Glutathione
... exists in reduced (GSH) and oxidized (GSSG) states. The ratio of reduced glutathione to oxidized glutathione within ... a tool to measure the cellular glutathione redox potential Glutathione-ascorbate cycle Bacterial glutathione transferase ... Glutathione enhances the function of citrulline as part of the nitric oxide cycle. It is a cofactor and acts on glutathione ... In plants, glutathione is involved in stress management. It is a component of the glutathione-ascorbate cycle, a system that ...
Glutathione synthetase
... (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the ... For instance, glutathione peroxidases catalyze the oxidation of GSH to glutathione disulfide (GSSG) by reducing free radicals ... Glutathione synthetase deficiency Glutathione Liver Sulfur Metabolism Gogos A, Shapiro L (Dec 2002). "Large conformational ... such as H2O2 or Glutathione S-transferases in the detoxification of xenobiotics. Glutathione synthetase is important for a ...
Glutathione thiolesterase
It is also called citryl-glutathione thioesterhydrolase. Kielley WW, Bradley LB (1954). "Glutathione thiolesterase". J. Biol. ... The enzyme glutathione thiolesterase (EC 3.1.2.7) catalyzes the reaction S-acylglutathione + H2O ⇌ {\displaystyle \ ... rightleftharpoons } glutathione + a carboxylate This enzyme belongs to the family of hydrolases, specifically those acting on ...
Glutathione disulfide
... (GSSG) is a disulfide derived from two glutathione molecules. In living cells, glutathione disulfide is ... Glutathione-ascorbate cycle Antioxidant Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry. 52: 711-60 ... This reaction is catalyzed by the enzyme glutathione reductase. Antioxidant enzymes, such as glutathione peroxidases and ... GSSG, along with glutathione and S-nitrosoglutathione (GSNO), have been found to bind to the glutamate recognition site of the ...
Glutathione hydrolase
Glutathione+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.19). ... Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. This enzyme catalyses the ... "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry. 32 (24 ... a key enzyme in glutathione metabolism, and its reaction intermediate". Proceedings of the National Academy of Sciences of the ...
Glutathione peroxidase
... was discovered in 1957 by Gordon C. Mills. Activity of glutathione peroxidase is measured ... Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially ... Zakowski JJ, Tappel AL (September 1978). "A semiautomated system for measurement of glutathione in the assay of glutathione ... RSeH Glutathione reductase then reduces the oxidized glutathione to complete the cycle: GS-SG + NADPH + H+ → 2 GSH + NADP+. ...
Glutathione reductase
... (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione ( ... In plants, reduced glutathione participates in the glutathione-ascorbate cycle in which reduced glutathione reduces ... Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the ... In particular, glutathione reductase appears to be a good target for anti-malarials, as the glutathione reductase of the ...
Glutathione oxidase
In enzymology, a glutathione oxidase (EC 1.8.3.3) is an enzyme that catalyzes the chemical reaction 2 glutathione + O2 ⇌ {\ ... The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione ... displaystyle \rightleftharpoons } glutathione disulfide + H2O2 Thus, the two substrates of this enzyme are glutathione and O2, ... Kusakabe H, Kuninaka A, Yoshino H (1982). "Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp ...
Glutathione synthetase deficiency
"Erythrocyte glutathione synthetase deficiency leads not only to glutathione but also to glutathione-S-transferase deficiency". ... Glutathione synthetase deficiency can be classified into three types: mild, moderate and severe. Mild glutathione synthetase ... Glutathione helps prevent damage to cells by neutralizing harmful molecules generated during energy production. Glutathione ... This cycle is necessary for producing a molecule called glutathione. Glutathione protects cells from damage caused by unstable ...
Glutathione-ascorbate cycle
Since glutathione, ascorbate and NADPH are present in high concentrations in plant cells it is assumed that the glutathione- ... yielding oxidized glutathione (GSSG). Finally GSSG is reduced by glutathione reductase (GR) using NADPH as the electron donor. ... such as glutathione S-transferase omega 1 or glutaredoxins. In plants, the glutathione-ascorbate cycle operates in the cytosol ... Thus ascorbate and glutathione are not consumed; the net electron flow is from NADPH to H2O2. The reduction of dehydroascorbate ...
Glutathione gamma-glutamylcysteinyltransferase
In enzymology, a glutathione gamma-glutamylcysteinyltransferase (EC 2.3.2.15) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase. Other ... the two substrates of this enzyme are glutathione and [Glu(-Cys)]n-Gly, whereas its two products are Gly and [Glu(-Cys)]n+1-Gly ... are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)". Proc ...
CoA-glutathione reductase
NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione ... In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction CoA + glutathione + ... glutathione, and NADP+, whereas its 3 products are CoA-glutathione, NADPH, and H+. This enzyme belongs to the family of ... The systematic name of this enzyme class is glutathione:NADP+ oxidoreductase (CoA-acylating). Other names in common use include ...
Glutathione amide reductase
... (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This ... glutathione amide disulfide + NADH + H+ Glutathione amide reductase is a dimeric flavoprotein (FAD). Vergauwen B, Pauwels F, ... Glutathione+amide+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.8.1) ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ...
Glutathione-homocystine transhydrogenase
This enzyme participates in methionine metabolism and glutathione metabolism. Racker E (December 1955). "Glutathione- ... glutathione disulfide + 2 homocysteine Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two ... In enzymology, a glutathione-homocystine transhydrogenase (EC 1.8.4.1) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. ...
Glutathione dehydrogenase (ascorbate)
... glutathione disulfide + ascorbate Thus, the two substrates of this enzyme are glutathione and dehydroascorbate, whereas its two ... In enzymology, a glutathione dehydrogenase (ascorbate) (EC 1.8.5.1) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:dehydroascorbate oxidoreductase. Other names in common use include ... Crook EM (March 1941). "The system dehydroascorbic acid-glutathione". The Biochemical Journal. 35 (3): 226-36. doi:10.1042/ ...
Bacterial glutathione transferase
Without glutathione in its reduced form, glutathione transferases are not able to utilize it as a substrate in redox reactions ... Glutathione transferases play a key role in catalyzing such reactions. Bacterial glutathione transferases of all classes are ... A GST monomer binds a glutathione molecule to its N-terminal glutathione-binding site. On the adjacent hydrophobic alpha- ... After completion of this reaction, glutathione reductase recycles oxidized glutathione back to the reduced form so that it ...
Glutathione S-transferase
Affinity chromatography Bacterial glutathione transferase Glutathione S-transferase Mu 1 Glutathione S-transferase, C-terminal ... Overview of Glutathione S-Transferases Glutathione+S-Transferase at the U.S. National Library of Medicine Medical Subject ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles ... "Glutathione S-transferase pull-down assays using dehydrated immobilized glutathione resin". Analytical Biochemistry. 322 (2): ...
Glutathione-cystine transhydrogenase
... glutathione disulfide + 2 cysteine Thus, the two substrates of this enzyme are glutathione and cystine, whereas its two ... In enzymology, a glutathione-cystine transhydrogenase (EC 1.8.4.4) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine ... This enzyme participates in cysteine metabolism and glutathione metabolism. Nagai S, Black S (1968). "A thiol-disulfide ...
Glutathione amide-dependent peroxidase
... (EC 1.11.1.17) is an enzyme with systematic name glutathione amide:hydrogen-peroxide ... Glutathione+amide-dependent+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ... This enzyme catalyses the following chemical reaction 2 glutathione amide + H2O2 ⇌ {\displaystyle \rightleftharpoons } ...
Glutathione-CoA-glutathione transhydrogenase
... glutathione-coenzyme A glutathione disulfide transhydrogenase, glutathione coenzyme A-glutathione transhydrogenase, glutathione ... CoA-glutathione + glutathione Thus, the two substrates of this enzyme are CoA and glutathione disulfide, whereas its two ... a glutathione-CoA-glutathione transhydrogenase (EC 1.8.4.3) is an enzyme that catalyzes the chemical reaction CoA + glutathione ... coenzyme A-glutathione transhydrogenase, coenzyme A:oxidized-glutathione oxidoreductase, and coenzyme A:glutathione-disulfide ...
Phospholipid-hydroperoxide glutathione peroxidase
... hydroperoxide glutathione peroxidase, or glutathione peroxidase 4 (GPX4). This enzyme participates in glutathione metabolism. ... glutathione disulfide + lipid + 2 H2O Thus, the two substrates of this enzyme are glutathione and lipid hydroperoxide, whereas ... glutathione, (phospholipid hydroperoxide-reducing), phospholipid hydroperoxide glutathione peroxidase, ... In enzymology, a phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) is an enzyme that catalyzes the chemical ...
Glutathione S-transferase A1
... is an enzyme that in humans is encoded by the GSTA1 gene. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTA1 glutathione S-transferase A1". Knapen, MF; Mulder, TP; Bisseling, JG; Penders, RH; Peters, WH; Steegers, EA ... This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped ... 1988). "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate ...
Protein-disulfide reductase (glutathione)
... glutathione disulfide + protein-dithiol Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas ... glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione), GSH-insulin transhydrogenase, protein- ... This enzyme participates in glutathione metabolism. As of late 2007, only one structure has been solved for this class of ... In enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction 2 ...
S-(hydroxymethyl)glutathione synthase
The systematic name of this enzyme class is S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming). Other names ... The enzyme S-(hydroxymethyl)glutathione synthase (EC 4.4.1.22) catalyzes the reaction S-(hydroxymethyl)glutathione ⇌ {\ ... Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA (February 2002). "A glutathione-dependent formaldehyde- ... in common use include glutathione-dependent formaldehyde-activating enzyme, Gfa, and S-(hydroxymethyl)glutathione formaldehyde- ...
Adenylyl-sulfate reductase (glutathione)
... and glutathione disulfide, whereas its two products are adenylyl sulfate and glutathione. This enzyme belongs to the family of ... glutathione disulfide ⇌ {\displaystyle \rightleftharpoons } adenylyl sulfate + 2 glutathione The 3 substrates of this enzyme ... Adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction AMP + sulfite + ... The systematic name of this enzyme class is AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate- ...
S-(hydroxymethyl)glutathione dehydrogenase
... glutathione) (incorrect), GS-FDH (incorrect), glutathione-dependent formaldehyde dehydrogenase (incorrect), NAD-dependent ... In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) is an enzyme that catalyzes the chemical reaction S ... The systematic name of this enzyme class is S-(hydroxymethyl)glutathione:NAD+ oxidoreductase. Other names in common use include ... Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF (2000). "Kinetic mechanism of human glutathione-dependent ...
Enzyme-thiol transhydrogenase (glutathione-disulfide)
2 glutathione Thus, the two substrates of this enzyme are xanthine dehydrogenase and glutathione disulfide, whereas its two ... oxidized-glutathione), glutathione-dependent thiol:disulfide oxidoreductase, and thiol:disulfide oxidoreductase. This enzyme ... In enzymology, an enzyme-thiol transhydrogenase (glutathione-disulfide) (EC 1.8.4.7) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase. Other names in ...
Glutathione S-transferase Mu 1
... (gene name GSTM1) is a human glutathione S-transferase. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTM1 glutathione S-transferase M1". Engel LS, Taioli E, Pfeiffer R, Garcia-Closas M, Marcus PM, Lan Q, et al. ( ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1 v t ... This gene encodes a cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in ...
Microsomal glutathione S-transferase 1
... is an enzyme that in humans is encoded by the MGST1 gene. The MAPEG family (Membrane- ... Cholon A, Giaccia AJ, Lewis AD (1992). "What role do glutathione S-transferases play in the cellular response to ionizing ... DeJong JL, Mohandas T, Tu CP (1990). "The gene for the microsomal glutathione S-transferase is on human chromosome 12". ... This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid ...
Glutathione S-transferase, C-terminal domain
... is a structural domain of glutathione S-transferase (GST). GST conjugates reduced ... GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol. Glutathione S- ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles ... The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed ...