Diisopropyl-fluorophosphatase
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Diisopropyl-fluorophosphatase
The enzyme diisopropyl-fluorophosphatase (EC 3.1.8.2) catalyzes the reaction :diisopropyl fluorophosphate + H2O \rightleftharpoons diisopropyl phosphate + fluoride This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. The systematic name is diisopropyl-fluorophosphate fluorohydrolase. Other names in common use include DFPase, tabunase, somanase, organophosphorus acid anhydrolase, organophosphate acid anhydrase, OPA anhydrase, diisopropylphosphofluoridase, dialkylfluorophosphatase, diisopropyl phosphorofluoridate hydrolase, isopropylphosphorofluoridase, and diisopropylfluorophosphonate dehalogenase. It employs one cofactor, divalent cation. At least one compound, chelating agent is known to inhibit this enzyme. Structural studies As of late 2007, 16 structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. ...
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Loligo Vulgaris
The European squid or common squid (''Loligo vulgaris'') is a large squid belonging to the family Loliginidae. It occurs abundantly in coastal waters from the North Sea to at least the west coast of Africa. This species lives from sea level to depths of . Its mantle (mollusc), mantle is up to long. The species is extensively exploited by commercial fisheries. ''Loligo reynaudii'', the Cape Hope squid, was previously treated as a subspecies of ''L. vulgaris''. Description The European squid has a long, moderately slender and cylindrical body. Rhomboid fins comprise two-thirds of the mantle (mollusc), mantle length, though locomotion is via Squid, jet propulsion. The posterior border is slightly concave. The head is relatively small and has large eyes which are covered with a transparent membrane. Like almost all squid, this species has cephalopod limb, ten limbs surrounding the mouth and Cephalopod beak, beak: eight are relatively short cephalopod limb, arms, and two, whi ...
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Catalysis
Catalysis () is the increase in rate of a chemical reaction due to an added substance known as a catalyst (). Catalysts are not consumed by the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. The rate increase occurs because the catalyst allows the reaction to occur by an alternative mechanism which may be much faster than the noncatalyzed mechanism. However the noncatalyzed mechanism does remain possible, so that the total rate (catalyzed plus noncatalyzed) can only increase in the presence of the catalyst and never decrease. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usual ...
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Diisopropyl Fluorophosphate
Diisopropyl fluorophosphate (DFP) or Isoflurophate is an oily, colorless liquid with the chemical formula C6H14FO3P. It is used in medicine and as an organophosphorus insecticide. It is stable, but undergoes hydrolysis when subjected to moisture. Uses in medicine Diisopropyl fluorophosphate is a parasympathomimetic drug irreversible anti-cholinesterase and has been used in ophthalmology as a miotic agent in treatment of chronic glaucoma, as a miotic in veterinary medicine, and as an experimental agent in neuroscience because of its acetylcholinesterase inhibitory properties and ability to induce delayed peripheral neuropathy. Uses as toxin The marked toxicity of esters of monofluorophosphoric acid was discovered in 1932, when Willy Lange and his PhD student Gerda von Krueger prepared the methyl, ethyl, n-propyl, and n-butyl esters and incidentally experienced their toxic effects. Another homologue of this series of esters, Diisopropyl fluorophosphate, was developed by B ...
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Diisopropyl Phosphate
Diisopropylphosphate is an acetylcholinesterase inhibitor. It acts by covalently binding to acetylcholinesterase. See also * Diisopropyl-fluorophosphatase The enzyme diisopropyl-fluorophosphatase (EC 3.1.8.2) catalyzes the reaction :diisopropyl fluorophosphate + H2O \rightleftharpoons diisopropyl phosphate + fluoride This enzyme belongs to the family of hydrolases, specifically those acting on ... References Acetylcholinesterase inhibitors Organophosphates Isopropyl esters {{ester-stub ...
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Fluoride
Fluoride (). According to this source, is a possible pronunciation in British English. is an Inorganic chemistry, inorganic, Monatomic ion, monatomic Ion#Anions and cations, anion of fluorine, with the chemical formula (also written ), whose salts are typically white or colorless. Fluoride salts typically have distinctive bitter tastes, and are odorless. Its salts and minerals are important Reagent, chemical reagents and industrial chemicals, mainly used in the production of hydrogen fluoride for fluorocarbons. Fluoride is classified as a weak base since it only partially associates in solution, but concentrated fluoride is corrosive and can attack the skin. Fluoride is the simplest fluorine anion. In terms of charge and size, the fluoride ion resembles the hydroxide ion. Fluoride ions occur on Earth in several minerals, particularly fluorite, but are present only in trace quantities in bodies of water in nature. Nomenclature Fluorides include compounds that contain ionic ...
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Hydrolase
In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond: :\ce \quad \xrightarrowtext\quad \ce This typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases. Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase, which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid. Acetic acid is an important metabolite in the body and a critical intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleo ...
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List Of Enzymes
Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: :Oxidoreductases (EC 1) ( Oxidoreductase) * Dehydrogenase * Luciferase * DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) ** Homoserine dehydrogenase ** Aminopropanol oxidoreductase ** Diacetyl reductase ** Glycerol dehydrogenase ** Propanediol-phosphate dehydrogenase ** glycerol-3-phoshitiendopene dehydrogenase (NAD+) ** D-xylulose reductase ** L-xylulose reductase ** Lactate dehydrogenase ** Malate dehydrogenase ** Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) ** Glucose oxidase ** L-gulonolactone oxidase ** Thiamine oxidase ** Xanthine oxidase * EC 1.1.4 (with a disulfide as accep ...
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Organophosphorus Acid Anhydrolase
Organophosphorus acid anhydrolase (OPAA) is an enzyme that been shown to be particularly effective in detoxifying organophosphorus-containing compounds, such as deadly Nerve agent, nerve gas used in chemical warfare. The enzyme is found in a diverse range of organisms, including protozoa, squid and clams, mammals, and soil bacteria. A highly active form of the enzyme is typically isolated from the marine bacteria ''Alteromonas, Alteromonas undina'' for laboratory study. This form is both halophilic and thermophilic, making it particularly useful for detoxification applications. A slightly less active variant of OPAA has also been isolated in mung beans and slime mold duckweed. Enzyme mechanism Although the exact mechanism of OPAA’s nerve-agent detoxification is unclear, researchers have deduced that the basic reaction follows a general base mechanism with a simple in-line displacement of fluoride at the phosphorus center using an activated water molecule, as seen in Figure 1. OP ...
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Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be classified into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a " prosthetic group", which consists of a coenzyme that is tightly (or even covalently and, therefore, permanently) bound to a ...
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Divalent Cation
In chemistry, the valence (US spelling) or valency (British spelling) of an atom is a measure of its combining capacity with other atoms when it forms chemical compounds or molecules. Valence is generally understood to be the number of chemical bonds that each atom of a given chemical element typically forms. Double bonds are considered to be two bonds, triple bonds to be three, quadruple bonds to be four, quintuple bonds to be five and sextuple bonds to be six. In most compounds, the valence of hydrogen is 1, of oxygen is 2, of nitrogen is 3, and of carbon is 4. Valence is not to be confused with the related concepts of the coordination number, the oxidation state, or the number of valence electrons for a given atom. Description The valence is the combining capacity of an atom of a given element, determined by the number of hydrogen atoms that it combines with. In methane, carbon has a valence of 4; in ammonia, nitrogen has a valence of 3; in water, oxygen has a valence of 2; ...
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Chelating Agent
Chelation () is a type of bonding of ions and their molecules to metal ions. It involves the formation or presence of two or more separate coordinate bonds between a polydentate (multiple bonded) ligand and a single central metal atom. These ligands are called chelants, chelators, chelating agents, or sequestering agents. They are usually organic compounds, but this is not a necessity. The word ''chelation'' is derived from Greek χηλή, ''chēlē'', meaning "claw"; the ligands lie around the central atom like the claws of a crab. The term ''chelate'' () was first applied in 1920 by Sir Gilbert T. Morgan and H. D. K. Drew, who stated: "The adjective chelate, derived from the great claw or ''chele'' (Greek) of the crab or other crustaceans, is suggested for the caliperlike groups which function as two associating units and fasten to the central atom so as to produce heterocyclic rings." Chelation is useful in applications such as providing nutritional supplements, in ch ...
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Enzyme Inhibitor
An enzyme inhibitor is a molecule that binds to an enzyme and blocks its Enzyme activity, activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which Substrate (biochemistry), substrate molecules are converted into Product (chemistry), products. An enzyme Enzyme catalysis, facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the Rate-determining step, most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. Enzyme inhibitors may bind Reversible reaction, reversibly or irreversibly. Irreversible inhibitors form a Covalent bond, chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By cont ...
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