Record Information
Version2.0
Creation Date2012-05-31 10:21:27 -0600
Update Date2015-09-13 12:56:06 -0600
Secondary Accession Numbers
  • ECMDB00125
Identification
Name:Glutathione
DescriptionGlutathione (GSH) is a compound synthesized from cysteine. Like cysteine, glutathione contains the crucial thiol (-SH) group that makes it an effective antioxidant. There are virtually no living organisms on this planet-animal or plant whose cells don't contain some glutathione. Scientists have speculated that glutathione was essential to the very development of life on earth. Glutathione has many roles; in none does it act alone. It is a coenzyme in various enzymatic reactions. The most important of these are redox reactions, in which the thiol grouping on the cysteine portion of cell membranes protects against peroxidation; and conjugation reactions, in which glutathione binds with toxic chemicals in order to detoxify them. GSH is known as a substrate in both conjugation reactions and reduction reactions, catalyzed by glutathione S-transferase enzymes in the bacterial cytosol.
Structure
Thumb
Synonyms:
  • γ-L-glutamyl-L-cysteinyl-glycine
  • 5-L-Glutamyl-L-cysteinylglycine
  • Agifutol S
  • Bakezyme RX
  • Copren
  • Deltathione
  • g-Glutamylcysteinylglycine
  • g-L-Glutamyl-L-cysteinyl-glycine
  • g-L-Glutamyl-L-cysteinylglycine
  • Gamma-Glutamylcysteinylglycine
  • Gamma-L-Glutamyl-L-cysteinyl-glycine
  • Gamma-L-Glutamyl-L-cysteinylglycine
  • Glutathion
  • Glutathionate
  • Glutathione
  • Glutathione red
  • Glutathione reduced
  • Glutathione-SH
  • Glutathionic acid
  • Glutatiol
  • Glutatione
  • Glutide
  • Glutinal
  • GSH
  • Isethion
  • L-g-Glutamyl-L-cysteinyl-glycine
  • L-g-Glutamyl-L-cysteinylglycine
  • L-gamma-Glutamyl-L-cysteinyl-glycine
  • L-gamma-Glutamyl-L-cysteinylglycine
  • L-Glutamyl-L-cysteinylglycine
  • L-Glutathione
  • L-Glutathione reduce
  • L-γ-Glutamyl-L-cysteinyl-glycine
  • L-γ-Glutamyl-L-cysteinylglycine
  • Ledac
  • Neuthion
  • Red. glutathione
  • Reduced glutathione
  • Tathion
  • Tathione
  • Triptide
  • γ-Glutamylcysteinylglycine
  • γ-L-Glutamyl-L-cysteinyl-glycine
  • γ-L-Glutamyl-L-cysteinylglycine
Chemical Formula:C10H17N3O6S
Weight:Average: 307.323
Monoisotopic: 307.083805981
InChI Key:RWSXRVCMGQZWBV-WDSKDSINSA-N
InChI:InChI=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
CAS number:70-18-8
IUPAC Name:(2S)-2-amino-4-{[(1R)-1-[(carboxymethyl)carbamoyl]-2-sulfanylethyl]carbamoyl}butanoic acid
Traditional IUPAC Name:glutathione
SMILES:N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O)C(O)=O
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
State:Solid
Charge:-1
Melting point:195 °C
Experimental Properties:
PropertyValueSource
Water Solubility:292.5 mg/mL [HMP experimental]PhysProp
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:Cytoplasm
Reactions:
Adenosine triphosphate + Water + Glutathione > ADP + Glutathione + Hydrogen ion + Phosphate
Adenosine triphosphate + Water + Glutathione > ADP + Glutathione + Hydrogen ion + Phosphate
glutaredoxin + 2 Glutathione > glutaredoxin + Glutathione disulfide
S-Formylglutathione + Water <> Formic acid + Glutathione + Hydrogen ion
Arsenate + 2 Glutathione > Arsenite + Glutathione disulfide + Water
Water + S-Lactoylglutathione > Glutathione + Hydrogen ion + D-Lactic acid
periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized) + 2 Glutathione > periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced) + Glutathione disulfide
Glutathione + Pyruvaldehyde <> S-Lactoylglutathione
2 Glutathione + Hydrogen peroxide <> Glutathione disulfide +2 Water
protein disulfide isomerase II (oxidized) + 2 Glutathione > protein disulfide isomerase II (reduced) + Glutathione disulfide
Adenosine triphosphate + gamma-Glutamylcysteine + Glycine <> ADP + Glutathione + Hydrogen ion + Phosphate
Adenosine triphosphate + Glutathione + Spermidine <> ADP + Glutathionylspermidine + Hydrogen ion + Phosphate
Glutathionylspermidine + Water <> Glutathione + Spermidine
Glutathione + Water > Cysteinylglycine + L-Glutamate
Glutathione disulfide + Hydrogen ion + NADPH <>2 Glutathione + NADP
Formaldehyde + Glutathione <> S-(Hydroxymethyl)glutathione
2 Glutathione + NAD <> Glutathione disulfide + NADH + Hydrogen ion
2 Glutathione + NADP <> Glutathione disulfide + NADPH + Hydrogen ion
Glutathione + Water <> Cysteinylglycine + L-Glutamate
Adenosine triphosphate + gamma-Glutamylcysteine + Glycine <> ADP + Phosphate + Glutathione
S-Formylglutathione + Water <> Formic acid + Glutathione
Glutathione + L-Amino acid <> Cysteinylglycine + (5-L-Glutamyl)-L-amino acid
S-Lactoylglutathione + Water <> Glutathione + D-Lactic acid
Adenosine triphosphate + Glutathione + Spermidine <> ADP + Phosphate + Glutathionylspermidine
S-Lactoylglutathione <> Glutathione + Pyruvaldehyde
RX + Glutathione <> Halide + R-S-Glutathione
(1R,2S)-Naphthalene 1,2-oxide + Glutathione <> (1R)-Hydroxy-(2R)-glutathionyl-1,2-dihydronaphthalene
(1S,2R)-Naphthalene 1,2-oxide + Glutathione <> (1R)-Glutathionyl-(2R)-hydroxy-1,2-dihydronaphthalene
(1S,2R)-Naphthalene 1,2-oxide + Glutathione <> (1S)-Hydroxy-(2S)-glutathionyl-1,2-dihydronaphthalene
1-Nitronaphthalene-7,8-oxide + Glutathione <> 1-Nitro-7-hydroxy-8-glutathionyl-7,8-dihydronaphthalene
1-Nitronaphthalene-7,8-oxide + Glutathione <> 1-Nitro-7-glutathionyl-8-hydroxy-7,8-dihydronaphthalene
1-Nitronaphthalene-5,6-oxide + Glutathione <> 1-Nitro-5-hydroxy-6-glutathionyl-5,6-dihydronaphthalene
1-Nitronaphthalene-5,6-oxide + Glutathione <> 1-Nitro-5-glutathionyl-6-hydroxy-5,6-dihydronaphthalene
2 Glutathione + 5(S)-Hydroperoxyeicosatetraenoic acid <> Glutathione disulfide + 5-HETE + Water
2 Glutathione + 15(S)-HPETE <> Glutathione disulfide + 15(S)-HETE + Water
Bromobenzene-3,4-oxide + Glutathione <> 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzene
Bromobenzene-2,3-oxide + Glutathione <> 2,3-Dihydro-2-S-glutathionyl-3-hydroxy bromobenzene
Benzo[a]pyrene-4,5-oxide + Glutathione <> 4,5-Dihydro-4-hydroxy-5-S-glutathionyl-benzo[a]pyrene
Benzo[a]pyrene-7,8-diol + Glutathione <> 7,8-Dihydro-7-hydroxy-8-S-glutathionyl-benzo[a]pyrene + Water
2,2-Dichloroacetaldehyde + Glutathione <> S-(2,2-Dichloro-1-hydroxy)ethyl glutathione
1,1-Dichloroethylene epoxide + Glutathione <> 2-(S-Glutathionyl)acetyl chloride + Hydrochloric acid
2,2-Dichloroacetaldehyde + Glutathione <> S-(2-Chloroacetyl)glutathione + Hydrochloric acid
2-(S-Glutathionyl)acetyl chloride + Glutathione <> 2-(S-Glutathionyl)acetyl glutathione + Hydrochloric acid
Trichloroethene + Glutathione <> S-(1,2-Dichlorovinyl)glutathione + Hydrochloric acid
1,2-Dibromoethane + Glutathione + Hydrogen ion <> Glutathione episulfonium ion +2 Hydrobromic acid
2-Bromoacetaldehyde + Glutathione <> S-(Formylmethyl)glutathione + Hydrobromic acid
Aldophosphamide + Glutathione <> 4-Glutathionyl cyclophosphamide + Water
Aflatoxin B1-exo-8,9-epoxide + Glutathione <> Aflatoxin B1exo-8,9-epoxide-GSH
Selenite + Glutathione + Hydrogen ion > Selenodiglutathione + Glutathione disulfide + Water
Glutathione + Adenosine triphosphate + Water > Glutathione + ADP + Phosphate + Hydrogen ion
Glutathione + Adenosine triphosphate + Water > Glutathione + ADP + Phosphate + Hydrogen ion
2-hydroxyethyldisulfide + Glutathione 2-mercaptoethanol + Glutathione disulfide
bromoacetate + Glutathione Hydrogen ion + glutathione-S-acetate + Br<SUP>-</SUP>
Hydrogen peroxide + Glutathione > Glutathione disulfide + Water
Glutathione + NADP < Glutathione disulfide + NADPH + Hydrogen ion
Glycine + gamma-Glutamylcysteine + Adenosine triphosphate > Hydrogen ion + Glutathione + Phosphate + ADP
S-Lactoylglutathione < Pyruvaldehyde + Glutathione
Glutathionylspermidine + Water > Glutathione + Spermidine
Spermidine + Glutathione + Adenosine triphosphate > Hydrogen ion + Glutathionylspermidine + ADP + Phosphate
1-chloro-2,4-dinitrobenzene + Glutathione <> Hydrogen ion + 2,4-dinitrophenyl-S-glutathione + Chloride
S-(Hydroxymethyl)glutathione <> Formaldehyde + Glutathione
S-Formylglutathione + Water > Hydrogen ion + Formic acid + Glutathione
S-(2-hydroxyacyl)glutathione + Water > Glutathione + a 2-hydroxy carboxylate
Adenosine triphosphate + gamma-Glutamylcysteine + Glycine > ADP + Inorganic phosphate + Glutathione
2 Glutathione + NADP > Glutathione disulfide + NADPH
Glutathione + Spermidine + Adenosine triphosphate > Glutathionylspermidine + ADP + Inorganic phosphate
RX + Glutathione > HX + R-S-glutathione
S-Lactoylglutathione > Glutathione + Pyruvaldehyde
S-Formylglutathione + Water > Glutathione + Formic acid
RX + Glutathione <> Halide + R-S-Glutathione
S-(2-Hydroxyacyl)glutathione + Water <> Glutathione + 2-Hydroxy carboxylate
gamma-Glutamylcysteine + Glycine + Adenosine triphosphate > Hydrogen ion + Phosphate + Adenosine diphosphate + Glutathione + ADP
Oxidized glutathione + Hydrogen ion + NADPH + Glutathione disulfide + NADPH > NADP +2 Glutathione
Naphthalene epoxide + Glutathione + (1R,2S)-Naphthalene 1,2-oxide > (1R)-Glutathionyl-(2R)-hydroxy-1,2-dihydronaphthalene
Naphthalene epoxide + Glutathione + (1R,2S)-Naphthalene 1,2-oxide > (1R)-Hydroxy-(2R)-glutathionyl-1,2-dihydronaphthalene
Glutathione + Naphthalene epoxide + (1R,2S)-Naphthalene 1,2-oxide > (1S)-Hydroxy-(2S)-glutathionyl-1,2-dihydronaphthalene
Glutathione + 1-Nitronaphthalene-5,6-oxide > 1-Nitro-5-glutathionyl-6-hydroxy-5,6-dihydronaphthalene
1-Nitronaphthalene-5,6-oxide + Glutathione > 1-Nitro-5-hydroxy-6-glutathionyl-5,6-dihydronaphthalene
Glutathione + 1-Nitronaphthalene-7,8-oxide > 1-Nitro-7-glutathionyl-8-hydroxy-7,8-dihydronaphthalene
1-Nitronaphthalene-7,8-oxide + Glutathione > 1-Nitro-7-hydroxy-8-glutathionyl-7,8-dihydronaphthalene
Glutathione + 2,2-Dichloroacetaldehyde > S-(Formylmethyl)glutathione
Glutathione + Bromobenzene-2,3-oxide > 2,3-Dihydro-2-S-glutathionyl-3-hydroxy bromobenzene
Glutathione + 2-(S-Glutathionyl)acetyl chloride > 2-(S-Glutathionyl)acetyl glutathione + Hydrochloric acid
Bromobenzene-3,4-oxide + Glutathione < 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzene
Pyruvaldehyde + Glutathione > S-Lactoylglutathione
S-Lactoylglutathione + Water > Glutathione + Hydrogen ion + L-Lactic acid
Adenosine triphosphate + gamma-Glutamylcysteine + Glycine <> ADP + Glutathione + Hydrogen ion + Phosphate
RX + Glutathione <> Halide + R-S-Glutathione
1-Nitronaphthalene-7,8-oxide + Glutathione <> 1-Nitro-7-hydroxy-8-glutathionyl-7,8-dihydronaphthalene
Glutathione + Water > Cysteinylglycine + L-Glutamate
Glutathione disulfide + Hydrogen ion + NADPH <>2 Glutathione + NADP
Glutathione + Pyruvaldehyde <> S-Lactoylglutathione
S-Formylglutathione + Water <> Formic acid + Glutathione + Hydrogen ion
Glutathione disulfide + Hydrogen ion + NADPH <>2 Glutathione + NADP
Glutathione + Water > Cysteinylglycine + L-Glutamate
More...

SMPDB Pathways:
Arachidonic acid metabolismPW000759 ThumbThumb?image type=greyscaleThumb?image type=simple
Glutathione metabolismPW000833 ThumbThumb?image type=greyscaleThumb?image type=simple
Selenium metabolismPW001894 ThumbThumb?image type=greyscaleThumb?image type=simple
glutathione metabolism IIPW001927 ThumbThumb?image type=greyscaleThumb?image type=simple
glutathione metabolism IIIPW002018 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
16600± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
17600± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
7970± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
51± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (x TMS)splash10-0a4i-0900000000-5841845f736f9a667622View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (x TMS)splash10-0a4i-0900000000-bdecde153761cb67852eView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-0900000000-5841845f736f9a667622View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-0900000000-bdecde153761cb67852eView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0a4i-1910000000-52bc43dd913b68d74f84View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-08fs-3960000000-63ce34def2ae94b95515View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Non-derivatized)splash10-0pb9-0921000000-88168b0a9f5fc5fead3fView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-7890000000-5853006f66d946dd3d2eView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-0596-9112300000-e82cf72540c283d8e323View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_1) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_2) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_3) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_4) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_5) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_1_6) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_2) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_3) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_4) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_5) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_6) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_7) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_8) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_9) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_10) - 70eV, PositiveNot AvailableView in JSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-004i-3795000000-d019cd7dcbad1f8a9e78View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-003r-9400000000-a83bf6292d41988256e3View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-001i-9000000000-305a92f8a9ffea58fa0eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-0009000000-e950bfc5867b391c6960View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-004i-0910000000-83f6c079d1112e74ecf4View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-003r-0910000000-5b243cf8bd357ab270b1View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-0009000000-29ef335479f56b620d88View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0a4i-0009001000-d1f5986166efa523d024View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-056s-0495300000-dba7be381fd1ef776527View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-004i-0920000000-de5b8a5a377324599b39View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-053r-0007920000-7500cef211e48c8ea244View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0119003000-4eb7ed4e2a4cf6a83c66View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0uki-0290000000-6893386899c6eed6a1a6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-05g0-0190000000-cacc2de4ab18ed59798bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0009000000-6b4268add43ab66ef015View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-08fr-0015009000-a01bdc13a34d6ce8416fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0uki-0290000000-ea94ec8247b4e025adbeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0039210000-e1f721157a9ea89959d6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a59-0039210000-35ce450ea95922abf0e1View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-0a4i-0009000000-9b01fba547d1fcde113aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-0006-0952000000-4a2a42699cf4aab2c559View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-002f-2900000000-bd9ba27b48b1322b7618View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Negativesplash10-004m-5900000000-cc7184d5bba50e6e49d0View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Negativesplash10-0a4i-9200000000-aecd0eb18a10c3ffb7abView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0729-4492000000-78a928563adf9038ba59View in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. Pubmed: 11978879
  • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. Pubmed: 19561621
  • Briz O, Romero MR, Martinez-Becerra P, Macias RI, Perez MJ, Jimenez F, San Martin FG, Marin JJ: OATP8/1B3-mediated cotransport of bile acids and glutathione: an export pathway for organic anions from hepatocytes? J Biol Chem. 2006 Oct 13;281(41):30326-35. Epub 2006 Jul 28. Pubmed: 16877380
  • 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
  • Calvo-Marzal P, Chumbimuni-Torres KY, Hoehr NF, Kubota LT: Determination of glutathione in hemolysed erythrocyte with amperometric sensor based on TTF-TCNQ. Clin Chim Acta. 2006 Sep;371(1-2):152-8. Epub 2006 May 2. Pubmed: 16650398
  • Czeczot H, Scibior D, Skrzycki M, Podsiad M: Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma. Acta Biochim Pol. 2006;53(1):237-42. Epub 2006 Jan 9. Pubmed: 16404476
  • Czeczot H, Scibior D, Skrzycki M, Podsiad M: [Antioxidant barrier in patients with gastric cancer--preliminary study] Pol Merkur Lekarski. 2005 Oct;19(112):521-5. Pubmed: 16379316
  • Djurhuus R, Segadal K, Svardal AM: Glutathione in blood cells decreases without DNA breaks after a simulated saturation dive to 250 msw. Aviat Space Environ Med. 2006 Jun;77(6):597-604. Pubmed: 16780237
  • Drevet JR: The antioxidant glutathione peroxidase family and spermatozoa: a complex story. Mol Cell Endocrinol. 2006 May 16;250(1-2):70-9. Epub 2006 Jan 19. Pubmed: 16427183
  • Grattagliano I, Portincasa P, Palmieri VO, Palasciano G: Contribution of canalicular glutathione efflux to bile formation. From cholestasis associated alterations to pharmacological intervention to modify bile flow. Curr Drug Targets Immune Endocr Metabol Disord. 2005 Jun;5(2):153-61. Pubmed: 16089347
  • Hung CR: Effect of lysozyme chloride on betel quid chewing aggravated gastric oxidative stress and hemorrhagic ulcer in diabetic rats. World J Gastroenterol. 2005 Oct 7;11(37):5853-8. Pubmed: 16270397
  • Iida M, Yasuhara T, Mochizuki H, Takakura H, Yanagisawa T, Kubo H: Two Japanese brothers with hereditary gamma-glutamyl transpeptidase deficiency. J Inherit Metab Dis. 2005;28(1):49-55. Pubmed: 15702405
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Iwasaki Y, Hoshi M, Ito R, Saito K, Nakazawa H: Analysis of glutathione and glutathione disulfide in human saliva using hydrophilic interaction chromatography with mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Jul 24;839(1-2):74-9. Epub 2006 Apr 18. Pubmed: 16621738
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Kawakami Y, Monobe M, Kuwabara K, Fujita T, Maeda M, Fujino O, Kojima S, Fukunaga Y: A comparative study of nitric oxide, glutathione, and glutathione peroxidase activities in cerebrospinal fluid from children with convulsive diseases/children with aseptic meningitis. Brain Dev. 2006 May;28(4):243-6. Epub 2006 Jan 10. Pubmed: 16376049
  • Kaynar H, Meral M, Turhan H, Keles M, Celik G, Akcay F: Glutathione peroxidase, glutathione-S-transferase, catalase, xanthine oxidase, Cu-Zn superoxide dismutase activities, total glutathione, nitric oxide, and malondialdehyde levels in erythrocytes of patients with small cell and non-small cell lung cancer. Cancer Lett. 2005 Sep 28;227(2):133-9. Epub 2005 Jan 8. Pubmed: 16112416
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. Pubmed: 15882454
  • Oztezcan S, Balkan J, Dogru-Abbasoglu S, Cevikbas U, Aykac-Toker G, Uysal M: Resistance of erythrocytes to lipid peroxidation in cirrhotic rats. Arch Med Res. 2005 Sep-Oct;36(5):459-63. Pubmed: 16099321
  • Schulpis KH, Papassotiriou I, Parthimos T, Tsakiris T, Tsakiris S: The effect of L-cysteine and glutathione on inhibition of Na+, K+-ATPase activity by aspartame metabolites in human erythrocyte membrane. Eur J Clin Nutr. 2006 May;60(5):593-7. Pubmed: 16391576
  • Sohlenius-Sternbeck AK, Schmidt S: Impaired glutathione-conjugating capacity by cryopreserved human and rat hepatocytes. Xenobiotica. 2005 Jul;35(7):727-36. Pubmed: 16316931
  • Struzynska L, Chalimoniuk M, Sulkowski G: The role of astroglia in Pb-exposed adult rat brain with respect to glutamate toxicity. Toxicology. 2005 Sep 1;212(2-3):185-94. Pubmed: 15955607
  • Tsai CC, Chen HS, Chen SL, Ho YP, Ho KY, Wu YM, Hung CC: Lipid peroxidation: a possible role in the induction and progression of chronic periodontitis. J Periodontal Res. 2005 Oct;40(5):378-84. Pubmed: 16105090
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Wielandt AM, Vollrath V, Farias M, Chianale J: Bucillamine induces glutathione biosynthesis via activation of the transcription factor Nrf2. Biochem Pharmacol. 2006 Aug 14;72(4):455-62. Epub 2006 Jun 27. Pubmed: 16806086
  • Witschi A, Reddy S, Stofer B, Lauterburg BH: The systemic availability of oral glutathione. Eur J Clin Pharmacol. 1992;43(6):667-9. Pubmed: 1362956
  • Wu G, Fang YZ, Yang S, Lupton JR, Turner ND: Glutathione metabolism and its implications for health. J Nutr. 2004 Mar;134(3):489-92. Pubmed: 14988435
  • Yim CY, Hibbs JB Jr, McGregor JR, Galinsky RE, Samlowski WE: Use of N-acetyl cysteine to increase intracellular glutathione during the induction of antitumor responses by IL-2. J Immunol. 1994 Jun 15;152(12):5796-805. Pubmed: 8207209
  • Zamek-Gliszczynski MJ, Hoffmaster KA, Nezasa K, Tallman MN, Brouwer KL: Integration of hepatic drug transporters and phase II metabolizing enzymes: mechanisms of hepatic excretion of sulfate, glucuronide, and glutathione metabolites. Eur J Pharm Sci. 2006 Apr;27(5):447-86. Epub 2006 Feb 10. Pubmed: 16472997
Synthesis Reference:Not Available
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID16856
HMDB IDHMDB00125
Pubchem Compound ID124886
Kegg IDC00051
ChemSpider ID111188
WikipediaGlutathione
BioCyc IDGLUTATHIONE
EcoCyc IDGLUTATHIONE
Ligand ExpoGTT

Enzymes

General function:
Involved in ATP binding
Specific function:
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Gene Name:
gshB
Uniprot ID:
P04425
Molecular weight:
35561
Reactions
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.
General function:
Involved in glutathione peroxidase activity
Specific function:
Not essential for B12 transport; however, it is an auxiliary component of the transport system
Gene Name:
btuE
Uniprot ID:
P06610
Molecular weight:
20469
General function:
Involved in oxidoreductase activity
Specific function:
Maintains high levels of reduced glutathione in the cytosol
Gene Name:
gor
Uniprot ID:
P06715
Molecular weight:
48772
Reactions
2 glutathione + NADP(+) = glutathione disulfide + NADPH.
General function:
Involved in protein binding
Specific function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Gene Name:
gst
Uniprot ID:
P0A9D2
Molecular weight:
22868
Reactions
RX + glutathione = HX + R-S-glutathione.
General function:
Involved in arsenate reductase (glutaredoxin) activity
Specific function:
Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of ArsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance
Gene Name:
arsC
Uniprot ID:
P0AB96
Molecular weight:
15853
Reactions
Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H(2)O.
General function:
Involved in lactoylglutathione lyase activity
Specific function:
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione
Gene Name:
gloA
Uniprot ID:
P0AC81
Molecular weight:
14920
Reactions
(R)-S-lactoylglutathione = glutathione + methylglyoxal.
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:
gloB
Uniprot ID:
P0AC84
Molecular weight:
28434
Reactions
S-(2-hydroxyacyl)glutathione + H(2)O = glutathione + a 2-hydroxy carboxylate.
General function:
Amino acid transport and metabolism
Specific function:
Catalyzes the formation of an amide bond between glutathione and spermidine coupled with hydrolysis of ATP; also catalyzes the hydrolysis of glutathionylspermidine to glutathione and spermidine
Gene Name:
gsp
Uniprot ID:
P0AES0
Molecular weight:
70531
Reactions
Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate.
Glutathionylspermidine + H(2)O = glutathione + spermidine.
General function:
Involved in gamma-glutamyltransferase activity
Specific function:
(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid
Gene Name:
ggt
Uniprot ID:
P18956
Molecular weight:
61768
Reactions
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
Glutathione + H(2)O = L-cysteinylglycine + L-glutamate.
General function:
Involved in carboxylesterase activity
Specific function:
Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids
Gene Name:
yeiG
Uniprot ID:
P33018
Molecular weight:
31259
Reactions
S-formylglutathione + H(2)O = glutathione + formate.
General function:
Involved in carboxylesterase activity
Specific function:
Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against two pNP-esters (pNP- acetate and pNP-propionate), alpha-naphthyl acetate and lactoylglutathione
Gene Name:
frmB
Uniprot ID:
P51025
Molecular weight:
31424
Reactions
S-formylglutathione + H(2)O = glutathione + formate.
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppB
Uniprot ID:
P0AFH2
Molecular weight:
33443
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppC
Uniprot ID:
P0AFH6
Molecular weight:
33022
General function:
Involved in nucleotide binding
Specific function:
Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system
Gene Name:
cydC
Uniprot ID:
P23886
Molecular weight:
62920
General function:
Involved in nucleotide binding
Specific function:
Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system
Gene Name:
cydD
Uniprot ID:
P29018
Molecular weight:
65055
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane (Probable)
Gene Name:
gsiC
Uniprot ID:
P75798
Molecular weight:
34066
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane (Probable)
Gene Name:
gsiD
Uniprot ID:
P75799
Molecular weight:
33238
General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import. Responsible for energy coupling to the transport system
Gene Name:
gsiA
Uniprot ID:
P75796
Molecular weight:
69113
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro
Gene Name:
dsbG
Uniprot ID:
P77202
Molecular weight:
27495
General function:
Involved in electron carrier activity
Specific function:
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (Probable)
Gene Name:
grxD
Uniprot ID:
P0AC69
Molecular weight:
12879
General function:
Involved in cell redox homeostasis
Specific function:
Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD
Gene Name:
dsbC
Uniprot ID:
P0AEG6
Molecular weight:
25622
General function:
Involved in electron carrier activity
Specific function:
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 some disulfides in a coupled system with glutathione reductase
Gene Name:
grxC
Uniprot ID:
P0AC62
Molecular weight:
9137
General function:
Involved in protein binding
Specific function:
Involved in reducing some disulfides in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase
Gene Name:
grxB
Uniprot ID:
P0AC59
Molecular weight:
24350
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import
Gene Name:
gsiB
Uniprot ID:
P75797
Molecular weight:
56470
General function:
Involved in electron carrier activity
Specific function:
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 some disulfides in a coupled system with glutathione reductase
Gene Name:
grxA
Uniprot ID:
P68688
Molecular weight:
9685
General function:
Not Available
Specific function:
Not Available
Gene Name:
yfcG
Uniprot ID:
P77526
Molecular weight:
Not Available

Transporters

General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppB
Uniprot ID:
P0AFH2
Molecular weight:
33443
General function:
Involved in transporter activity
Specific function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane
Gene Name:
oppC
Uniprot ID:
P0AFH6
Molecular weight:
33022
General function:
Involved in transporter activity
Specific function:
Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides
Gene Name:
sapB
Uniprot ID:
P0AGH3
Molecular weight:
36038
General function:
Involved in transporter activity
Specific function:
Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides
Gene Name:
sapC
Uniprot ID:
P0AGH5
Molecular weight:
31548
General function:
Involved in peptide transporter activity
Specific function:
Proton-dependent permease that transports di- and tripeptides. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate
Gene Name:
dtpB
Uniprot ID:
P36837
Molecular weight:
53575
General function:
Involved in peptide transporter activity
Specific function:
Probable proton-dependent permease that transports di- and tripeptides. Shows significantly higher specificity towards dipeptides
Gene Name:
yjdL
Uniprot ID:
P39276
Molecular weight:
53054
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane (Probable)
Gene Name:
gsiC
Uniprot ID:
P75798
Molecular weight:
34066
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane (Probable)
Gene Name:
gsiD
Uniprot ID:
P75799
Molecular weight:
33238
General function:
Involved in peptide transporter activity
Specific function:
Proton-dependent permease that transports di- and tripeptides as well as structurally related peptidomimetics such as aminocephalosporins into the cell. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate
Gene Name:
dtpA
Uniprot ID:
P77304
Molecular weight:
53991
General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import. Responsible for energy coupling to the transport system
Gene Name:
gsiA
Uniprot ID:
P75796
Molecular weight:
69113
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Involved in transporter activity
Specific function:
Part of the ABC transporter complex gsiABCD involved in glutathione import
Gene Name:
gsiB
Uniprot ID:
P75797
Molecular weight:
56470
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368