P. aeruginosa Metabolome Database: Glutathione disulfide (PAMDB001629)

Identification Taxonomy Physical Properties Biological Properties Spectra Concentrations Links References Enzymes Transporters

Proteins (3280)

Record Information

Version

1.0

Update Date

1/22/2018 12:54:54 PM

Metabolite ID

PAMDB001629

Identification

Name:

Glutathione disulfide

Description:

Glutathione (GSH) is a tripeptide with a gamma peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. Glutathione is a cofactor for the enzyme glutathione peroxidase. 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 (EC 4.4.1.5) catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase (EC 3.1.2.6) catalyzes the hydrolysis of S-D-Lactoyl-glutathione to glutathione and D-lactate.; Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules.

Structure

🔍MOL SDF PDB SMILES InChI View Structure

Synonyms:

(2S,2'S)-5,5'-[disulfanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoate)
(2S,2'S)-5,5'-[disulfanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoate) (non-preferred name)
(2S,2'S)-5,5'-[disulfanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoic acid)
(2S,2'S)-5,5'-[disulfanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoic acid) (non-preferred name)
(2S,2'S)-5,5'-[disulphanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoate)
(2S,2'S)-5,5'-[disulphanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoate) (non-preferred name)
(2S,2'S)-5,5'-[disulphanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoic acid)
(2S,2'S)-5,5'-[disulphanediylbis({(2R)-3-[(carboxymethyl)amino]-3-oxopropane-1,2-diyl}imino)]bis(2-amino-5-oxopentanoic acid) (non-preferred name)
Glutathione disulfide
Glutathione disulphide
Glutathione ox
Glutathione oxidized
GSSG
L(-)-Glutathione(oxidized)
L-Glutathione oxidized
Oxidised glutathione
Oxidized glutathione
OXIDIZED GLUTATHIONE DISULFIDE
OXIDIZED glutathione disulphide
Oxiglutatione

Chemical Formula:

C₂₀H₃₂N₆O₁₂S₂

Average Molecular Weight:

612.631

Monoisotopic Molecular Weight:

612.151961898

InChI Key:

YPZRWBKMTBYPTK-UHFFFAOYSA-N

InChI:

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)

CAS number:

27025-41-8

IUPAC Name:

(2S)-2-amino-4-{[(1R)-2-{[(2R)-2-[(4S)-4-amino-4-carboxybutanamido]-2-[(carboxymethyl)carbamoyl]ethyl]disulfanyl}-1-[(carboxymethyl)carbamoyl]ethyl]carbamoyl}butanoic acid

Traditional IUPAC Name:

glutathione disulfide

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

Chemical Taxonomy

Taxonomy Description

This compound belongs to the class of organic compounds known as gamma-glutamyl peptides. These are oligo- and polypeptides consisting of any C-terminal alpha peptide having a gamma-glutamyl residue attached at the N alpha-position.

Kingdom

Organic compounds

Super Class

Organic acids and derivatives

Class

Carboxylic acids and derivatives

Sub Class

Amino acids, peptides, and analogues

Direct Parent

Gamma-glutamyl peptides

Alternative Parents

Substituents

Gamma-glutamyl alpha peptide
N-acyl-aliphatic-alpha amino acid
Tetracarboxylic acid or derivatives
N-acyl-alpha amino acid or derivatives
N-acyl-alpha-amino acid
Alpha-amino acid amide
L-alpha-amino acid
Alpha-amino acid or derivatives
N-substituted-alpha-amino acid
Alpha-amino acid
Amino fatty acid
Fatty acyl
N-acyl-amine
Fatty amide
Dialkyldisulfide
Secondary carboxylic acid amide
Organic disulfide
Carboxamide group
Sulfenyl compound
Carboxylic acid
Carboxylic acid amide
Hydrocarbon derivative
Primary amine
Organosulfur compound
Organooxygen compound
Organonitrogen compound
Primary aliphatic amine
Carbonyl group
Amine
Aliphatic acyclic compound

Molecular Framework

Aliphatic acyclic compounds

External Descriptors

organic disulfide (CHEBI:17858 )
glutathione derivative (CHEBI:17858 )

Physical Properties

State:

Solid

Charge:

-2

Melting point:

Not Available

Experimental Properties:

Property	Value	Source

Predicted Properties

Property	Value	Source
Water Solubility	0.406 mg/mL	ALOGPS
logP	-3.6	ALOGPS
logP	-10	ChemAxon
logS	-3.2	ALOGPS
pKa (Strongest Acidic)	1.44	ChemAxon
pKa (Strongest Basic)	9.61	ChemAxon
Physiological Charge	-2	ChemAxon
Hydrogen Acceptor Count	14	ChemAxon
Hydrogen Donor Count	10	ChemAxon
Polar Surface Area	317.64 Å²	ChemAxon
Rotatable Bond Count	21	ChemAxon
Refractivity	136.65 m³·mol^-1	ChemAxon
Polarizability	58.47 Å³	ChemAxon
Number of Rings	0	ChemAxon
Bioavailability	0	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	Yes	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Biological Properties

Cellular Locations:

Cytoplasm

Reactions:

Pathways:

Arachidonic acid metabolism pae00590
Glutathione metabolism pae00480

Spectra

Spectra:

Spectrum Type	Description	Splash Key
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-0292-1000291000-9683d81eec1eab3f9883	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-01u0-8214980000-1738ea6e3b4537936eee	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-057i-9534520000-7ef32e723a98599c32d7	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-03di-0147096000-e516803ef5124daee1a7	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-0a4l-2497151000-ef5ab8f9bbe20555f37c	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-006y-9411230000-cc41719d1e717d214643	View in MoNA
1D NMR	1H NMR Spectrum	Not Available

References

References:

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
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
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
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

Synthesis Reference:

Not Available

Material Safety Data Sheet (MSDS)

Download (PDF)

Links

External Links:

Resource	Link
CHEBI ID	17858
HMDB ID	HMDB03337
Pubchem Compound ID	975
Kegg ID	C00127
ChemSpider ID	58835
Wikipedia	Glutathione_disulfide
BioCyc ID	OXIDIZED-GLUTATHIONE
EcoCyc ID	OXIDIZED-GLUTATHIONE
Ligand Expo	GDS

Enzymes

Protein Details

• Glutathione reductase

General function:: Involved in oxidoreductase activity
Specific function:: Maintains high levels of reduced glutathione in the cytosol
Gene Name:: gor
Locus Tag:: PA2025
Molecular weight:: 49.2 kDa

Reactions

2 glutathione + NADP(+) = glutathione disulfide + NADPH.

Protein Details

• Arsenate reductase

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
Locus Tag:: PA2279
Molecular weight:: 16.6 kDa

Reactions

Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H(2)O.

Protein Details

• Thiol:disulfide interchange protein DsbG

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
Locus Tag:: PA2476
Molecular weight:: 28.1 kDa

Protein Details

• Glutaredoxin-4

General function:: Involved in electron carrier activity
Specific function:: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (Probable)
Gene Name:: grxD
Locus Tag:: PA3533
Molecular weight:: 11.8 kDa

Protein Details

• Thiol:disulfide interchange protein DsbC

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
Locus Tag:: PA3737
Molecular weight:: 26.1 kDa

Protein Details

• Glutaredoxin-3

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
Locus Tag:: PA5129
Molecular weight:: 9.2 kDa

Glutathione disulfide (PAMDB001629)

Structure for Glutathione disulfide (PAMDB001629)

Enzymes

Reactions

Reactions

Transporters