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Identification
YMDB IDYMDB00057
NameOxidized glutathione
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionGlutathione (GSH) is a tripeptide that contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side-chain. It is an antioxidant and a coenzyme in various enzymatic reactions. Glutathione exists in reduced (GSH) and oxidized (GSSG) states. Glutathione is found almost exclusively in its reduced form, since the enzyme that reverts it from its oxidized form, glutathione reductase, is constitutively active and inducible upon oxidative stress.
Structure
Thumb
Synonyms
  • (2S)-2-Azaniumyl-4-{[(1R)-2-{[(2R)-2-[(4S)-4-azaniumyl-4-carboxylatobutanamido]-2-[(carboxylatomethyl)carbamoyl]ethyl]disulfanyl}-1-[(carboxylatomethyl)carbamoyl]ethyl]carbamoyl}butanoate
  • glutathione
  • Glutathione disulfide
  • glutathione disulphide
  • glutathione ox
  • glutathione oxidized
  • GSH
  • GSSG
  • l-glutathione oxidized
  • L(-)-Glutathione(oxidized)
  • oxidised glutathione
  • Oxidized glutathione
  • OXIDIZED GLUTATHIONE DISULFIDE
  • OXIDIZED-GLUTATHIONE
  • Oxiglutatione
CAS number27025-41-8
WeightAverage: 612.631
Monoisotopic: 612.151961898
InChI KeyYPZRWBKMTBYPTK-UHFFFAOYSA-N
InChIInChI=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)
IUPAC Name2-amino-4-[(2-{[2-(4-amino-4-carboxybutanamido)-2-[(carboxymethyl)carbamoyl]ethyl]disulfanyl}-1-[(carboxymethyl)carbamoyl]ethyl)carbamoyl]butanoic acid
Traditional IUPAC Nameoxiglutatione
Chemical FormulaC20H32N6O12S2
SMILES[H]OC(=O)C([H])([H])N([H])C(=O)C([H])(N([H])C(=O)C([H])([H])C([H])([H])C([H])(N([H])[H])C(=O)O[H])C([H])([H])SSC([H])([H])C([H])(N([H])C(=O)C([H])([H])C([H])([H])C([H])(N([H])[H])C(=O)O[H])C(=O)N([H])C([H])([H])C(=O)O[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as oligopeptides. These are organic compounds containing a sequence of between three and ten alpha-amino acids joined by peptide bonds.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
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
Physical Properties
StateSolid
Charge0
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
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
Polarizability58.43 ųChemAxon
Number of Rings0ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Glutathione metabolismPW002395 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glutathione metabolismec00480 Map00480
Pyruvate metabolismec00620 Map00620
SMPDB ReactionsNot Available
KEGG Reactions
NADPH + hydron + Oxidized glutathioneNADP + Glutathione
Hydrogen peroxide + Glutathionewater + Oxidized glutathione
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
94 ± 4 µM YPD medium/SC mediumaerobicBaker's yeastPMID: 15277542
Conversion Details Here
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-0900000000-c8147955c6b355f0fc5cJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-0910000000-3e6195d480fbfe87b449JSpectraViewer | MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-02t9-2121090000-ae2cd04146f2eea049a5JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-01q3-2111039000-a2c6d786111b549344feJSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , negativesplash10-0uki-0290000000-04456f914411a2ecbe4fJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , negativesplash10-0a4i-0039210000-772eee67ad10a2d98fa7JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , negativesplash10-08fr-1957008000-f8812fd72d475ecd2693JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-03di-0000109000-65d563bcfc551b4a7abdJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-03di-0003309000-7555effd0b74737b9d2fJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-0a4i-0259201000-2cd328143ce713c285d9JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-05d0-0493000000-93bd088394049a484b9dJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ , positivesplash10-001r-0190000000-88b871b5a3f668f4b3a1JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-IT , positivesplash10-0a59-0019811000-b24651cf6fc55de750b8JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , positivesplash10-053s-0495300000-69ab8e397b7a546ecd3fJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT , positivesplash10-053r-0007920000-39da34018ceb610daa32JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , positivesplash10-03di-0000009000-9cde769e8905f413f7e3JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , positivesplash10-03di-0000009000-4e3c9569882ab5507bf2JSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-02na-2011492000-e5bf21a4b84acc1cf18fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-00di-9002540000-c313b0aedf04e56ccf77JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00di-9012110000-27ec93f3d13ce2136a4fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-0147096000-d734e389344c1dc9b900JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0lxx-1597071000-aba0237f549185706415JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0007-9501140000-204a269186f92e44ac10JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Muller, E. G. (1996). "A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth." Mol Biol Cell 7:1805-1813.8930901
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Outten, C. E., Culotta, V. C. (2004). "Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase." J Biol Chem 279:7785-7791.14672937
  • Ostergaard, H., Tachibana, C., Winther, J. R. (2004). "Monitoring disulfide bond formation in the eukaryotic cytosol." J Cell Biol 166:337-345.15277542
Synthesis Reference:Saito, 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.
External Links:
ResourceLink
CHEBI ID17858
HMDB IDHMDB03337
Pubchem Compound ID975
Kegg IDC00127
ChemSpider ID950
FOODB IDFDB023147
WikipediaGlutathione
BioCyc IDOXIDIZED-GLUTATHIONE

Enzymes

General function:
Involved in glutathione peroxidase activity
Specific function:
May constitute a glutathione peroxidase-like protective system against oxidative stresses
Gene Name:
GPX2
Uniprot ID:
P38143
Molecular weight:
18406.0
Reactions
2 glutathione + H(2)O(2) → glutathione disulfide + 2 H(2)O.
2 glutathione + a lipid hydroperoxide → glutathione disulfide + lipid + H2O
General function:
Involved in oxidoreductase activity
Specific function:
Maintains high levels of reduced glutathione in the cytosol
Gene Name:
GLR1
Uniprot ID:
P41921
Molecular weight:
53440.60156
Reactions
2 glutathione + NADP(+) → glutathione disulfide + NADPH.
General function:
Involved in glutathione peroxidase activity
Specific function:
May constitute a glutathione peroxidase-like protective system against oxidative stresses
Gene Name:
GPX1
Uniprot ID:
P36014
Molecular weight:
19484.5
Reactions
2 glutathione + H(2)O(2) → glutathione disulfide + 2 H(2)O.
2 glutathione + a lipid hydroperoxide → glutathione disulfide + lipid + H2O
General function:
Involved in electron carrier activity
Specific function:
Monothiol glutaredoxin involved in iron-sulfur biogenesis. Required for normal iron homeostasis. Protects cells against oxidative damage due to reactive oxygen species
Gene Name:
GRX5
Uniprot ID:
Q02784
Molecular weight:
16931.30078
Reactions
General function:
Involved in glutathione peroxidase activity
Specific function:
Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3
Gene Name:
HYR1
Uniprot ID:
P40581
Molecular weight:
18641.40039
Reactions
2 R'-SH + ROOH → R'-S-S-R' + H(2)O + ROH.
2 glutathione + a lipid hydroperoxide → glutathione disulfide + lipid + H2O
General function:
Involved in electron carrier activity
Specific function:
Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage
Gene Name:
GRX2
Uniprot ID:
P17695
Molecular weight:
15861.2998
Reactions
General function:
Involved in electron carrier activity
Specific function:
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable)
Gene Name:
GRX4
Uniprot ID:
P32642
Molecular weight:
27492.59961
General function:
Involved in electron carrier activity
Specific function:
Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage
Gene Name:
GRX1
Uniprot ID:
P25373
Molecular weight:
12380.09961
Reactions