glutathione

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glutathione:

see coenzymecoenzyme
, any one of a group of relatively small organic molecules required for the catalytic function of certain enzymes. A coenzyme may either be attached by covalent bonds to a particular enzyme or exist freely in solution, but in either case it participates intimately in
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.

Glutathione

 

γ-glutamyl cysteinyl glycine, a tripep-tide formed from radicals of three amino acids—glutamic acid, cysteine, and glycine. A peculiarity of the structure of glutathione is the peptide bond between cysteine and glutamic acid, in which the γ-carboxyl of the glutamic acid participates. Glutathione is present in all living organisms and is very important for oxidation-reduction reactions in connection with the capacity of the sulfhydryl group (SH—) of cysteine to undergo the reversible reaction

Glutathione can act as a coenzyme in the action of cathepsins, papain, and other proteolytic enzymes. The function of glutathione in metabolism apparently also includes the protection of the SH group of cytoplasm proteins against oxidation.

glutathione

[¦glüd·ə′thī‚ōn]
(biochemistry)
C10H17O6N3S A widely distributed tripeptide that is important in plant and animal tissue oxidation reactions.
References in periodicals archive ?
Williams, "Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni," Biochemistry, vol.
This article was derived from a master's degree thesis conducted in 2015, entitled: "The effects of copenhagen football test on glutathione reductase and catalase activity in female football players" with the code 20021404931002.
Jiang, F., et al., Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120.
Mannervik, Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver, Biochim Biophys Acta, 582:67-78 (1979).
Anderson, "Simultaneous inactivation of the catalytic activities of yeast glutathione reductase by N-alkylmaleimides," Biochimica et Biophysica Acta, vol.
Recent efforts have made available a large repertoire of molecular activities screened for inhibition of thioredoxin glutathione reductase of Schistosoma mansoni [20, 21].
[14] reported that dextran coated ferrite nanoparticles failed to induce delayed hypersensitivity or did not significantly alter the level of lipid peroxidation, reduced glutathione, glutathione reductase, glutathione peroxidase, superoxide dismutase, or oxidative stress related DNA damage.
STZ, DL-dithiothreitol (DTT), glutathione, 5,5,-dithiobis(2)-nitrobenzoic acid (DTNB), sodium nitrate, vanadium (III) chloride, sulphanilamide, N-(1-naphthyl)ethylenediamine, glutathione reductase, epinephrine hydrochloride, [beta]-nicotinamide adenine dinucleotide 27-phosphate reduced tetrasodium salt hydrate, and L-glutathione oxidized disodium salt were obtained from SigmaAldrich (St.
Cervinkova, "Glutathione reductase is inhibited by acetaminophen-glutathione conjugate in vitro," Physiological Research, vol.
Considering their importance, scientists evaluated the enzymatic activities of superoxide dismutase, guaiacol peroxidase and glutathione reductase, as well as the hydrogen peroxide content during the drying of two types of coffee bean, one processed as natural coffee and the other as pulped natural coffee.
In cells, glutathione is maintained in the reduced form by the enzyme glutathione reductase, which in turn reduces other metabolites and enzyme systems, such as ascorbate (in the glutathione-ascorbate cycle), glutathione peroxidases and glutaredoxins and reacts directly with oxidants (50, 53).
2004; Thomas 2009); and d) inhibiting glutathione reductase, thereby limiting the regeneration of GSH from GSSG (Massey and Williams 1965; Styblo et al.

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