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Glutathione peroxidase 1, also known as GPx1, is an enzyme that in humans is encoded by the GPX1 gene on chromosome 3. [5] This gene encodes a member of the glutathione peroxidase family. Glutathione peroxidase functions in the detoxification of hydrogen peroxide , and is one of the most important antioxidant enzymes in humans.
Since oxytosis/ferroptosis is a form of regulated cell death, [10] some of the molecules that regulate oxytosis/ferroptosis are involved in metabolic pathways that regulate cysteine exploitation, glutathione state, nicotinamide adenine dinucleotide phosphate (NADP) function, lipid peroxidation, and iron homeostasis. [9]
Glutathione peroxidase 1 (GPx1) is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose preferred substrate is hydrogen peroxide. Glutathione peroxidase 4 (GPx4) has a high preference for lipid hydroperoxides; it is expressed in nearly every mammalian cell, though at much lower levels.
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.
In molecular biology a selenoprotein is any protein that includes a selenocysteine (Sec, U, Se-Cys) amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. [1] Selenoprotein P is the most common selenoprotein found in the plasma.
Gpx1, Gpx2, Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, whereas Gpx6 is a selenoprotein in humans with cysteine-containing homologues in rodents. Amyloid beta, when bound to heme, has been shown to have peroxidase activity. [2] A typical group of peroxidases are the haloperoxidases. This group is able to form reactive ...
Erastin is a small molecule capable of initiating ferroptotic cell death. [1] Erastin binds and activates voltage-dependent anion channels (VDAC) by reversing tubulin's inhibition on VDAC2 and VDAC3, [2] and functionally inhibits the cystine-glutamate antiporter system X c −. [3]
Human protein-coding gene pages: •Python code for maintaining the list •List of human protein-coding genes page 1 covers genes A1BG–EPGN •List of human protein-coding genes page 2 covers genes EPHA1–MTMR3
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