR + GSH → GS-SG + RSeH Glutathione reductase then reduces the oxidized glutathione to complete the cycle: GS–SG + NADPH + H+ → 2
Glutathione_peroxidase
dehydroascorbate reductase (DHAR) at the expense of GSH, yielding oxidized glutathione (GSSG). Finally GSSG is reduced by glutathione reductase (GR) using NADPH
Glutathione-ascorbate_cycle
Class of enzymes
including humans. This TxR is related to glutathione reductase, trypanothione reductase, mercuric reductase and lipoamide dehydrogenase. In the following
Thioredoxin_reductase
Enzyme
In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction CoA + glutathione + NADP+ ⇌ {\displaystyle
CoA-glutathione_reductase
Compound that inhibits the oxidation of other molecules
thioredoxin reductase, using NADPH as an electron donor. The glutathione system includes glutathione, glutathione reductase, glutathione peroxidases,
Antioxidant
Chemical compound
molecules of glutathione with reducing equivalents from the coenzyme NADPH. This reaction is catalyzed by the enzyme glutathione reductase. Antioxidant
Glutathione_disulfide
reductase, glutathione dehydroascorbate reductase, DHA reductase, dehydroascorbate reductase, GDOR, and glutathione:dehydroascorbic acid oxidoreductase.
Glutathione dehydrogenase (ascorbate)
Glutathione_dehydrogenase_(ascorbate)
Glutathione amide reductase (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This enzyme catalyses the following
Glutathione_amide_reductase
Mammalian protein found in Homo sapiens
during the reduction of hydroperoxides by GPX4, is recycled by glutathione reductase and NADPH/H+. GPX4 differs from the other GPX family members in
Glutathione_peroxidase_4
Class of enzymes
in plants. The glutathione-reductase-type FNRs (InterPro: IPR022890, InterPro: IPR021163), sometimes named adrenodoxin-NADP+ reductase for distinction
Ferredoxin—NADP(+)_reductase
Person who has turned 100 years old
living in Upper Silesia had significantly higher red blood cell glutathione reductase and catalase activities, although serum levels of vitamin E were
Centenarian
Enzyme
Adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction AMP + sulfite + glutathione disulfide ⇌ {\displaystyle
Adenylyl-sulfate reductase (glutathione)
Adenylyl-sulfate_reductase_(glutathione)
Swedish scientist (born 1943)
Depierre, Joseph W.; Mannervik, Bengt (1979). "Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver". Biochim
Bengt_Mannervik
Class of enzymes
enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction 2 glutathione + protein-disulfide ⇌ {\displaystyle
Protein-disulfide reductase (glutathione)
Protein-disulfide_reductase_(glutathione)
Vitamin, dietary supplement, and yellow food dye
required for the activity of glutathione reductase, an essential enzyme in the formation of the endogenous antioxidant, glutathione. Riboflavin, FMN, and FAD
Riboflavin
Protein family
oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system. Like
Glutaredoxin
Active region of an enzyme
be broken, In human cells, this is done by glutathione reductase(GR).[citation needed] Glutathione reductase is a dimer that contains two identical subunits
Active_site
such proteins include thioredoxin, thioredoxin reductase, glutathione reductase, glutaredoxin, glutathione peroxidase, and peroxiredoxin. They are involved
Thiol_oxidoreductase
reaction, glutathione reductase recycles oxidized glutathione back to the reduced form so that it again can be picked up by GSTs. This glutathione system
Bacterial glutathione transferase
Bacterial_glutathione_transferase
Incorporation of sulfur into living organisms
synthesis of glutathione are ATP dependent reactions. Glutathione is maintained in the reduced form by an NADPH-dependent glutathione reductase and the ratio
Sulfur_assimilation
Hormone released by the pineal gland
antioxidant enzymes, such as superoxide dismutase, glutathione peroxidase, glutathione reductase, and catalase. This increase in antioxidant enzyme expression
Melatonin
Mammalian protein found in humans
Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as an electron donor, which can be
Dihydrofolate_reductase
Non-protein chemical compound or metallic ion
Carlberg, Inger; Mannervik, Bengt (1985), "Glutathione reductase", Glutamate, Glutamine, Glutathione, and Related Compounds, Methods in Enzymology
Cofactor_(biochemistry)
Series of interconnected biochemical reactions
oxidative stress. It reduces glutathione via glutathione reductase, which converts reactive H2O2 into H2O by glutathione peroxidase. If absent, the H2O2
Pentose_phosphate_pathway
Protein-coding gene in the species Homo sapiens
glyoxalase system does not oxidize glutathione, which usually acts as a redox coenzyme. Although aldose reductase can also detoxify methylglyoxal, the
Lactoylglutathione_lyase
Protein family
to the interior of the subunit. The flavoprotein subunit has a glutathione reductase-like fold consisting of a beta(3,4)-alpha(3) core, and an alpha+beta
Flavocytochrome c sulfide dehydrogenase
Flavocytochrome_c_sulfide_dehydrogenase
German biochemist
tutelage of R. Heiner Schirmer. The topic of her dissertation was "Glutathione reductase and its apoenzyme: contributions to malaria chemotherapy and to
Katja_Becker
in common use include protein disulphide reductase, insulin-glutathione transhydrogenase, disulfide reductase, and NAD(P)H2:protein-disulfide oxidoreductase
Protein-disulfide_reductase
Illness from ingesting arsenic
members of the disulfide oxidoreductase family like glutathione reductase and thioredoxin reductase. The remaining unbound arsenic (≤ 10%) accumulates
Arsenic_poisoning
Chemical compound
enzymes, glutathione reductase (GR) and thioredoxin reductase (Trx1), and two mitochondrial enzymes, lipoamide dehydrogenase and thioredoxin reductase (Trx2)
Lipoic_acid
Clouding of the eye's lens due to excess galactose in the blood
competition between aldose reductase and glutathione reductase for nicotinamide adenine dinucleotide phosphate (NADPH). Aldose reductase requires NADPH for the
Galactosemic_cataract
Chemical compound
of phosphatidylcholine levels, and stimulation of glutathione synthesis and glutathione reductase activity. Citicoline's effects may also be explained
Citicoline
Medication used to treat sleeping sickness
spermidine-glutathione adduct that replaces glutathione in trypanosomes). While Mel T is a competitive inhibitor of trypanothione reductase, research suggests
Melarsoprol
Topics referred to by the same term
Kolkata, West Bengal, India Glucocorticoid receptor, a structure Glutathione reductase, an enzyme .gr, Greece's top-level domain Google Reader, a defunct
GR
Atom, molecule, or ion that has an unpaired valence electron; typically highly reactive
such as the enzymes superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase. In addition, antioxidants play a key role in these
Radical_(chemistry)
Redox-active coenzyme
flavin can reduce the product. Glutathione reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) to glutathione (GSH). GR requires FAD and
Flavin_adenine_dinucleotide
"Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox
Glutathione amide-dependent peroxidase
Glutathione_amide-dependent_peroxidase
Series of interconnected biochemical reactions
subsequently oxidized to fructose. It is also called the sorbitol-aldose reductase pathway. The pathway is implicated in diabetic complications, especially
Polyol_pathway
Chemical compound
"Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids". Science. 227 (4693): 1485–1487. Bibcode:1985Sci
Trypanothione
Systematic investigation into what factors influence centenarians' aging
living in Upper Silesia had significantly higher red blood cell glutathione reductase and catalase activities and higher, although insignificantly, serum
Research_into_centenarians
Medical drug
potassium levels and decreased glutathione levels lead to cataract formation. Topical administration of aldose reductase inhibitors have been shown to
Aldose_reductase_inhibitor
acceptors) Nitrite reductase EC 1.7.99.3 Nitrate reductase EC 1.7.99.4 Category:EC 1.8.1 (with NAD+ or NADP+ as acceptor) Glutathione reductase EC 1.8.1.7 Thioredoxin
List_of_enzymes
by sodA and sodB), catalases (katE and katG), glutathione synthetase (gshAB) and glutathione reductase (gor). Some bacteria have NADH-dependent peroxidases
Oxidation_response
Species of grasshopper
by almost 50%. Exposure to dimethoate also decreases glutathione peroxidase, glutathione reductase, and carboxylesterases activity. Because C. brunneus
Chorthippus_brunneus
Enzyme
in tissue in the form of S-nitrosoglutathione (GSNO), its adduct with glutathione (GSH). The enzyme is a class III alcohol dehydrogenase (ADH) encoded
Formaldehyde_dehydrogenase
Type of protein
functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec
Selenoprotein
Class of enzymes
In enzymology, a nitroquinoline-N-oxide reductase (EC 1.7.1.9) is an enzyme that catalyzes the chemical reaction 4-(hydroxyamino)quinoline N-oxide + 2
Nitroquinoline-N-oxide reductase
Nitroquinoline-N-oxide_reductase
8.4.1: glutathione—homocystine transhydrogenase EC 1.8.4.2: protein-disulfide reductase (glutathione) EC 1.8.4.3: glutathione—CoA-glutathione transhydrogenase
List_of_EC_numbers_(EC_1)
metabolism. In plants, the monodehydroascorbate reductase (MDAR) is an enzymatic component of the glutathione-ascorbate cycle that is one of the major antioxidant
Monodehydroascorbate reductase (NADH)
Monodehydroascorbate_reductase_(NADH)
Class of enzymes
sulfurtransferase. Other names in common use include glutathione-dependent thiosulfate reductase, sulfane reductase, and sulfane sulfurtransferase. Peck HD, Fisher
Thiosulfate—thiol sulfurtransferase
Thiosulfate—thiol_sulfurtransferase
Changes that happen to the faces of smokers
pigmentation, cancers and more. Important enzymes like glutathione peroxidase and glutathione reductase, which help clean up the extracellular matrix also
Smoker's_face
High grade of Nigerian crude oil
exposure, the activities of antioxidant enzymes, such as SOD and glutathione reductase (GR), were reduced in week 4. Raji, Y; Hart, VO (7 June 2012). "Influence
Bonny_Light_oil
Chemical compound
of o,p-dichlorodiphenyldichloroethane and perthane in vitro on glutathione reductase activity in the adrenals of dogs and guinea pigs". Bulletin of Experimental
Mitotane
Chemical compound
glutathione peroxidase, a central antioxidant enzyme that uses glutathione to remove ROS, and glutathione reductase, which regenerates glutathione, are
3-Deoxyglucosone
Enzyme decomposing hydrogen peroxide
Rathinasabapathi B, Ma LQ (October 2009). "Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure"
Catalase
Enzyme
Bao-Shan (2010), "Role of Ascorbate Peroxidase and Glutathione Reductase in Ascorbate–Glutathione Cycle and Stress Tolerance in Plants", in Anjum, Naser
Ascorbate_peroxidase
Species of fluke
different inhibitors of the central antioxidant enzyme thioredoxin glutathione reductase (TGR) results in reduced viability of worms. Decay accelerating
Schistosoma_mansoni
Chemical compound
pyruvate dehydrogenase, citrate synthetase, malate dehydrogenase, glutathione reductase, and pyruvate decarboxylase. Adverse effects for topical use are
Nitrofurazone
Medical scientist
Heiner; Williams, Charles H. (2000). "Kinetic Characterization of Glutathione Reductase from the Malarial Parasite Plasmodium falciparum". Journal of Biological
Catharina_Boehme
Medical condition
also reduces glutathione reductase, an enzyme that catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which
Nitrogen_dioxide_poisoning
domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions"
Mercury(II)_reductase
Mammalian protein found in Homo sapiens
homeostasis. This protein has dehydroascorbate reductase activity and may function in the glutathione-ascorbate cycle as part of antioxidant metabolism
GSTO1
Autosomal recessive metabolic disorder
damage levels, and the enzymatic activity of GPS (glutathione peroxidase), GR (glutathione reductase), CAT (catalase), and SOD (superoxide dismutase).
Maple_syrup_urine_disease
Selenium-containing amino acid
(for example glutathione peroxidases, tetraiodothyronine 5′ deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases, selenophosphate
Selenocysteine
Proteins performing more than one function
JJ (1996). "Prevention of the fructation-induced inactivation of glutathione reductase by bovine alpha-crystallin acting as a molecular chaperone". Ophthalmic
Protein_moonlighting
Species of edible alga
of scavenging enzymes including: catalase, superoxide dismutase, glutathione reductase, and ascorbate peroxidase (to scavenge hydrogen peroxide). After
Mastocarpus_stellatus
British biochemist (born 1964)
Scrutton, Nigel Shaun (1988). Mechanistic and structural studies on glutathione reductase by protein engineering (PhD thesis). University of Cambridge. OCLC 557267794
Nigel_Scrutton
Tomato with modified genes
1999 thus assumed the same would hold for a transfer of E. coli's glutathione reductase → the chloroplasts of S. lycopersicum and S. peruvianum. They overexpressed
Genetically_modified_tomato
Class of enzymes
participates in glutathione metabolism. Enzyme 1.8.1.13 at KEGG Pathway Database. Sundquist AR, Fahey RC (1988). "The novel disulfide reductase bis-gamma-glutamylcystine
Bis-gamma-glutamylcystine reductase
Bis-gamma-glutamylcystine_reductase
Topics referred to by the same term
Statutory Rules Galvanic skin response, physiological phenomenon Glutathione-disulfide reductase, enzyme Gunshot residue Gas Safe Register, in the United Kingdom
GSR
Condition of elevated methemoglobin in the blood
systems, e.g., NADH methemoglobin reductase (cytochrome-b5 reductase) (major pathway), NADPH methemoglobin reductase (minor pathway) and to a lesser extent
Methemoglobinemia
enzymology, a methylarsonate reductase (EC 1.20.4.2) is an enzyme that catalyzes the chemical reaction methylarsonate + 2 glutathione ⇌ {\displaystyle \rightleftharpoons
Methylarsonate_reductase
Enzyme
adenylyl-sulfate reductase from others is it uses thioredoxin as an electron donor instead of other donors such as glutathione (see Adenylyl-sulfate reductase (glutathione))
Adenylyl-sulfate reductase (thioredoxin)
Adenylyl-sulfate_reductase_(thioredoxin)
Class of enzymes
(September 2011). "Adenosine 5'-phosphosulfate reductase (APR2) mutation in Arabidopsis implicates glutathione deficiency in selenate toxicity". The Biochemical
Adenylyl-sulfate_reductase
Chemical compound
to act as an inhibitory agent against glutathione reductase, which is responsible for regenerating glutathione, a scavenger of free radicals and peroxides
Myricetin
being a potent inhibitor of glutathione peroxidase, glutathione reductase, pyruvate dehydrogenase, and thioredoxin reductase. Arsenic is a cause of mortality
Arsenic_biochemistry
English biochemist and professor
Scrutton, Nigel Shaun (1988). Mechanistic and structural studies on glutathione reductase by protein engineering (PhD thesis). University of Cambridge. OCLC 557267794
Richard_Perham
Chemical compound
functionality of certain enzymes such as glutathione reductase, glutathione peroxidases, thioredoxin reductase, and thioredoxin peroxidase. These enzymes
Potassium_arsenite
Gene
Additional RpoS-dependent factors involved in oxidative stress include glutathione reductase (encoded by gor), and superoxide dismutase (encoded by sodC). It
RpoS
element nutrient that functions as cofactor for glutathione peroxidases and certain forms of thioredoxin reductase. Selenium-containing proteins are produced
Selenium_in_biology
Professor of Plant Science
Christine H.; Halliwell, Barry (1976). "The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism"
Christine_Foyer
Enzyme family
Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction arsenate + glutaredoxin ⇌ {\displaystyle \rightleftharpoons
Arsenate reductase (glutaredoxin)
Arsenate_reductase_(glutaredoxin)
Protein-coding gene in the species Homo sapiens
"Comparison of in vivo effect of inorganic lead and cadmium on glutathione reductase system and delta-aminolevulinate dehydratase in human erythrocytes"
Delta-aminolevulinic acid dehydratase
Delta-aminolevulinic_acid_dehydratase
Peroxide-decomposing enzyme
Thiol: glutathione peroxidase, peroxiredoxin vanadium bromoperoxidase Alkyl hydroperoxide reductase Manganese peroxidase NADH peroxidase The glutathione peroxidase
Peroxidase
Enzyme
fulfills this role by regenerating glutathione and thioredoxin via glutathione reductase and thioredoxin reductase, respectively, thereby supporting the
NADK2
antioxidative enzymes such as superoxide dismutase, ascorbate peroxidase, glutathione reductase, and catalase are depressed. Cd Thlaspi caerulescens Alpine pennycress
Hyperaccumulators_table_–_3
peroxidase. The crystal structure of NADH peroxidase resembles glutathione reductase with respect to chain fold and location as well as conformation
NADH_peroxidase
Proteinogenic amino acid
can usually be oxidized in the following ways, where GSH is glutathione, GSSG is glutathione disulfide, RSH is a protein containing a thiol group with R
Cysteine
– ferredoxin-nadp reductase MeSH D08.811.682.667.092 – glutathione reductase MeSH D08.811.682.667.124 – hydrogensulfite reductase MeSH D08.811.682.667
List_of_MeSH_codes_(D08)
Chemical compound
mycothione reductase. Mycothiol biosynthesis and mycothiol-dependent enzymes such as mycothiol-dependent formaldehyde dehydrogenase and mycothione reductase have
Mycothiol
Protein-coding gene in the species Homo sapiens
product is characterised as a cyanocobalamin reductase (cyanide-eliminating) and a alkylcobalamin reductase. It enables the interconversion of cyano- and
MMACHC
Metabolism in hematopoietic progenitors
against accumulation of ROS because it is a key component in the glutathione-reductase system. Additionally, NADPH is required for synthesis of nucleic
Metabolic regulation of hematopoiesis
Metabolic_regulation_of_hematopoiesis
Class of enzymes
proteins such ER oxidoreductin 1 (Ero 1), VKOR (vitamin K epoxide reductase), glutathione peroxidase (Gpx7/8), and PrxIV (peroxiredoxin IV). Ero1 is thought
Protein_disulfide-isomerase
German physician and biochemist
Katja (26 Jan 2001), "Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster", Science, 291 (5504): 643–646, Bibcode:2001Sci
R._Heiner_Schirmer
Class of enzymes
glutathione disulfide; the cells then metabolize glutathione disulfide back to glutathione in a glutathione reductase-dependent reaction that converts NADPH to
5-Hydroxyeicosanoid dehydrogenase
5-Hydroxyeicosanoid_dehydrogenase
Protein-coding gene in the species Homo sapiens
PMID 1559707. Palmer EJ, MacManus JP, Mutus B (1990). "Inhibition of glutathione reductase by oncomodulin". Arch. Biochem. Biophys. 277 (1): 149–54. doi:10
Oncomodulin_2
Coenzyme acting as an electron carrier in biochemical redox reactions
toxicity of reactive oxygen species (ROS), allowing the regeneration of glutathione (GSH). NADPH is also used for anabolic pathways, such as cholesterol
Nicotinamide adenine dinucleotide phosphate
Nicotinamide_adenine_dinucleotide_phosphate
Chemical compound
metabolite menthofuran to be an inhibitor of CYP2A6. Menthofuran may deplete glutathione levels, leaving hepatocytes vulnerable to free radical damage. Anderson
Menthofuran
GLUTATHIONE REDUCTASE
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GLUTATHIONE REDUCTASE
GLUTATHIONE REDUCTASE
GLUTATHIONE REDUCTASE
GLUTATHIONE REDUCTASE
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GLUTATHIONE REDUCTASE