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Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species, free radicals, peroxides, lipid peroxides, and heavy metals. [2] It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine .
Sinecatechins, the first botanical drug approved by the US FDA, is an extract from the leaves of Camellia sinensis.. A botanical drug is defined in the United States Federal Food, Drug, and Cosmetic Act as a botanical product that is marketed as diagnosing, mitigating, treating, or curing a disease; a botanical product in turn, is a finished, labeled product that contains ingredients from plants.
The antioxidant enzyme glutathione peroxidase 4 (GPX4) belongs to the family of glutathione peroxidases, which consists of 8 known mammalian isoenzymes (GPX1–8).GPX4 catalyzes the reduction of hydrogen peroxide, organic hydroperoxides, and lipid peroxides at the expense of reduced glutathione and functions in the protection of cells against oxidative stress.
Phytochelatin binds to Pb ions leading to sequestration of Pb ions in plants and thus serves as an important component of the detoxification mechanism in plants. [6] Phytochelatin seems to be transported into the vacuole of plants, so that the metal ions it carries are stored safely away from the proteins of the cytosol .
Genetically modified crops are plants used in agriculture, the DNA of which has been modified using genetic engineering techniques. In most cases, the aim is to introduce a new trait to the plant which does not occur naturally in the species. As of 2015, 26 plant species have been genetically modified and approved for commercial release in at ...
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. [2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants. [3]
Glutaredoxins [1] [2] [3] (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose metabolism.
The NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage from compounds like hydrogen peroxide. [1] Of greater quantitative importance is the production of NADPH for tissues involved in biosynthesis of fatty acids or isoprenoids , such as the liver, mammary glands ...
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