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MetaCyc Pathway: glutathione redox reactions I

Enzyme View:

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Biosynthesis Cofactors, Prosthetic Groups, Electron Carriers Biosynthesis Reductants Biosynthesis

Some taxa known to possess this pathway include ? : Homo sapiens , Pisum sativum

Expected Taxonomic Range: Bacteria , Eukaryota

Summary:
General Background

Thiols such as glutathione play several major roles in the cell, including maintainance of the redox balance, fighting reactive oxygen and nitrogen species, and the detoxification of many other toxins and stress-inducing factors (see glutathione-mediated detoxification I). In most organisms the major thiol is the tripeptide glutathione (γ-Glu-Cys-Gly, known as GSH), whose intracellular concentration ranges from 0.5-10 mM (see γ-glutamyl cycle).

Most of the glutathione pool is kept in its reduced form. For example, in Escherichia coli, the ratio of reduced to oxidized glutathione is 200:1 [Ritz01]. The functionality of GSH largely depends on its being in a reduced form.

About This Pathway

One of the main roles of glutathione in the cell is the reduction of other molecules, such as peroxides or protein-disulfide groups. In this pathway the process is represnted by reaction EC 1.11.1.12

a lipid hydroperoxide + 2 glutathione + H+ → a lipid + glutathione disulfide + 2 H2O

In the process two molecules of GSH are condensed into a single molecule of the oxidized form, glutathione disulfide. In eukaryotes this oxidation reaction is often catalyzed by enzymes belonging to the glutathione peroxidase family. It was believed that glutathione-dependent peroxidases are not present in prokaryotic organisms, but recently some glutathione-dependent peroxidases have been discovered in bacteria [Pauwels03].

The glutathione disulfide is reduced back to GSH by the action of glutathione reductase.

Another redox cycle involving glutathione is described in glutathione redox reactions II.

Credits:
Created 14-Jul-2005 by Caspi R , SRI International


References

Arthur00: Arthur, J. R. (2000). "The glutathione peroxidases." Cell. Mol. Life Sci. 57:1825-1835.

Pauwels03: Pauwels F, Vergauwen B, Vanrobaeys F, Devreese B, Van Beeumen JJ (2003). "Purification and characterization of a chimeric enzyme from Haemophilus influenzae Rd that exhibits glutathione-dependent peroxidase activity." J Biol Chem 278(19);16658-66. PMID: 12606554

Ritz01: Ritz D, Beckwith J (2001). "Roles of thiol-redox pathways in bacteria." Annu Rev Microbiol 55;21-48. PMID: 11544348

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Akasaka90: Akasaka M, Mizoguchi J, Takahashi K (1990). "A human cDNA sequence of a novel glutathione peroxidase-related protein." Nucleic Acids Res 18(15);4619. PMID: 2388849

Anderson90: Anderson, James, Hess, John, Chevone, Boris "Purification, characterization, and immunological properties of two isoforms of glutathione reductase from Eastern white pine needles." Plant Physiology, 1990, 94:1402-1409.

Arenas10: Arenas FA, Diaz WA, Leal CA, Perez-Donoso JM, Imlay JA, Vasquez CC (2010). "The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions." Biochem Biophys Res Commun 398(4);690-4. PMID: 20621065

Bjornstedt94: Bjornstedt M, Xue J, Huang W, Akesson B, Holmgren A (1994). "The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase." J Biol Chem 269(47);29382-4. PMID: 7961915

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Broderick87: Broderick DJ, Deagen JT, Whanger PD (1987). "Properties of glutathione peroxidase isolated from human plasma." J Inorg Biochem 30(4);299-308. PMID: 3668526

Chu93: Chu FF, Doroshow JH, Esworthy RS (1993). "Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI." J Biol Chem 268(4);2571-6. PMID: 8428933

Edwards90: Edwards, E. Anne, Rawsthorne, Stephen, Mullineaux, Philip M. "Subcellular distribution of multiple forms of glutathione reductase in leaves of pea." Planta, 1990, 180:278-284.

Esworthy94: Esworthy RS, Doan K, Doroshow JH, Chu FF (1994). "Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase." Gene 144(2);317-8. PMID: 8039723

Flohe71: Flohe L, Eisele B, Wendel A (1971). "[Glutathion peroxidase. I. Isolation and determinations of molecular weight]." Hoppe Seylers Z Physiol Chem 352(2);151-8. PMID: 5549561

Flohe73: Flohe L, Gunzler WA, Schock HH (1973). "Glutathione peroxidase: a selenoenzyme." FEBS Lett 32(1);132-4. PMID: 4736708

Grossmann83: Grossmann A, Wendel A (1983). "Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids." Eur J Biochem 135(3);549-52. PMID: 6413205

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Henderson91: Henderson GB, Murgolo NJ, Kuriyan J, Osapay K, Kominos D, Berry A, Scrutton NS, Hinchliffe NW, Perham RN, Cerami A (1991). "Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction." Proc Natl Acad Sci U S A 88(19);8769-73. PMID: 1924337

Knapp04: Knapp KG, Swartz JR (2004). "Cell-free production of active E. coli thioredoxin reductase and glutathione reductase." FEBS Lett 559(1-3);66-70. PMID: 14960309

KrohneEhrich77: Krohne-Ehrich G, Schirmer RH, Untucht-Grau R (1977). "Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide." Eur J Biochem 80(1);65-71. PMID: 923580

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Mata84: Mata AM, Pinto MC, Lopez-Barea J (1984). "Purification by affinity chromatography of glutathione reductase (EC 1.6.4.2) from Escherichia coli and characterization of such enzyme." Z Naturforsch [C] 39(9-10);908-15. PMID: 6393625

Mills57: Mills, G. C. (1957). "Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown." J Biol Chem 229(1);189-97. PMID: 13491573

Nakashima76: Nakashima K, Miwa S, Yamauchi K (1976). "Human erythrocyte glutathione reductase. I. Purification and properties." Biochim Biophys Acta 445(2);309-23. PMID: 8143

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Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc13.