Aspergillomarasmine A
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Aspergillomarasmine A
Aspergillomarasmine A is an polyamino acid naturally produced by the mold ''Aspergillus versicolor''. The substance has been reported to inhibit two antibiotic resistance carbapenemase proteins in bacteria, New Delhi metallo-beta-lactamase 1 (NDM-1) and Verona integron-encoded metallo-beta-lactamase (VIM-2), and make those antibiotic-resistant bacteria susceptible to antibiotics. Aspergillomarasmine A is toxic to leaves of barley and other plants, being termed as "Toxin C" when produced by ''Pyrenophora teres''. The molecule is a tetracarboxylic acid with four -COOH groups. One section of the molecule is the amino acid aspartic acid. This has two alanine molecules attached by substituting a hydrogen on the methyl group with a link to the amine group. Aspergillomarasmine B differs in that the last alanine is replaced by glycine. The crystalline substance was first isolated in 1956, but its name was given until 1965. In addition to ''Aspergillus versicolor'', aspergillomarasmine A ...
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Aspergillus Versicolor
''Aspergillus versicolor'' is a slow-growing filamentous fungus commonly found in damp indoor environments and on food products. It has a characteristic musty odor associated with moldy homes and is a major producer of the hepatotoxic and carcinogenic mycotoxin sterigmatocystin. Like other ''Aspergillus'' species, ''A. versicolor'' is an eye, nose, and throat irritant. Taxonomy The fungus was first described by Jean-Paul Vuillemin in 1903 under the name ''Sterigmatocystis versicolor'', and was later moved to the genus ''Aspergillus'' by Carlo Tiraboschi in 1908. Presently, the genus ''Sterigmatocystis'' is obsolete. Ecology ''Aspergillus versicolor'' is a highly ubiquitous species commonly isolated from soil, plant debris, marine environments, and indoor air environments. It is among the most common of indoor Mold (fungus), molds, often reported in dust and in water-damaged building materials, such as wallboards, insulation, textiles, ceiling tiles, and manufactured wood. ''Asp ...
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Colletotrichum Gloeosporioides
''Glomerella cingulata'' is a fungal plant pathogen, being the name of the sexual stage (teleomorph) while the more commonly referred to asexual stage (anamorph) is called ''Colletotrichum gloeosporioides''. For most of this article the pathogen will be referred to as ''C. gloeosporioides.'' This pathogen is a significant problem worldwide, causing anthracnose and fruit rotting diseases on hundreds of economically important hosts. Hosts and symptoms ''C. gloeosporioides'' has an extremely broad host range, causing anthracnose disease on a variety of crops such as cereals and grasses, legumes, fruits, vegetables, perennial crops, and trees. It has been observed as infecting harvested durian of the species ''Durio graveolens''. Some studies suggest that ''C. gloeosporioides'' has sub-populations specific to each host.Nelson, C. Scot "Mango Anthracnose (''Colletotrichum gloeosporioides'')" University of Hawaii at Manoa cooperative extension service. Aug. 2008 The symptoms can vary ...
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Isoserine
Isoserine is a non-proteinogenic α-hydroxy-β-amino acid, and an isomer of serine. Non-proteinogenic amino acids do not form proteins, and are not part of the genetic code of any known organism. Isoserine has only been produced synthetically. The first documented synthesis of isoserine in a laboratory setting was by Miyazawa et al., who published their results in 1976. See also * Abiogenesis * Miller–Urey experiment The Miller–Urey experiment (or Miller experiment) is a famous chemistry experiment that simulated the conditions thought at the time (1952) to be present in the atmosphere of the early, prebiotic Earth, in order to test the hypothesis of the ... References Non-proteinogenic amino acids Alpha hydroxy acids {{Biochemistry-stub ...
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Deamination
Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver, however it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia. The rest of the amino acid is made up of mostly carbon and hydrogen, and is recycled or oxidized for energy. Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. Urea and uric acid can safely diffuse into the blood and then be excreted in urine. Deamination reactions in DNA Cytosine Spontaneous deamination is the hydrolysis reaction of cytosine into uracil, releasing ammonia in the process. This can occur in vitro thr ...
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2,3-diaminopropionic Acid
2,3-Diaminopropionic acid (2,3-diaminopropionate, Dpr) is a non-proteinogenic amino acid found in certain secondary metabolites, including zwittermicin A and tuberactinomycin. Biosynthesis 2,3-Diaminopropionate is formed by the pyridoxal phosphate (PLP) mediated amination of serine Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated − form un .... References {{DEFAULTSORT:Diaminopropionate, 2,3- Amino acids Carboxylic acids ...
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Hydrolysis
Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution reaction, substitution, elimination reaction, elimination, and solvation reactions in which water is the nucleophile. Biological hydrolysis is the cleavage of biomolecules where a water molecule is consumed to effect the separation of a larger molecule into component parts. When a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g., sucrose being broken down into glucose and fructose), this is recognized as saccharification. Hydrolysis reactions can be the reverse of a condensation reaction in which two molecules join into a larger one and eject a water molecule. Thus hydrolysis adds water to break down, whereas condensation builds up by removing water. Types Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both the substance and w ...
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Chemical Decomposition
Chemical decomposition, or chemical breakdown, is the process or effect of simplifying a single chemical entity (normal molecule, reaction intermediate, etc.) into two or more fragments. Chemical decomposition is usually regarded and defined as the exact opposite of chemical synthesis. In short, the chemical reaction in which two or more products are formed from a single reactant is called a decomposition reaction. The details of a decomposition process are not always well defined but some of the process is understood; much energy is needed to break bonds. Since all decomposition reactions break apart the bonds holding it together in order to produce into its simpler basic parts, the reactions would require some form of this energy in varying degrees. Because of this fundamental rule, it is known that most of these reactions are endothermic although exceptions do exist. The stability of a chemical compound is eventually limited when exposed to extreme environmental conditions ...
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Metalloprotease
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands coordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline. Classification There are two subgroups of metalloproteinases: * Exopeptidases, metalloexopeptidases ( EC number: 3.4.17). * Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM prot ...
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Endothelin Converting Enzyme
converting enzyme 1, also known as ECE1, is an enzyme which in humans is encoded by the ''ECE1'' gene. Function Endothelin-converting enzyme-1 is involved in the proteolytic processing of endothelin-1 (EDN1), -2 ( EDN2), and -3 (EDN3 Endothelin-3 is a protein that in humans is encoded by the ''EDN3'' gene. The protein encoded by this gene is a member of the endothelin family. Endothelins are endothelium-derived vasoactive peptides involved in a variety of biological functions ...) to biologically active peptides. References Further reading

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Ferric
In chemistry, iron(III) refers to the element iron in its +3 oxidation state. In ionic compounds (salts), such an atom may occur as a separate cation (positive ion) denoted by Fe3+. The adjective ferric or the prefix ferri- is often used to specify such compounds — as in "ferric chloride" for iron(III) chloride, . The adjective "ferrous" is used instead for iron(II) salts, containing the cation Fe2+. The word ferric is derived from the Latin word ''ferrum'' for iron. Iron(III) metal centres also occur in coordination complexes, such as in the anion ferrioxalate, , where three bidentate oxalate ions surrounding the metal centre; or, in organometallic compounds, such as the ferrocenium cation , where two cyclopentadienyl anions are bound to the FeIII centre. Iron is almost always encountered in the oxidation states 0 (as in the metal), +2, or +3. Iron(III) is usually the most stable form in air, as illustrated by the pervasiveness of rust, an insoluble iron(III)-containing ...
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Chelation
Chelation is a type of bonding of ions and molecules to metal ions. It involves the formation or presence of two or more separate coordinate bonds between a Denticity, 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, as in the case of zinc and its use as a maintenance therapy to prevent the absorption of copper in people with Wilson's disease. Chelation is useful in applications such as providing nutritional supplements, in chelation therapy to remove toxic metals from the body, as contrast medium, contrast agents in MRI, MRI scanning, in manufacturing using homogeneous catalysts, in chemical water treatment to assist in the removal of metals, and in fertilizers. Chelate effect The chelate effect is the greater affinity of chelating ligands for a metal ion than that of similar nonchelating (monodentate ...
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Trifluoroacetic Acid
Trifluoroacetic acid (TFA) is an organofluorine compound with the chemical formula CF3CO2H. It is a structural analogue of acetic acid with all three of the acetyl group's hydrogen atoms replaced by fluorine atoms and is a colorless liquid with a vinegar-like odor. TFA is a stronger acid than acetic acid, having an acid ionisation constant, ''K''a, that is approximately 34,000 times higher, as the highly electronegative fluorine atoms and consequent electron-withdrawing nature of the trifluoromethyl group weakens the oxygen-hydrogen bond (allowing for greater acidity) and stabilises the anionic conjugate base. TFA is widely used in organic chemistry for various purposes. Synthesis TFA is prepared industrially by the electrofluorination of acetyl chloride or acetic anhydride, followed by hydrolysis of the resulting trifluoroacetyl fluoride: : + 4 → + 3 + : + → + Where desired, this compound may be dried by addition of trifluoroacetic anhydride. An older route to ...
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