Peroxiredoxins
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Peroxiredoxins
Peroxiredoxins (Prxs, ; HGNC root symbol ''PRDX'') are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels and thereby mediate signal transduction in mammalian cells. The family members in humans are PRDX1, PRDX2, PRDX3, PRDX4, PRDX5, and PRDX6. The physiological importance of peroxiredoxins is indicated by their relative abundance (one of the most abundant proteins in erythrocytes after hemoglobin is peroxiredoxin 2). Their function is the reduction of peroxides, specifically hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. Classification Prxs were historically divided into three (mechanistic) classes: *Typical 2-Cys Prxs *Atypical 2-Cys Prxs and *1-Cys Prxs. The designation of "1-Cys" and "2-Cys" Prxs was introduced in 1994 as it was noticed that, among the 22 Prx sequences known at the time, only one Cys residue was absolutely conserved; this is the residue now recognized as the (required) peroxidatic cysteine, CP. The ...
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Sulfenic Acid
In chemistry, a sulfenic acid is an organosulfur compound and oxoacid with the general formula . It is the first member of the family of organosulfur oxoacids, which also include sulfinic acids () and sulfonic acids (), respectively. The base member of the sulfenic acid series with R = H is hydrogen thioperoxide. Properties In contrast to sulfinic and sulfonic acids, simple sulfenic acids, such as methanesulfenic acid, CH3SOH, are highly reactive and cannot be isolated in solution. In the gas phase the lifetime of methanesulfenic acid is about one minute. The gas phase structure of methanesulfenic acid was found by microwave spectroscopy (rotational spectroscopy) to be CH3–S–O–H. Sulfenic acids can be stabilized through steric effects, which prevent the sulfenic acid from condensing with itself to form thiosulfinates, RS(O)SR, such as allicin from garlic. Through the use of X-ray crystallography, the structure of such stabilized sulfenic acids were shown to be R–S– ...
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Antioxidant
Antioxidants are compounds that inhibit oxidation, a chemical reaction that can produce free radicals. This can lead to polymerization and other chain reactions. They are frequently added to industrial products, such as fuels and lubricants, to prevent oxidation, and to foods to prevent spoilage, in particular the rancidification of oils and fats. In cells, antioxidants such as glutathione, mycothiol or bacillithiol, and enzyme systems like superoxide dismutase, can prevent damage from oxidative stress. The only dietary antioxidants are vitamins A, C, and E, but the term ''antioxidant'' has also been applied to numerous other dietary compounds that only have antioxidant properties in vitro, with little evidence for antioxidant properties in vivo. Dietary supplements marketed as antioxidants have not been shown to maintain health or prevent disease in humans. History As part of their adaptation from marine life, terrestrial plants began producing non-marine antioxi ...
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Peroxiredoxin 1
Peroxiredoxin-1 is a protein that in humans is encoded by the ''PRDX1'' gene. Function This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Three transcript variants encoding the same protein have been identified for this gene. Interactions Peroxiredoxin 1 has been shown to interact with PRDX4. A chemoproteomic approach has revealed that peroxiredoxin 1 is the main target of theonellasterone. Clinical significance As enzymes that combat oxidative stress, peroxiredoxins play an important role in health and disease. Peroxiredoxin 1 and peroxiredoxin 2 have been shown to be released by some cells when stimulated by LPS or TNF-alpha. The released peroxiredoxin can ...
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PRDX1
Peroxiredoxin-1 is a protein that in humans is encoded by the ''PRDX1'' gene. Function This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Three transcript variants encoding the same protein have been identified for this gene. Interactions Peroxiredoxin 1 has been shown to interact with PRDX4. A chemoproteomic approach has revealed that peroxiredoxin 1 is the main target of theonellasterone. Clinical significance As enzymes that combat oxidative stress, peroxiredoxins play an important role in health and disease. Peroxiredoxin 1 and peroxiredoxin 2 have been shown to be released by some cells when stimulated by LPS or TNF-alpha. The released peroxiredoxin can ...
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Bacterial
Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms. Typically a few micrometres in length, bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. Bacteria inhabit soil, water, acidic hot springs, radioactive waste, and the deep biosphere of Earth's crust. Bacteria are vital in many stages of the nutrient cycle by recycling nutrients such as the fixation of nitrogen from the atmosphere. The nutrient cycle includes the decomposition of dead bodies; bacteria are responsible for the putrefaction stage in this process. In the biological communities surrounding hydrothermal vents and cold seeps, extremophile bacteria provide the nutrients needed to sustain life by converting dissolved compounds, such as hydrogen sulphide and methane, to energy. Bacteria also live in symbiotic and parasitic relationships ...
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Glutathione
Glutathione (GSH, ) is an antioxidant in plants, animals, fungi, and some bacteria and archaea. 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. It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine. The carboxyl group of the cysteine residue is attached by normal peptide linkage to glycine. Biosynthesis and occurrence Glutathione biosynthesis involves two adenosine triphosphate-dependent steps: *First, γ-glutamylcysteine is synthesized from L- glutamate and cysteine. This conversion requires the enzyme glutamate–cysteine ligase (GCL, glutamate cysteine synthase). This reaction is the rate-limiting step in glutathione synthesis. *Second, glycine is added to the C-terminal of γ-glutamylcysteine. This condensation is catalyzed by glutathione synthetase. While all animal ...
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Ascorbic Acid
Vitamin C (also known as ascorbic acid and ascorbate) is a water-soluble vitamin found in citrus and other fruits and vegetables, also sold as a dietary supplement and as a topical 'serum' ingredient to treat melasma (dark pigment spots) and wrinkles on the face. It is used to prevent and treat scurvy. Vitamin C is an essential nutrient involved in the repair of tissue, the formation of collagen, and the enzymatic production of certain neurotransmitters. It is required for the functioning of several enzymes and is important for immune system function. It also functions as an antioxidant. Most animals are able to synthesize their own vitamin C. However, apes (including humans) and monkeys (but not all primates), most bats, some rodents, and certain other animals must acquire it from dietary sources. There is some evidence that regular use of supplements may reduce the duration of the common cold, but it does not appear to prevent infection. It is unclear whether supp ...
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Glutathione S-transferase
Glutathione ''S''-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal—also known as MAPEG—proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions. GSTs can constitute up to 10% of cytosolic protein in some mammalian organs. GSTs catalyse the conjugation of GSH—via a sulfhydryl group—to electrophilic centers on a wide variety of substrates in order to make the compounds more water-soluble. This activity detoxifies endogenous co ...
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Sulfinic Acid
Sulfinic acids are oxoacids of sulfur with the structure RSO(OH). In these organosulfur compounds, sulfur is pyramidal. Structure and properties Sulfinic acids RSO2H are about 1000x more acidic than the corresponding carboxylic acid RCO2H. Sulfur is pyramidal, consequently sulfinic acids are chiral. Preparation They are often prepared in situ by acidification of the corresponding sulfinate salts, which are typically more robust than the acid. These salts are generated by reduction of sulfonyl chlorides. An alternative route is the reaction of Grignard reagents with sulfur dioxide. Transition metal sulfinates are also generated by insertion of sulfur dioxide into metal alkyls, a reaction that may proceed via a metal sulfur dioxide complex. Unsubstituted sulfinic acid, when R is the hydrogen atom, is a higher energy isomer of sulfoxylic acid, both of which are unstable. Examples An example of a simple, well-studied sulfinic acid is phenylsulfinic acid. A commercially import ...
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Sulfiredoxin
In enzymology, a sulfiredoxin () is an enzyme that catalyzes the chemical reaction :peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH \rightleftharpoons peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R The 3 substrates of this enzyme are peroxiredoxin-(S-hydroxy-S-oxocysteine), ATP, and a thiol, whereas its 4 products are peroxiredoxin-(S-hydroxycysteine), ADP, phosphate, and a disulfide. This enzyme is involved in antioxidant metabolism by re-activating peroxiredoxins, which are a group of peroxidases, when these enzymes are inhibited by over-oxidation. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other, known, acceptors. The systematic name of this enzyme class is peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]. Other names in common use include Srx1, sulphiredoxin, and peroxiredoxin-(S-hydroxy-S-oxocysteine) re ...
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Peroxiredoxin 2
Peroxiredoxin-2 is a protein that in humans is encoded by the PRDX2 gene. PRDX2 encodes a member of the peroxiredoxin family of antioxidant enzyme Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products ...s, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. The crystal structure of this protein has been resolved to 0.27 nm (= 2.7 angstroms). Transcript variants encoding distinct isoforms have been identified for this gene. References Further reading

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Phosphorylation
In chemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. This process and its inverse, dephosphorylation, are common in biology and could be driven by natural selection. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License. Protein phosphorylation often activates (or deactivates) many enzymes. Glucose Phosphorylation of sugars is often the first stage in their catabolism. Phosphorylation allows cells to accumulate sugars because the phosphate group prevents the molecules from diffusing back across their transporter. Phosphorylation of glucose is a key reaction in sugar metabolism. The chemical equation for the conversion of D-glucose to D-glucose-6-phosphate in the first step of glycolysis is given by :D-glucose + ATP → D-glucose-6-phosphate + ADP : ΔG° = −16.7 kJ/mol (° indicates measurement at standard condition) Hepatic cells are freely permeable to glucose, and ...
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