In enzymology, a glutathione oxidase (EC 1.8.3.3) is an enzyme that catalyzes the chemical reaction
2 glutathione + O2 glutathione disulfide + H2O2
Thus, the two substrates of this enzyme are glutathione and O2, whereas its two products are glutathione disulfide and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione metabolism. It employs one cofactor, FAD.
and 27 Related for: Glutathione oxidase information
In enzymology, a glutathioneoxidase (EC 1.8.3.3) is an enzyme that catalyzes the chemical reaction 2 glutathione + O2 ⇌ {\displaystyle \rightleftharpoons...
decrease in oxidative stress, including glutathione oxidation and lipid peroxidation, when xanthine oxidase was inhibited using allopurinol. Oxidative...
environment. The enzymes of xenobiotic metabolism, particularly the glutathione S-transferases are also important in agriculture, since they may produce...
cancer. The source of Se used in biosynthesis is selenophosphate. Glutathioneoxidase is an enzyme with a selenol at its active site. Organoselenium compounds...
catalase. More specifically, they may use a NADH oxidase/NADH peroxidase (NOX/NPR) system or a glutathione peroxidase system. An example of an aerotolerant...
dose) of NAPQI is produced, which is inactivated by conjugation with glutathione (GSH). The amount of NAPQI produced differs in certain populations.[citation...
dual function of the same egg oxidase, and secondarily through cytoplasmic ROS scavengers, such as catalase and glutathione. Oxidative burst acts as a defence...
5-lipoxygenase-activating protein (FLAP) and LTC4 synthase (LTC4S), which couples glutathione to an LTA4 intermediate. The MRP1 transporter then secretes cytosolic...
hydrochloride, glutathione are examples of antioxidants that have been studied for their anti-browning properties. Chelating agents − Polyphenol oxidase requires...
flavin can reduce the product. Glutathione reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) to glutathione (GSH). GR requires FAD and...
cofactor glutathione to function. Ser 15, Cys 16, Gln 111, and the helix dipole of alpha 1 of the enzyme stabilize the thiolate form of glutathione which...
amino acid proline is not broken down properly by the enzymes proline oxidase or pyrroline-5-carboxylate dehydrogenase, causing a buildup of proline...
prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms". Free Radical Biology and Medicine...
detoxification metabolism include cytochrome P450 oxidases, UDP-glucuronosyltransferases, and glutathione S-transferases. These processes are particularly...
compounds crucial for life. Many cofactors also contain sulfur, including glutathione, and iron–sulfur proteins. Disulfides, S–S bonds, confer mechanical strength...
xanthine oxidase, NADPH oxidases and cytochromes P450. Hydrogen peroxide is produced by a wide variety of enzymes including several oxidases. Reactive...
mitochondria, it is found in cytochrome c oxidase, which is the last protein in oxidative phosphorylation. Cytochrome c oxidase is the protein that binds the O2...
is then recycled back to ascorbate by endogenous antioxidants such as glutathione.: 98–99 In the eye, ascorbate is thought to protect against photolytically...
used after the publications by Beers & Sizer and Aebi. Enzyme kinetics Glutathione peroxidase Peroxidase Superoxide dismutase GRCh38: Ensembl release 89:...
especially high abundance can be observed for enzymes called MOX (methanol oxidase), FMDH (formate dehydrogenase), and DHAS (dihydroxyacetone synthase). Their...
make glutathione. Excess cysteine and methionine are oxidized to sulfate by sulfite oxidase, eliminated in the urine, or stored as glutathione (which...
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