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Adenosyl-fluoride Synthase
The fluorinase enzyme (, also known as adenosyl-fluoride synthase) catalyzes the reaction between fluoride ion and the co-factor '' S'' -adenosyl-L-methionine to generate L-methionine and 5'-fluoro-5'-deoxyadenosine, the first committed product of the fluorometabolite biosynthesis pathway. The fluorinase was originally isolated from the soil bacterium ''Streptomyces cattleya'', but homologues have since been identified in a number of other bacterial species, including ''Streptomyces'' sp. MA37, '' Nocardia brasiliensis'' and ''Actinoplanes'' sp. N902-109. This is the only known enzyme capable of catalysing the formation of a carbon-fluorine bond, the strongest single bond in organic chemistry. A homologous chlorinase enzyme, which catalyses the same reaction with chloride rather than fluoride ion, has been isolated from ''Salinospora tropica'', from the biosynthetic pathway of salinosporamide A. Reactivity The fluorinase catalyses an SN2-type nucleophilic substitution at the ...
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Catalysis
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in 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. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some st ...
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Nucleophile
In chemistry, a nucleophile is a chemical species that forms bonds by donating an electron pair. All molecules and ions with a free pair of electrons or at least one pi bond can act as nucleophiles. Because nucleophiles donate electrons, they are Lewis bases. ''Nucleophilic'' describes the affinity of a nucleophile to bond with positively charged atomic nuclei. Nucleophilicity, sometimes referred to as nucleophile strength, refers to a substance's nucleophilic character and is often used to compare the affinity of atoms. Neutral nucleophilic reactions with solvents such as alcohols and water are named solvolysis. Nucleophiles may take part in nucleophilic substitution, whereby a nucleophile becomes attracted to a full or partial positive charge, and nucleophilic addition. Nucleophilicity is closely related to basicity. History The terms ''nucleophile'' and ''electrophile'' were introduced by Christopher Kelk Ingold in 1933, replacing the terms ''anionoid'' and ''cation ...
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Organofluorine
Organofluorine chemistry describes the chemistry of the organofluorines, organic compounds that contain the carbon–fluorine bond. Organofluorine compounds find diverse applications ranging from oil and water repellents to pharmaceuticals, refrigerants, and reagents in catalysis. In addition to these applications, some organofluorine compounds are pollutants because of their contributions to ozone depletion, global warming, bioaccumulation, and toxicity. The area of organofluorine chemistry often requires special techniques associated with the handling of fluorinating agents. The carbon–fluorine bond Fluorine has several distinctive differences from all other substituents encountered in organic molecules. As a result, the physical and chemical properties of organofluorines can be distinctive in comparison to other organohalogens. # The carbon–fluorine bond is one of the strongest in organic chemistry (an average bond energy around 480 kJ/molKirsch, Peer ''Modern fluoroo ...
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Carbon–fluorine Bond
The carbon–fluorine bond is a polar covalent bond between carbon and fluorine that is a component of all organofluorine compounds. It is one of the strongest single bonds in chemistry (after the B–F single bond, Si–F single bond, and H–F single bond), and relatively short, due to its partial ionic character. The bond also strengthens and shortens as more fluorines are added to the same carbon on a chemical compound. As such, fluoroalkanes like tetrafluoromethane (carbon tetrafluoride) are some of the most unreactive organic compounds. Electronegativity and bond strength The high electronegativity of fluorine (4.0 for fluorine vs. 2.5 for carbon) gives the carbon–fluorine bond a significant polarity or dipole moment. The electron density is concentrated around the fluorine, leaving the carbon relatively electron poor. This introduces ionic character to the bond through partial charges (Cδ+—Fδ−). The partial charges on the fluorine and carbon are attract ...
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Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, RCSB, and BMRB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. History Two ...
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Tertiary Structure
Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of poly ...
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Positron Emission Tomography
Positron emission tomography (PET) is a functional imaging technique that uses radioactive substances known as radiotracers to visualize and measure changes in metabolic processes, and in other physiological activities including blood flow, regional chemical composition, and absorption. Different tracers are used for various imaging purposes, depending on the target process within the body. For example: * Fluorodeoxyglucose ( 18F">sup>18FDG or FDG) is commonly used to detect cancer; * 18Fodium fluoride">sup>18Fodium fluoride (Na18F) is widely used for detecting bone formation; * Oxygen-15 (15O) is sometimes used to measure blood flow. PET is a common imaging technique, a medical scintillography technique used in nuclear medicine. A radiopharmaceutical – a radioisotope attached to a drug – is injected into the body as a radioactive tracer, tracer. When the radiopharmaceutical undergoes beta plus decay, a positron is emitted, and when the positron interacts with an or ...
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Radioactive Tracer
A radioactive tracer, radiotracer, or radioactive label is a chemical compound in which one or more atoms have been replaced by a radionuclide so by virtue of its radioactive decay it can be used to explore the mechanism of chemical reactions by tracing the path that the radioisotope follows from reactants to products. Radiolabeling or radiotracing is thus the radioactive form of isotopic labeling. In biological contexts, use of radioisotope tracers are sometimes called radioisotope feeding experiments. Radioisotopes of hydrogen, carbon, phosphorus, sulfur, and iodine have been used extensively to trace the path of biochemical reactions. A radioactive tracer can also be used to track the distribution of a substance within a natural system such as a cell or tissue, or as a flow tracer to track fluid flow. Radioactive tracers are also used to determine the location of fractures created by hydraulic fracturing in natural gas production.Reis, John C. (1976). ''Environmental Con ...
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Transhalogenation
Transhalogenation is a substitution reaction in which the halide of a halide compound is exchanged for another halide. Finkelstein reaction A common method is halide metathesis. An example is the conversion of alkyl chloride into alkyl fluoride: :C3H5-Cl + NaF → R-F + NaCl This kind of reaction is called Finkelstein reaction. However, it is also possible, for example, to produce phosphorus fluoride compounds by transhalogenating chlorine, bromine or iodine bound to phosphorus with a metal fluoride. Details and biological use As a halogen source for transhalogenation, metal halides (such as sodium fluoride or lithium fluoride Lithium fluoride is an inorganic compound with the chemical formula LiF. It is a colorless solid, that transitions to white with decreasing crystal size. Although odorless, lithium fluoride has a bitter-saline taste. Its structure is analogous to ...) are often used, but also the use of onium halides is possible. Transhalogenation has been described a ...
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Fluorine-18
Fluorine-18 (18F) is a fluorine radioisotope which is an important source of positrons. It has a mass of 18.0009380(6) u and its half-life is 109.771(20) minutes. It decays by positron emission 96% of the time and electron capture 4% of the time. Both modes of decay yield stable oxygen-18. Natural occurrence is a natural trace radioisotope produced by cosmic ray spallation of atmospheric argon as well as by reaction of protons with natural oxygen: 18O + p → 18F + n.sup>18Oater with high energy protons (typically ~18 MeV). The fluorine produced is in the form of a water solution of 18F">sup>18F luoride, which is then used in a rapid chemical synthesis of various radio pharmaceuticals. The organic oxygen-18 pharmaceutical molecule is not made before the production of the radiopharmaceutical, as high energy protons destroy such molecules (radiolysis). Radiopharmaceuticals using fluorine must therefore be synthesized after the fluorine-18 has been produced. History First p ...
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Chlorinase Reaction
Adenosyl-chloride synthase (, ''chlorinase'', ''5'-chloro-5'-deoxyadenosine synthase'') is an enzyme with systematic name ''S-adenosyl-L-methionine:chloride adenosyltransferase''. This enzyme catalyses the following chemical reaction : S-adenosyl-L-methionine + chloride \rightleftharpoons 5-deoxy-5-chloroadenosine + L-methionine This enzyme is isolated from the marine bacterium ''Salinispora tropica ''Salinispora tropica'' is an obligate marine actinomycete bacterium species. It produces salinosporamide A and salinosporamide B, potential anti-cancer agents, as well as the polycyclic macrolides The Macrolides are a class of natural pr ...''. References External links * {{Portal bar, Biology, border=no EC 2.5.1 ...
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L-amino-acid Oxidase
In enzymology, an L-amino acid oxidase (LAAO) () is an enzyme that catalyzes the chemical reaction :an L-amino acid + H2O + O2 \rightleftharpoons a 2-oxo acid + NH3 + H2O2 The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. As suggested by the name of the family, LAAOs are flavoenzymes which function to catalyze the stereospecific oxidative deamination of an L-amino acid. The three substrates of the enzymatic reaction are an L-amino acid, water, and oxygen, whereas the three products are the corresponding α-keto acid (2-oxo acid), ammonia, and hydrogen peroxide. One example of the enzyme in action occurs with the conversion L-alanine into pyruvic acid (2-oxopropanoic ...
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