L-threo-3-Methylaspartate
-''threo''-3-Methylaspartate is an unusual amino acid formed by glutamate mutase and can be metabolised by methylaspartate ammonia-lyase. It is found in the structures of the antibiotics friulimicin and vicenistatin and in carbon metabolism of haloarchaea (Methylaspartate cycle Methylaspartate may refer to: * L-''threo''-3-Methylaspartate * ''N''-Methyl-D-aspartic acid {{Short pages monitor [Baidu]   |
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Methylaspartate Cycle
Methylaspartate may refer to: * L-threo-3-Methylaspartate, L-''threo''-3-Methylaspartate * N-Methyl-D-aspartic acid, ''N''-Methyl-D-aspartic acid {{Short pages monitor ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid ''residues'' form the second-largest component ( water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling li ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Methylaspartate Mutase
In enzymology, a methylaspartate mutase () is an enzyme that catalyzes the chemical reaction :L-threo-3-methylaspartate \rightleftharpoons L-glutamate Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and one product, L-glutamate. This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is L-threo-3-methylaspartate carboxy-aminomethylmutase. Other names in common use include glutamate mutase, glutamic mutase, glutamic isomerase, glutamic acid mutase, glutamic acid isomerase, methylaspartic acid mutase, beta-methylaspartate-glutamate mutase, and glutamate isomerase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide. Structural studies As of late 2007, 8 structures have been solved for this class of enzymes, with PDB PDB may refer to: * Chess Problem Database Server (PDB Server) * 1,4-Dichlorobenzene (para ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Methylaspartate Ammonia-lyase
The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalysis, catalyzes the chemical reaction :L-''threo''-3-methylaspartate \rightleftharpoons mesaconate + NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The List of enzymes, systematic name of this enzyme class is L-''threo''-3-methylaspartate ammonia-lyase (mesaconate-forming). Other names in common use include β-methylaspartase, 3-methylaspartase, and L-''threo''-3-methylaspartate ammonia-lyase. This enzyme participates in c5-branched dibasic acid metabolism and nitrogen metabolism. It employs one cofactor (biochemistry), cofactor, cobamide. Structural studies Several structures of this enzyme have been deposited in the Protein Data Bank (linked in the infobox) which show it possesses a TIM barrel domain. References * * EC 4.3.1 Cobamide enzymes Enzymes of known structure {{enzyme-stub ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Friulimicin
Friulimicin B is a lipopeptide antibiotic produced by ''Actinoplanes friuliensis ''Actinoplanes friuliensis'' is a species of bacteria that produces lipopeptide antibiotics with peptidoglycan Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-li ...''. It includes the unusual amino acid methylaspartate. References {{reflist Antibiotics Lipopeptides Cyclic peptides ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Vicenistatin
Vicenistatin is a macrolactam antibiotic synthesized by ''Streptomyces halstedii ''Streptomyces halstedii'' is a bacterium species from the genus of ''Streptomyces'' which has been isolated from deeper soil layers. ''Streptomyces halstedii'' produces magnamycin B, vicenistatin deltamycin A2, deltamycin A3, bafilomycin B1 ...'' HC34. It was originally isolated from this bacterium in 1993. It includes the unusual starter unit methylaspartate. References {{reflist Macrolide antibiotics ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Haloarchaea
Haloarchaea (halophilic archaea, halophilic archaebacteria, halobacteria) are a class of the Euryarchaeota, found in water saturated or nearly saturated with salt. Halobacteria are now recognized as archaea rather than bacteria and are one of the largest groups. The name 'halobacteria' was assigned to this group of organisms before the existence of the domain Archaea was realized, and while valid according to taxonomic rules, should be updated. Halophilic archaea are generally referred to as haloarchaea to distinguish them from halophilic bacteria. These microorganisms are among the halophile organisms, that they require high salt concentrations to grow, with most species requiring more than 2.0M NaCl for growth and survival. They are a distinct evolutionary branch of the Archaea distinguished by the possession of ether-linked lipids and the absence of murein in their cell walls. Haloarchaea can grow aerobically or anaerobically. Parts of the membranes of haloarchaea are ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |