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Record Information
Version4.0
StatusDetected and Quantified
Creation Date2006-08-12 19:06:03 UTC
Update Date2017-10-23 19:04:02 UTC
HMDB IDHMDB0003337
Secondary Accession Numbers
  • HMDB03337
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 KeyYPZRWBKMTBYPTK-UHFFFAOYSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities known as oligopeptides. These are organic compounds containing a sequence of between three and ten alpha-amino acids joined by peptide bonds.
KingdomChemical entities
Super ClassOrganic compounds
ClassOrganic acids and derivatives
Sub ClassCarboxylic acids and derivatives
Direct ParentOligopeptides
Alternative Parents
Substituents
  • Alpha-oligopeptide
  • Gamma-glutamyl alpha peptide
  • Glutamine or derivatives
  • N-acyl-alpha-amino acid
  • Tetracarboxylic acid or derivatives
  • N-acyl-alpha amino acid or derivatives
  • Alpha-amino acid amide
  • Cysteine or derivatives
  • Alpha-amino acid
  • N-substituted-alpha-amino acid
  • Alpha-amino acid or derivatives
  • Fatty amide
  • N-acyl-amine
  • Fatty acyl
  • Amino acid or derivatives
  • Carboxamide group
  • Amino acid
  • Dialkyldisulfide
  • Secondary carboxylic acid amide
  • Organic disulfide
  • Sulfenyl compound
  • Carboxylic acid
  • Organopnictogen compound
  • Primary aliphatic amine
  • Hydrocarbon derivative
  • Organic oxygen compound
  • Organic nitrogen compound
  • Carbonyl group
  • Organic oxide
  • Amine
  • Organonitrogen compound
  • Organooxygen compound
  • Organosulfur compound
  • Primary amine
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External DescriptorsNot Available
Ontology
Physiological effect

Health effect:

  Health condition:

Disposition

Biological Location:

  Subcellular:

  Biofluid and excreta:

  Organ and components:

  Tissue and substructures:

  Cell and elements:

    Cell:

    Element:

Source:

Process

Naturally occurring process:

  Biological process:

    Biochemical pathway:

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 g/LALOGPS
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 ŲChemAxon
Rotatable Bond Count21ChemAxon
Refractivity136.65 m³·mol⁻¹ChemAxon
Polarizability58.41 ųChemAxon
Number of Rings0ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-02t9-2121090000-ae2cd04146f2eea049a5View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-01q3-2111039000-a2c6d786111b549344feView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-02na-2011492000-e5bf21a4b84acc1cf18fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-00di-9002540000-c313b0aedf04e56ccf77View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00di-9012110000-27ec93f3d13ce2136a4fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-0147096000-d734e389344c1dc9b900View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0lxx-1597071000-aba0237f549185706415View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0007-9501140000-204a269186f92e44ac10View in MoNA
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/PathwhizKEGG
2-Hydroxyglutric Aciduria (D And L Form)Pw000212Pw000212 greyscalePw000212 simpleNot Available
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase DeficiencyPw000070Pw000070 greyscalePw000070 simpleNot Available
5-OxoprolinuriaPw000074Pw000074 greyscalePw000074 simpleNot Available
5-oxoprolinase deficiencyPw000476Pw000476 greyscalePw000476 simpleNot Available
Acetaminophen Action PathwayPw000687Pw000687 greyscalePw000687 simpleNot Available
Displaying entries 1 - 5 of 53 in total
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. [PubMed: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. [PubMed: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. [PubMed: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
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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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