Antimycin
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Antimycin
Antimycins are produced as secondary metabolites by ''Streptomyces'' bacteria, a soil bacteria. These specialized metabolites likely function to kill neighboring organisms in order to provide the streptomyces bacteria with a competitive edge. Chemical structures Biosynthesis Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as an assembly line for antimycin production. The assembly is genetically coded for by the ant gene family. The assembly requires 14 proteins, AntBCDEFGHIJKLMNO, which shuttle the intermediates along the assembly line through a series of transesterifications, keto reductions, thiolations (addition of a sulfur containing group), condensations, anadenylations The last two steps involving AntB and AntO are tailoring steps. The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with tryptophan, an amino acid. 1. The in ...
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Antimycin A
Antimycin A (more exactly Antimycin A1b) is a secondary metabolite produced by ''Streptomyces'' bacteria and a member of a group of related compounds called antimycins. Antimycin A is classified as an List of extremely hazardous substances, extremely hazardous substance in the United States, as defined in Section 302 of the U.S. Emergency Planning and Community Right-to-Know Act (42 U.S.C. 11002), and is subject to strict reporting requirements by facilities which produce, store, or use it in significant quantities. Use Antimycin A is the active ingredient in Fintrol, a chemical piscicide (fish poison) used in fisheries management. Antimycin A was first discovered in 1945 and registered for use as a fish toxicant in 1960. Fintrol ® is the only currently registered product containing Antimycin A and is classified as a restricted use pesticide because of its aquatic toxicity and requirement for highly specialized training in order to use it. In 1993, several toxicology studie ...
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Antimycin Congeners
Antimycins are produced as secondary metabolites by ''Streptomyces'' bacteria, a soil bacteria. These specialized metabolites likely function to kill neighboring organisms in order to provide the streptomyces bacteria with a competitive edge. Chemical structures Biosynthesis Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as an assembly line for antimycin production. The assembly is genetically coded for by the ant gene family. The assembly requires 14 proteins, AntBCDEFGHIJKLMNO, which shuttle the intermediates along the assembly line through a series of transesterifications, keto reductions, thiolations (addition of a sulfur containing group), condensations, anadenylations The last two steps involving AntB and AntO are tailoring steps. The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with tryptophan, an amino acid. 1. The in ...
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Antimycin A Synthesis
Antimycins are produced as secondary metabolites by ''Streptomyces'' bacteria, a soil bacteria. These specialized metabolites likely function to kill neighboring organisms in order to provide the streptomyces bacteria with a competitive edge. Chemical structures Biosynthesis Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as an assembly line for antimycin production. The assembly is genetically coded for by the ant gene family. The assembly requires 14 proteins, AntBCDEFGHIJKLMNO, which shuttle the intermediates along the assembly line through a series of transesterifications, keto reductions, thiolations (addition of a sulfur containing group), condensations, anadenylations The last two steps involving AntB and AntO are tailoring steps. The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with tryptophan, an amino acid. 1. The in ...
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Antimycin A Synthesis2
Antimycins are produced as secondary metabolites by ''Streptomyces'' bacteria, a soil bacteria. These specialized metabolites likely function to kill neighboring organisms in order to provide the streptomyces bacteria with a competitive edge. Chemical structures Biosynthesis Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as an assembly line for antimycin production. The assembly is genetically coded for by the ant gene family. The assembly requires 14 proteins, AntBCDEFGHIJKLMNO, which shuttle the intermediates along the assembly line through a series of transesterifications, keto reductions, thiolations (addition of a sulfur containing group), condensations, anadenylations The last two steps involving AntB and AntO are tailoring steps. The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with tryptophan, an amino acid. 1. The in ...
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Urauchimycin
Urauchimycins are antimycin Antimycins are produced as secondary metabolites by ''Streptomyces'' bacteria, a soil bacteria. These specialized metabolites likely function to kill neighboring organisms in order to provide the streptomyces bacteria with a competitive edge. Che ... antibiotics isolated from marine actinomycete. References External links Antibiotics {{antibiotic-stub ...
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Streptomyces
''Streptomyces'' is the largest genus of Actinomycetota and the type genus of the family Streptomycetaceae. Over 500 species of ''Streptomyces'' bacteria have been described. As with the other Actinomycetota, streptomycetes are gram-positive, and have genomes with high GC content. Found predominantly in soil and decaying vegetation, most streptomycetes produce spores, and are noted for their distinct "earthy" odor that results from production of a volatile metabolite, geosmin. Streptomycetes are characterised by a complex secondary metabolism. They produce over two-thirds of the clinically useful antibiotics of natural origin (e.g., neomycin, streptomycin, cypemycin, grisemycin, bottromycins and chloramphenicol). The antibiotic streptomycin takes its name directly from ''Streptomyces''. Streptomycetes are infrequent pathogens, though infections in humans, such as mycetoma, can be caused by '' S. somaliensis'' and '' S. sudanensis'', and in plants can be caused by '' S. cavi ...
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Membrane Transport Protein
A membrane transport protein (or simply transporter) is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins; that is they exist permanently within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion or active transport. The two main types of proteins involved in such transport are broadly categorized as either ''channels'' or ''carriers''. The solute carriers and atypical SLCs are secondary active or facilitative transporters in humans. Collectively membrane transporters and channels are known as the transportome. Transportomes govern cellular influx and efflux of not only ions and nutrients but drugs as well. Difference between channels and carriers A carrier is not open simultaneously to both the extracellular and intracellular environments. ...
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Acyltransferase
Acyltransferase is a type of transferase enzyme that acts upon acyl groups. Examples include: * Glyceronephosphate O-acyltransferase * Lecithin-cholesterol acyltransferase *Long-chain-alcohol O-fatty-acyltransferase In enzymology, a long-chain-alcohol O-fatty-acyltransferase () is an enzyme that catalyzes the chemical reaction :acyl-CoA + a long-chain alcohol \rightleftharpoons CoA + a long-chain ester Thus, the two substrates of this enzyme are acyl-C ... See also * Acetyltransferase External links * Transferases EC 2.3 {{2.3-enzyme-stub ...
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Lactone
Lactones are cyclic carboxylic esters, containing a 1-oxacycloalkan-2-one structure (), or analogues having unsaturation or heteroatoms replacing one or more carbon atoms of the ring. Lactones are formed by intramolecular esterification of the corresponding hydroxycarboxylic acids, which takes place spontaneously when the ring that is formed is five- or six-membered. Lactones with three- or four-membered rings (α-lactones and β-lactones) are very reactive, making their isolation difficult. Special methods are normally required for the laboratory synthesis of small-ring lactones as well as those that contain rings larger than six-membered. Nomenclature Lactones are usually named according to the precursor acid molecule (''aceto'' = 2 carbon atoms, ''propio'' = 3, ''butyro'' = 4, ''valero'' = 5, ''capro'' = 6, etc.), with a ''-lactone'' suffix and a Greek letter prefix that specifies the number of carbon atoms in the heterocycle — that is, the distance between the relevant -OH ...
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Thioester
In organic chemistry, thioesters are organosulfur compounds with the functional group . They are analogous to carboxylate esters () with the sulfur in the thioester playing the role of the linking oxygen in the carboxylate ester, as implied by the ''thio-'' prefix. They are the product of esterification between a carboxylic acid () and a thiol (). In biochemistry, the best-known thioesters are derivatives of coenzyme A, e.g., acetyl-CoA.Matthys J. Janssen "Carboxylic Acids and Esters" in PATAI's Chemistry of Functional Groups: Carboxylic Acids and Esters, Saul Patai, Ed. John Wiley, 1969, New York: pp. 705–764. Synthesis The most typical route to thioester involves the reaction of an acid chloride with an alkali metal salt of a thiol: :RSNa + R'COCl -> R'COSR + NaCl Another common route entails the displacement of halides by the alkali metal salt of a thiocarboxylic acid. For example, thioacetate esters are commonly prepared by alkylation of potassium thioacetate: :CH3COSK + ...
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Ketoacyl Synthase
Ketoacyl synthases (KSs) catalyze the condensation reaction of acyl-CoA or acyl-acyl ACP with malonyl-CoA to form 3-ketoacyl-CoA or with malonyl-ACP to form 3-ketoacyl-ACP. This reaction is a key step in the fatty acid synthesis cycle, as the resulting acyl chain is two carbon atoms longer than before. KSs exist as individual enzymes, as they do in type II fatty acid synthesis and type II polyketide synthesis, or as domains in large multidomain enzymes, such as type I fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs are divided into five families: KS1, KS2, KS3, KS4, and KS5. Multidomain enzyme systems Fatty acid synthase Fatty acid synthase (FAS) is the enzyme system involved in de novo fatty acid synthesis. FAS is an iterative multienzyme consisting of several component enzymes, one of which is ketoacyl synthase. There are two types of FASs: type I and type II. Type I FASs are highly integrated multidomain enzymes. They contain discrete functional domains resp ...
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