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Identification
YMDB IDYMDB00160
NameGlutathione
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
  • 5-L-Glutamyl-L-cysteinylglycine
  • Agifutol S
  • Bakezyme RX
  • Copren
  • Deltathione
  • gamma-Glutamylcysteinylglycine
  • gamma-L-glutamyl-L-cysteinyl-glycine
  • gamma-L-Glutamyl-L-cysteinylglycine
  • Glutathion
  • Glutathione
  • Glutathione red
  • Glutathione reduced
  • Glutathione-SH
  • Glutatiol
  • Glutatione
  • Glutide
  • Glutinal
  • GSH
  • Isethion
  • L-g-glutamyl-L-cysteinyl-glycine
  • L-gamma-glutamyl-L-cysteinyl-glycine
  • L-gamma-glutamyl-L-cysteinylglycine
  • L-glutamyl-L-cysteinylglycine
  • L-Glutathione
  • L-Glutathione reduce
  • Ledac
  • Neuthion
  • red. glutathione
  • Reduced glutathione
  • Tathion
  • Tathione
  • Triptide
  • N-(N-gamma-L-Glutamyl-L-cysteinyl)glycine
  • Poly(gamma-glutamylcysteine)glycine
  • (gamma-Glutamylcysteine)N-glycine
  • g-L-Glutamyl-L-cysteinyl-glycine
  • Γ-L-glutamyl-L-cysteinyl-glycine
  • N-(N-g-L-Glutamyl-L-cysteinyl)glycine
  • N-(N-Γ-L-glutamyl-L-cysteinyl)glycine
  • Poly(g-glutamylcysteine)glycine
  • Poly(γ-glutamylcysteine)glycine
  • (g-Glutamylcysteine)N-glycine
  • (Γ-glutamylcysteine)N-glycine
  • Glutathione, reduced
  • gamma L Glu L cys gly
  • gamma-L-Glu-L-cys-gly
  • gamma L Glutamyl L cysteinylglycine
CAS number70-18-8
WeightAverage: 307.323
Monoisotopic: 307.083805981
InChI KeyRWSXRVCMGQZWBV-WDSKDSINSA-N
InChIInChI=1S/C10H17N3O6S/c11-5(10(18)19)1-2-7(14)13-6(4-20)9(17)12-3-8(15)16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1
IUPAC Name(2S)-2-amino-4-{[(1R)-1-[(carboxymethyl)carbamoyl]-2-sulfanylethyl]carbamoyl}butanoic acid
Traditional IUPAC Nameglutathione
Chemical FormulaC10H17N3O6S
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])S[H]
Chemical Taxonomy
Description belongs to the class of organic compounds known as peptides. Peptides are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentPeptides
Alternative Parents
Substituents
  • Alpha peptide
  • N-acyl-alpha-amino acid
  • N-acyl-alpha amino acid or derivatives
  • Alpha-amino acid
  • Alpha-amino acid or derivatives
  • L-alpha-amino acid
  • Dicarboxylic acid or derivatives
  • Fatty acid
  • Amino acid or derivatives
  • Amino acid
  • Alkylthiol
  • Carboximidic acid
  • Carboximidic acid derivative
  • Carboxylic acid
  • Organic 1,3-dipolar compound
  • Propargyl-type 1,3-dipolar organic compound
  • Hydrocarbon derivative
  • Primary aliphatic amine
  • Organic oxide
  • Organic oxygen compound
  • Organic nitrogen compound
  • Carbonyl group
  • Amine
  • Organonitrogen compound
  • Organooxygen compound
  • Organosulfur compound
  • Organopnictogen compound
  • Primary amine
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point195 °C
Experimental Properties
PropertyValueReference
Water Solubility292.5 mg/mL [HMP experimental]PhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility0.88 g/LALOGPS
logP-2.7ALOGPS
logP-4.9ChemAxon
logS-2.5ALOGPS
pKa (Strongest Acidic)1.94ChemAxon
pKa (Strongest Basic)9.22ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count7ChemAxon
Hydrogen Donor Count6ChemAxon
Polar Surface Area158.82 ŲChemAxon
Rotatable Bond Count9ChemAxon
Refractivity69.11 m³·mol⁻¹ChemAxon
Polarizability29.11 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • vacuole
  • 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
Cysteine and methionine metabolismec00270 Map00270
Glutathione metabolismec00480 Map00480
Pyruvate metabolismec00620 Map00620
SMPDB Reactions
Gamma-Glutamylcysteine + Glycine + Adenosine triphosphateADP + phosphate + hydron + Glutathione
Glutathione + L-CysteineL-cysteinylglycine + Gamma-Glutamylcysteine
Glutathione + PyruvaldehydeS-Lactoylglutathione
S-Lactoylglutathione + waterGlutathione + D-Lactic acid
KEGG Reactions
Formaldehyde + NAD + GlutathioneS-Formylglutathione + NADH + hydron
Glutathione + L-AlanineL-cysteinylglycine + L-gamma-Glutamyl-L-alanine
NADPH + hydron + Oxidized glutathioneNADP + Glutathione
Hydrogen peroxide + Glutathionewater + Oxidized glutathione
Adenosine triphosphate + Glycine + Gamma-Glutamylcysteinephosphate + Glutathione + hydron + ADP
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
355 ± 296 µM YM mediumaerobicBaker's yeastPMID: 15357293
2113 ± 41 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 (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (x TMS)splash10-0a4i-0900000000-5841845f736f9a667622JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (x TMS)splash10-0a4i-0900000000-bdecde153761cb67852eJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-0900000000-5841845f736f9a667622JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-0900000000-bdecde153761cb67852eJSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-1910000000-52bc43dd913b68d74f84JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-08fs-3960000000-63ce34def2ae94b95515JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0pb9-0921000000-88168b0a9f5fc5fead3fJSpectraViewer | MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-7890000000-5853006f66d946dd3d2eJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-0596-9112300000-e82cf72540c283d8e323JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_1) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_2) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_3) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_4) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_5) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_6) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_2) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_3) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_4) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_5) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_6) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_7) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_8) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_9) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_10) - 70eV, PositiveNot AvailableJSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-004i-3795000000-d019cd7dcbad1f8a9e78JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-003r-9400000000-a83bf6292d41988256e3JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-001i-9000000000-305a92f8a9ffea58fa0eJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-0009000000-e950bfc5867b391c6960JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-004i-0910000000-83f6c079d1112e74ecf4JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-003r-0910000000-5b243cf8bd357ab270b1JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-0009000000-29ef335479f56b620d88JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-0009001000-d1f5986166efa523d024JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-056s-0495300000-dba7be381fd1ef776527JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-004i-0920000000-de5b8a5a377324599b39JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-053r-0007920000-7500cef211e48c8ea244JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0119003000-4eb7ed4e2a4cf6a83c66JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0uki-0290000000-6893386899c6eed6a1a6JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-05g0-0190000000-cacc2de4ab18ed59798bJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0009000000-6b4268add43ab66ef015JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-08fr-0015009000-a01bdc13a34d6ce8416fJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0uki-0290000000-ea94ec8247b4e025adbeJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0039210000-e1f721157a9ea89959d6JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a59-0039210000-35ce450ea95922abf0e1JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-0a4i-0009000000-9b01fba547d1fcde113aJSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-0006-0952000000-4a2a42699cf4aab2c559JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-002f-2900000000-bd9ba27b48b1322b7618JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Negativesplash10-004m-5900000000-cc7184d5bba50e6e49d0JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Negativesplash10-0a4i-9200000000-aecd0eb18a10c3ffb7abJSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0729-4492000000-78a928563adf9038ba59JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • 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
  • Grant, C. M., MacIver, F. H., Dawes, I. W. (1996). "Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae." Curr Genet 29:511-515.8662189
  • Mehdi, K., Penninckx, M. J. (1997). "An important role for glutathione and gamma-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae." Microbiology 143 ( Pt 6):1885-1889.9202464
  • Penninckx, M., Jaspers, C., Wiame, J. M. (1980). "Glutathione metabolism in relation to the amino-acid permeation systems of the yeast Saccharomyces cerevisiae. Occurrence of gamma-glutamyltranspeptidase: its regulation and the effects of permeation mutations on the enzyme cellular level." Eur J Biochem 104:119-123.6102906
  • 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
  • Rebbeor, J. F., Connolly, G. C., Dumont, M. E., Ballatori, N. (1998). "ATP-dependent transport of reduced glutathione in yeast secretory vesicles." Biochem J 334 ( Pt 3):723-729.9729482
  • Inoue, Y., Watanabe, K., Shimosaka, M., Saikusa, T., Fukuda, Y., Murata, K., Kimura, A. (1985). "Metabolism of 2-oxoaldehydes in yeasts. Purification and characterization of lactaldehyde dehydrogenase from Saccharomyces cerevisiae." Eur J Biochem 153:243-247.3908097
  • Cha, J. Y., Park, J. C., Jeon, B. S., Lee, Y. C., Cho, Y. S. (2004). "Optimal fermentation conditions for enhanced glutathione production by Saccharomyces cerevisiae FF-8." J Microbiol 42:51-55.15357293
  • Ostergaard, H., Tachibana, C., Winther, J. R. (2004). "Monitoring disulfide bond formation in the eukaryotic cytosol." J Cell Biol 166:337-345.15277542
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID16856
HMDB IDHMDB00125
Pubchem Compound ID124886
Kegg IDC00051
ChemSpider ID111188
FOODB IDFDB001498
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 ATP binding
Specific function:
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Gene Name:
GSH2
Uniprot ID:
Q08220
Molecular weight:
55814.69922
Reactions
ATP + gamma-L-glutamyl-L-cysteine + glycine → ADP + phosphate + glutathione.
General function:
Involved in zinc ion binding
Specific function:
Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde
Gene Name:
SFA1
Uniprot ID:
P32771
Molecular weight:
41041.69922
Reactions
S-(hydroxymethyl)glutathione + NAD(P)(+) → S-formylglutathione + NAD(P)H.
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
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 gamma-glutamyltransferase activity
Specific function:
Plays a role in the turnover of the vacuolar glutathione and in the supply of growth requirements during nitrogen starvation
Gene Name:
ECM38
Uniprot ID:
Q05902
Molecular weight:
73179.79688
Reactions
(5-L-glutamyl)-peptide + an amino acid → peptide + 5-L-glutamyl amino acid.
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Active as '1-Cys' thiol transferase against beta- hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis
Gene Name:
ECM4
Uniprot ID:
P36156
Molecular weight:
43273.39844
Reactions
RX + glutathione → HX + R-S-glutathione.
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Active as '1-Cys' thiol transferase against beta- hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB)
Gene Name:
GTO3
Uniprot ID:
Q04806
Molecular weight:
42402.60156
Reactions
RX + glutathione → HX + R-S-glutathione.
General function:
Involved in protein binding
Specific function:
RX + glutathione = HX + R-S-glutathione
Gene Name:
GTT2
Uniprot ID:
Q12390
Molecular weight:
26339.40039
Reactions
RX + glutathione → HX + R-S-glutathione.
General function:
Involved in hydrolase activity
Specific function:
Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid
Gene Name:
GLO2
Uniprot ID:
Q05584
Molecular weight:
31326.30078
Reactions
S-(2-hydroxyacyl)glutathione + H(2)O → glutathione + a 2-hydroxy carboxylate.
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Active as '1-Cys' thiol transferase against beta- hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB)
Gene Name:
GTO1
Uniprot ID:
P48239
Molecular weight:
41300.19922
Reactions
RX + glutathione → HX + R-S-glutathione.
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 protein binding
Specific function:
RX + glutathione = HX + R-S-glutathione
Gene Name:
GTT1
Uniprot ID:
P40582
Molecular weight:
26794.5
Reactions
RX + glutathione → HX + R-S-glutathione.
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 carboxylesterase activity
Specific function:
Serine hydrolase involved in the detoxification of formaldehyde
Gene Name:
Not Available
Uniprot ID:
P40363
Molecular weight:
33934.0
Reactions
S-formylglutathione + H(2)O → glutathione + formate.
4-methylumbelliferyl acetate + H2O → 4-methylumbelliferone + acetate
General function:
Involved in lactoylglutathione lyase activity
Specific function:
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione
Gene Name:
GLO1
Uniprot ID:
P50107
Molecular weight:
37208.69922
Reactions
(R)-S-lactoylglutathione → glutathione + methylglyoxal.
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 hydrolase activity
Specific function:
Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid
Gene Name:
GLO4
Uniprot ID:
Q12320
Molecular weight:
32338.59961
Reactions
S-(2-hydroxyacyl)glutathione + H(2)O → glutathione + a 2-hydroxy carboxylate.
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

Transporters

General function:
Involved in transmembrane transport
Specific function:
High affinity transporter for glutathione. Also transports tetra- and pentapeptides like the opioids leucine enkephalin (Tyr-Gly-Gly-Phe-Leu) and methionine enkephalin (Tyr- Gly-Gly_Phe-Met) across the cell membrane
Gene Name:
OPT1
Uniprot ID:
P40897
Molecular weight:
91614.79688
General function:
Involved in ATP binding
Specific function:
Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates
Gene Name:
BPT1
Uniprot ID:
P14772
Molecular weight:
176872.0