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Record Information
Version3.6
Creation Date2006-08-12 19:06:03 UTC
Update Date2016-10-12 18:17:00 UTC
HMDB IDHMDB03337
Secondary Accession NumbersNone
Metabolite Identification
Common NameOxidized glutathione
DescriptionOxidized glutathione is a glutathione dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized. glutathione participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It is also important as a hydrophilic molecule that is added to lipophilic toxins and waste in the liver during biotransformation before they can become part of the bile. glutathione is also needed for the detoxification of methylglyoxal, a toxin produced as a by-product of metabolism. This detoxification reaction is carried out by the glyoxalase system. Glyoxalase I (EC 4.4.1.5) catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S-D-Lactoyl-glutathione to glutathione and D-lactate.
Structure
Thumb
Synonyms
ValueSource
(2S)-2-Azaniumyl-4-{[(1R)-2-{[(2R)-2-[(4S)-4-azaniumyl-4-carboxylatobutanamido]-2-[(carboxylatomethyl)carbamoyl]ethyl]disulfanyl}-1-[(carboxylatomethyl)carbamoyl]ethyl]carbamoyl}butanoateHMDB
Glutathione disulfideHMDB
GSSGHMDB
L(-)-Glutathione(oxidized)HMDB
OxiglutationeHMDB
Chemical FormulaC20H32N6O12S2
Average Molecular Weight612.631
Monoisotopic Molecular Weight612.151961898
IUPAC Name2-amino-4-[(2-{[2-(4-amino-4-carboxybutanamido)-2-[(carboxymethyl)carbamoyl]ethyl]disulfanyl}-1-[(carboxymethyl)carbamoyl]ethyl)carbamoyl]butanoic acid
Traditional Nameoxiglutatione
CAS Registry Number27025-41-8
SMILES
NC(CCC(=O)NC(CSSCC(NC(=O)CCC(N)C(O)=O)C(=O)NCC(O)=O)C(=O)NCC(O)=O)C(O)=O
InChI Identifier
InChI=1S/C20H32N6O12S2/c21-9(19(35)36)1-3-13(27)25-11(17(33)23-5-15(29)30)7-39-40-8-12(18(34)24-6-16(31)32)26-14(28)4-2-10(22)20(37)38/h9-12H,1-8,21-22H2,(H,23,33)(H,24,34)(H,25,27)(H,26,28)(H,29,30)(H,31,32)(H,35,36)(H,37,38)
InChI KeyInChIKey=YPZRWBKMTBYPTK-UHFFFAOYSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as gamma-glutamyl peptides. These are oligo- and polypeptides consisting of any C-terminal alpha peptide having a gamma-glutamyl residue attached at the N alpha-position.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentGamma-glutamyl peptides
Alternative Parents
Substituents
  • Gamma-glutamyl alpha peptide
  • N-acyl-aliphatic-alpha amino acid
  • Tetracarboxylic acid or derivatives
  • N-acyl-alpha amino acid or derivatives
  • N-acyl-alpha-amino acid
  • Alpha-amino acid amide
  • Alpha-amino acid or derivatives
  • N-substituted-alpha-amino acid
  • Alpha-amino acid
  • Amino fatty acid
  • Fatty acyl
  • N-acyl-amine
  • Fatty amide
  • Dialkyldisulfide
  • Secondary carboxylic acid amide
  • Organic disulfide
  • Carboxamide group
  • Sulfenyl compound
  • Carboxylic acid
  • Carboxylic acid amide
  • Hydrocarbon derivative
  • Primary amine
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Amine
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External DescriptorsNot Available
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Glutamate metabolism
  • Component of Glutathione metabolism
ApplicationNot Available
Cellular locations
  • Extracellular
  • Mitochondria
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility0.41 mg/mLALOGPS
logP-3.6ALOGPS
logP-10ChemAxon
logS-3.2ALOGPS
pKa (Strongest Acidic)1.44ChemAxon
pKa (Strongest Basic)9.61ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count14ChemAxon
Hydrogen Donor Count10ChemAxon
Polar Surface Area317.64 Å2ChemAxon
Rotatable Bond Count21ChemAxon
Refractivity136.65 m3·mol-1ChemAxon
Polarizability58.41 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
Biological Properties
Cellular Locations
  • Extracellular
  • Mitochondria
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Saliva
Tissue Location
  • Brain
  • Epidermis
  • Erythrocyte
  • Fibroblasts
  • Granulocytes
  • Liver
  • Lymphocyte
  • Pancreas
  • Placenta
  • Platelet
  • Red Blood Cell
Pathways
NameSMPDB LinkKEGG Link
2-Hydroxyglutric Aciduria (D And L Form)SMP00136Not Available
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase DeficiencySMP00243Not Available
5-oxoprolinase deficiencySMP00500Not Available
5-OxoprolinuriaSMP00143Not Available
Acetaminophen Action PathwaySMP00710Not Available
Acetylsalicylic Acid PathwaySMP00083Not Available
Antipyrine Action PathwaySMP00692Not Available
Antrafenine Action PathwaySMP00693Not Available
Arachidonic Acid MetabolismSMP00075map00590
Bromfenac PathwaySMP00102Not Available
Carprofen Action PathwaySMP00694Not Available
Celecoxib PathwaySMP00096Not Available
Diclofenac PathwaySMP00093Not Available
Diflunisal PathwaySMP00289Not Available
Etodolac PathwaySMP00084Not Available
Etoricoxib Action PathwaySMP00695Not Available
Fenoprofen Action PathwaySMP00696Not Available
Flurbiprofen Action PathwaySMP00697Not Available
Gamma-glutamyl-transpeptidase deficiencySMP00501Not Available
Gamma-Glutamyltransferase DeficiencySMP00183Not Available
Glutamate MetabolismSMP00072map00250
Glutathione MetabolismSMP00015map00480
Glutathione Synthetase DeficiencySMP00337Not Available
HomocarnosinosisSMP00385Not Available
Hyperinsulinism-Hyperammonemia SyndromeSMP00339Not Available
Ibuprofen PathwaySMP00086Not Available
Indomethacin PathwaySMP00104Not Available
Ketoprofen PathwaySMP00085Not Available
Ketorolac PathwaySMP00098Not Available
Leukotriene C4 Synthesis DeficiencySMP00353Not Available
Lornoxicam Action PathwaySMP00700Not Available
Lumiracoxib Action PathwaySMP00699Not Available
Magnesium salicylate Action PathwaySMP00698Not Available
Mefanamic Acid PathwaySMP00109Not Available
Meloxicam PathwaySMP00106Not Available
Nabumetone PathwaySMP00114Not Available
Naproxen PathwaySMP00120Not Available
Nepafenac Action PathwaySMP00702Not Available
Oxaprozin PathwaySMP00113Not Available
Phenylbutazone Action PathwaySMP00701Not Available
Piroxicam PathwaySMP00077Not Available
Rofecoxib PathwaySMP00087Not Available
Salicylate-sodium Action PathwaySMP00708Not Available
Salicylic Acid Action PathwaySMP00709Not Available
Salsalate Action PathwaySMP00707Not Available
Succinic semialdehyde dehydrogenase deficiencySMP00567Not Available
Sulindac PathwaySMP00094Not Available
Suprofen PathwaySMP00101Not Available
Tenoxicam Action PathwaySMP00706Not Available
Tiaprofenic Acid Action PathwaySMP00705Not Available
Tolmetin Action PathwaySMP00704Not Available
Trisalicylate-choline Action PathwaySMP00703Not Available
Valdecoxib PathwaySMP00116Not Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified19.96 +/- 24.82 uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified1.69 +/- 0.38 uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified0.041 +/- 0.01 uMAdult (>18 years old)Not SpecifiedNormal details
SalivaDetected and Quantified0.88 +/- 0.43 uMAdult (>18 years old)FemaleNormal details
SalivaDetected and Quantified0.0156 +/- 0.0359 uMAdult (>18 years old)Female
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.207 +/- 0.264 uMAdult (>18 years old)Female
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.216 +/- 0.250 uMAdult (>18 years old)BothNormal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.249 +/- 0.397 uMAdult (>18 years old)BothNormal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.349 +/- 0.436 uMAdult (>18 years old)Not Specified
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.350 +/- 1.05 uMAdult (>18 years old)Female
Normal
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.350 +/- 1.05 uMAdult (>18 years old)Not Specified
Normal
    • Sugimoto et al. (...
details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified27.94 +/- 23.19 uMAdult (>18 years old)BothSchizophrenia details
BloodDetected and Quantified1.98 +/- 0.41 uMAdult (>18 years old)BothCanavan disease details
Cerebrospinal Fluid (CSF)Detected and Quantified0.065 +/- 0.01 uMAdult (>18 years old)Not SpecifiedMultiple sclerosis details
Cerebrospinal Fluid (CSF)Detected and Quantified0.044 +/- 0.01 uMAdult (>18 years old)Not Specified
Multiple sclerosis
details
SalivaDetected and Quantified0.39 +/- 0.18 uMAdult (>18 years old)MaleAlzheimer's disease details
SalivaDetected and Quantified0.58 +/- 0.47 uMAdult (>18 years old)MaleFrontotemporal lobe dementia details
SalivaDetected and Quantified0.434 +/- 0.405 uMAdult (>18 years old)BothTemporomandibular joint disorder (TMD)
    • Sugimoto et al. (...
details
SalivaDetected and Quantified0.441 +/- 0.403 uMAdult (>18 years old)BothDental caries
    • Sugimoto et al. (...
details
SalivaDetected and Quantified2.91 +/- 4.90 uMAdult (>18 years old)BothLewy body disease details
Associated Disorders and Diseases
Disease References
Canavan disease
  1. Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [16139832 ]
Schizophrenia
  1. Ballesteros A, Summerfelt A, Du X, Jiang P, Chiappelli J, Tagamets M, O'Donnell P, Kochunov P, Hong LE: Electrophysiological intermediate biomarkers for oxidative stress in schizophrenia. Clin Neurophysiol. 2013 Nov;124(11):2209-15. doi: 10.1016/j.clinph.2013.05.021. Epub 2013 Jun 30. [23823132 ]
Multiple sclerosis
  1. Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [12938853 ]
Associated OMIM IDs
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB023147
KNApSAcK IDNot Available
Chemspider ID950
KEGG Compound IDC00127
BioCyc IDOXIDIZED-GLUTATHIONE
BiGG ID33951
Wikipedia LinkGlutathione disulfide
NuGOwiki LinkHMDB03337
Metagene LinkHMDB03337
METLIN ID6893
PubChem Compound975
PDB IDNot Available
ChEBI ID17858
References
Synthesis ReferenceSaito, Susumu; Nishijima, Kunihide; Kataoka, Katsuyuki; Aoyanagi, Yoshinori; Fukuda, Yoji; Ito, Homare. Manufacture of oxidized glutathione from reduced glutathione with ascorbic acid and ascorbate oxidase. Jpn. Kokai Tokkyo Koho (1995), 4 pp.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Kondo T, Ohtsuka Y, Shimada M, Kawakami Y, Hiyoshi Y, Tsuji Y, Fujii H, Miwa S: Erythrocyte-oxidized glutathione transport in pyrimidine 5'-nucleotidase deficiency. Am J Hematol. 1987 Sep;26(1):37-45. [2888306 ]
  2. Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [12938853 ]
  3. Tauler P, Sureda A, Cases N, Aguilo A, Rodriguez-Marroyo JA, Villa G, Tur JA, Pons A: Increased lymphocyte antioxidant defences in response to exhaustive exercise do not prevent oxidative damage. J Nutr Biochem. 2006 Oct;17(10):665-71. Epub 2005 Nov 28. [16481153 ]
  4. Slivka A, Spina MB, Cohen G: Reduced and oxidized glutathione in human and monkey brain. Neurosci Lett. 1987 Feb 10;74(1):112-8. [3561870 ]
  5. Aukrust P, Svardal AM, Muller F, Lunden B, Berge RK, Ueland PM, Froland SS: Increased levels of oxidized glutathione in CD4+ lymphocytes associated with disturbed intracellular redox balance in human immunodeficiency virus type 1 infection. Blood. 1995 Jul 1;86(1):258-67. [7795231 ]
  6. Sakhi AK, Russnes KM, Smeland S, Blomhoff R, Gundersen TE: Simultaneous quantification of reduced and oxidized glutathione in plasma using a two-dimensional chromatographic system with parallel porous graphitized carbon columns coupled with fluorescence and coulometric electrochemical detection. J Chromatogr A. 2006 Feb 3;1104(1-2):179-89. [16376913 ]
  7. Glazyrin AL, Kolesnikov SI, Safronov AYu: Histochemical localization of oxidized glutathione-catalysing enzymes in human term placenta. Histochem J. 1993 Jan;25(1):45-50. [8432663 ]
  8. Carru C, Zinellu A, Pes GM, Marongiu G, Tadolini B, Deiana L: Ultrarapid capillary electrophoresis method for the determination of reduced and oxidized glutathione in red blood cells. Electrophoresis. 2002 Jun;23(11):1716-21. [12179993 ]
  9. Tohgi H, Abe T, Saheki M, Hamato F, Sasaki K, Takahashi S: Reduced and oxidized forms of glutathione and alpha-tocopherol in the cerebrospinal fluid of parkinsonian patients: comparison between before and after L-dopa treatment. Neurosci Lett. 1995 Jan 16;184(1):21-4. [7739798 ]
  10. Yoshida T: Determination of reduced and oxidized glutathione in erythrocytes by high-performance liquid chromatography with ultraviolet absorbance detection. J Chromatogr B Biomed Appl. 1996 Apr 12;678(2):157-64. [8738017 ]
  11. Sofic E, Lange KW, Jellinger K, Riederer P: Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci Lett. 1992 Aug 17;142(2):128-30. [1454205 ]
  12. Muda P, Kampus P, Zilmer M, Zilmer K, Kairane C, Ristimae T, Fischer K, Teesalu R: Homocysteine and red blood cell glutathione as indices for middle-aged untreated essential hypertension patients. J Hypertens. 2003 Dec;21(12):2329-33. [14654754 ]
  13. Satoh T, Yoshioka Y: Contribution of reduced and oxidized glutathione to signals detected by magnetic resonance spectroscopy as indicators of local brain redox state. Neurosci Res. 2006 May;55(1):34-9. Epub 2006 Feb 24. [16503064 ]
  14. Srivastava SK, Beutler E: Oxidized glutathione levels in erythrocytes of glucose-6-phosphate-dehydrogenase-deficient subjects. Lancet. 1968 Jul 6;2(7558):23-4. [4172687 ]
  15. Board P, Nishida T, Gatmaitan Z, Che M, Arias IM: Erythrocyte membrane transport of glutathione conjugates and oxidized glutathione in the Dubin-Johnson syndrome and in rats with hereditary hyperbilirubinemia. Hepatology. 1992 Apr;15(4):722-5. [1551648 ]

Enzymes

General function:
Involved in oxidoreductase activity
Specific function:
Maintains high levels of reduced glutathione in the cytosol.
Gene Name:
GSR
Uniprot ID:
P00390
Molecular weight:
56256.565
Reactions
Glutathione + NADP → Oxidized glutathione + NADPHdetails
Glutathione + NAD → Oxidized glutathione + NADH + Hydrogen Iondetails
Glutathione + NADP → Oxidized glutathione + NADPH + Hydrogen Iondetails
General function:
Involved in antioxidant activity
Specific function:
Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
Gene Name:
PRDX6
Uniprot ID:
P30041
Molecular weight:
25034.715
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
General function:
Involved in proteolysis
Specific function:
Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.
Gene Name:
ANPEP
Uniprot ID:
P15144
Molecular weight:
Not Available
General function:
Involved in glutathione peroxidase activity
Specific function:
It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.
Gene Name:
GPX7
Uniprot ID:
Q96SL4
Molecular weight:
20995.88
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid → Oxidized glutathione + 5-HETE + Waterdetails
Glutathione + 15(S)-HPETE → Oxidized glutathione + 15(S)-HETE + Waterdetails
General function:
Involved in glutathione peroxidase activity
Specific function:
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.
Gene Name:
GPX5
Uniprot ID:
O75715
Molecular weight:
25202.14
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid → Oxidized glutathione + 5-HETE + Waterdetails
Glutathione + 15(S)-HPETE → Oxidized glutathione + 15(S)-HETE + Waterdetails
General function:
Involved in glutathione transferase activity
Specific function:
Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
Gene Name:
GSTO1
Uniprot ID:
P78417
Molecular weight:
27565.6
Reactions
Glutathione + Dehydroascorbic acid → Oxidized glutathione + Ascorbic aciddetails
Methylarsonate + Glutathione → Methylarsonite + Oxidized glutathione + Waterdetails
General function:
Involved in glutathione peroxidase activity
Specific function:
Not Available
Gene Name:
GPX6
Uniprot ID:
P59796
Molecular weight:
24970.46
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid → Oxidized glutathione + 5-HETE + Waterdetails
Glutathione + 15(S)-HPETE → Oxidized glutathione + 15(S)-HETE + Waterdetails
General function:
Involved in glutathione peroxidase activity
Specific function:
Protects the hemoglobin in erythrocytes from oxidative breakdown.
Gene Name:
GPX1
Uniprot ID:
P07203
Molecular weight:
22087.94
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid → Oxidized glutathione + 5-HETE + Waterdetails
Glutathione + 15(S)-HPETE → Oxidized glutathione + 15(S)-HETE + Waterdetails
General function:
Involved in glutathione peroxidase activity
Specific function:
Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity).
Gene Name:
GPX4
Uniprot ID:
P36969
Molecular weight:
25046.57
Reactions
Glutathione + a lipid hydroperoxide → Oxidized glutathione + lipid + Waterdetails
Lipid hydroperoxide + Glutathione → Lipid + Oxidized glutathione + Waterdetails
General function:
Involved in glutathione peroxidase activity
Specific function:
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Gene Name:
GPX3
Uniprot ID:
P22352
Molecular weight:
25552.185
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid → Oxidized glutathione + 5-HETE + Waterdetails
Glutathione + 15(S)-HPETE → Oxidized glutathione + 15(S)-HETE + Waterdetails
General function:
Involved in glutathione transferase activity
Specific function:
Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
Gene Name:
GSTO2
Uniprot ID:
Q9H4Y5
Molecular weight:
24399.09
Reactions
Glutathione + Dehydroascorbic acid → Oxidized glutathione + Ascorbic aciddetails
Methylarsonate + Glutathione → Methylarsonite + Oxidized glutathione + Waterdetails
General function:
Involved in glutathione peroxidase activity
Specific function:
Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.
Gene Name:
GPX2
Uniprot ID:
P18283
Molecular weight:
21953.835
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails
Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid → Oxidized glutathione + 5-HETE + Waterdetails
Glutathione + 15(S)-HPETE → Oxidized glutathione + 15(S)-HETE + Waterdetails
General function:
Involved in cell redox homeostasis
Specific function:
Possesses significant protein thiol-disulfide oxidase activity.
Gene Name:
TXNDC12
Uniprot ID:
O95881
Molecular weight:
19205.615
Reactions
Glutathione + protein-disulfide → Oxidized glutathione + protein-dithioldetails
Insulin + Glutathione → Reduced insulin + Oxidized glutathionedetails
Protein dithiol + Oxidized glutathione → Protein disulfide + Glutathionedetails
General function:
Not Available
Specific function:
Not Available
Gene Name:
GPX8
Uniprot ID:
Q8TED1
Molecular weight:
23880.83
Reactions
Glutathione + Hydrogen peroxide → Oxidized glutathione + Waterdetails