Glutathione (ECMDB00125) (M2MDB000048)
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Version | 2.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Creation Date | 2012-05-31 10:21:27 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Update Date | 2015-09-13 12:56:06 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary Accession Numbers |
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Identification | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Name: | Glutathione | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Description | Glutathione (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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Synonyms: |
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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. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Kingdom | Organic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Super Class | Organic acids and derivatives | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Class | Carboxylic acids and derivatives | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sub Class | Amino acids, peptides, and analogues | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Direct Parent | Peptides | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Alternative Parents |
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Substituents |
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Molecular Framework | Aliphatic acyclic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
External Descriptors |
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Physical Properties | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
State: | Solid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Charge: | -1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Melting point: | 195 °C | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental Properties: |
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Predicted Properties |
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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 More...(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 | 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SMPDB Pathways: |
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KEGG Pathways: |
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EcoCyc Pathways: |
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Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Find out more about how we convert literature concentrations. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Spectra | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Spectra: | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
References | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
References: |
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Synthesis Reference: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Material Safety Data Sheet (MSDS) | Download (PDF) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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External Links: |
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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