Results 291 to 300 of about 487,455 (339)
Some of the next articles are maybe not open access.
Physiologia Plantarum, 1997
Oxidative stress in plants causes the induction of several enzymes, including superoxide dismutase (EC 1.15.1.1), ascorbate peroxidase (EC 1.11.1.11) and glutathione reductase (EC 1.6.4.2). The first two are responsible for converting superoxide to H2O2 and its subsequent reduction to H2O, and the third is involved in recycling of ascorbate ...
Gozal Ben-Hayyim +3 more
openaire +2 more sources
Oxidative stress in plants causes the induction of several enzymes, including superoxide dismutase (EC 1.15.1.1), ascorbate peroxidase (EC 1.11.1.11) and glutathione reductase (EC 1.6.4.2). The first two are responsible for converting superoxide to H2O2 and its subsequent reduction to H2O, and the third is involved in recycling of ascorbate ...
Gozal Ben-Hayyim +3 more
openaire +2 more sources
Regulatory phenomena in the glutathione peroxidase superfamily.
Antioxidants and Redox Signaling, 2019Expression of glutathione peroxidases (GPxs) and the regulatory consequences of their action are reviewed. The selenium-containing GPXs 1-4 protect against oxidative challenge, inhibit inflammation and oxidant-induced regulated cell death.
R. Brigelius-Flohé, L. Flohé
semanticscholar +1 more source
Cellular and Molecular Life Sciences, 2001
There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
openaire +3 more sources
There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
openaire +3 more sources
[5] Diversity of glutathione peroxidases
1995Publisher Summary This chapter focuses on the diversity of glutathione peroxidases. Selenium was identified as a toxic factor for grazing animals in the first half of the twentieth century and since then has been considered hazardous. Only long after the identification of the first selenoenzymes in bacteria and mammals was a Recommended Dietary ...
URSINI, FULVIO +6 more
openaire +3 more sources
Selenoglutaredoxin as a Glutathione Peroxidase Mimic
ChemBioChem, 2008AbstractGlutaredoxin (Grx1) from Escherichia coli is a monomeric, 85‐amino‐acid‐long, disulfide‐containing redox protein. A Grx1 variant in which the redox‐active disulfide was replaced with a selenocysteine (C11U/C14S) was prepared by native chemical ligation from three fragments as a potential mimic of the natural selenoenzyme glutathione peroxidase (
Gerard Roelfes +2 more
openaire +3 more sources
Reaction of cyanide with glutathione peroxidase
Biochemical and Biophysical Research Communications, 1980An oxidized form of ovine erythrocyte GSH peroxidase (Form C) that contains bound glutathione in equimolar ratio to the enzyme selenium is inactivated by cyanide. When Form C was treated with 1 or 10 mM KCN at pH 7.5, there was a rapid increase in ultraviolet absorption at 250 nm, S-cyanoglutathione was released, and the enzyme was reduced, as shown by
Howard E. Ganther, Richard J. Kraus
openaire +3 more sources
2011
Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE +5 more
openaire +3 more sources
Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE +5 more
openaire +3 more sources
2016
Glutathione peroxidase 4 (GPx4) is a selenocysteine (Sec)-containing glutathione peroxidase. GPx4 catalyzes the reduction of hydroperoxides and the oxidation of thiols through a ping-pong mechanism in which the redox transitions are faster than the formation of enzyme-substrate complexes; thus, K m and V max are infi nite.
MAIORINO, MATILDE +8 more
openaire +2 more sources
Glutathione peroxidase 4 (GPx4) is a selenocysteine (Sec)-containing glutathione peroxidase. GPx4 catalyzes the reduction of hydroperoxides and the oxidation of thiols through a ping-pong mechanism in which the redox transitions are faster than the formation of enzyme-substrate complexes; thus, K m and V max are infi nite.
MAIORINO, MATILDE +8 more
openaire +2 more sources
The glutathione peroxidase activity of glutathione S-transferases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1980Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
openaire +3 more sources
Glutathione Peroxidase of Fish
Journal of Food Science, 1992ABSTRACTGlutathione peroxidase (GSH‐Px) activity was detected in the muscle and skin tissues from several fish species. The muscle GSH‐Px showed an optimum pH at 8.0 for salmon and 8.5 for carp. Stability of salmon muscle enzyme was enhanced in the presence of reduced glutathione (GSH), but considerably decreased in the presence of tert ...
Toshiki Nakano +2 more
openaire +2 more sources