Valine Transaminase
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Valine Transaminase
Valine (symbol Val or V) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α- carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, beans and legumes. It is encoded by all codons starting with GU (GUU, GUC, GUA, and GUG). History and etymology Valine was first isolated from casein in 1901 by Hermann Emil Fischer. The name valine comes from valeric acid, which in turn is named after the plant valerian due to the presence of the acid in the roots of the plant. Nomenclature According to IUPAC, carbon atoms forming valine are numbered sequentially st ...
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Skeletal Formula
The skeletal formula, or line-angle formula or shorthand formula, of an organic compound is a type of molecular structural formula that serves as a shorthand representation of a molecule's bonding and some details of its molecular geometry. A skeletal formula shows the skeletal structure or skeleton of a molecule, which is composed of the skeletal atoms that make up the molecule. It is represented in two dimensions, as on a piece of paper. It employs certain conventions to represent carbon and hydrogen atoms, which are the most common in organic chemistry. An early form of this representation was first developed by organic chemist August Kekulé, while the modern form is closely related to and influenced by the Lewis structure of molecules and their valence electrons. Hence they are sometimes termed Kekulé structures or Lewis–Kekulé structures. Skeletal formulae have become ubiquitous in organic chemistry, partly because they are relatively quick and simple to draw, and ...
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Valerian (herb)
Valerian (''Valeriana officinalis'', Caprifoliaceae) is a perennial flowering plant native to Europe and Asia. In the summer when the mature plant may have a height of , it bears sweetly scented pink or white flowers that attract many fly species, especially hoverflies of the genus ''Eristalis''. It is consumed as food by the larvae of some Lepidoptera (butterfly and moth) species, including the grey pug. Crude extract of valerian root may have sedative and anxiolytic effects, and is commonly sold in dietary supplement capsules to promote sleep, but there is insufficient clinical evidence that it is effective for this purpose. Its roots and leaves cause a catnip-like response in cats. History Valerian has been used as a herb in traditional medicine since at least the time of ancient Greece and Rome. Hippocrates described its properties, and Galen later prescribed it as a remedy for insomnia. In medieval Sweden, it was sometimes placed in the wedding clothes of the groom to wa ...
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Transamination
Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids. This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism). Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases. α-ketoglutarate acts as the predominant amino-group acceptor and produces glutamate as the new amino acid. :Aminoacid + α-ketoglutarate ↔ α-keto acid + glutamate Glutamate's amino group, in turn, is transferred to oxaloacetate in a second transamination reaction yielding aspartate. :Glutamate + oxaloacetate ↔ α-ketoglutarate + aspartate Mechanism of action Transamination catalyzed by aminotransferase occurs in two stages. In the first step, the α amino group of an amino acid is transferred to the enzyme, producing the ...
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Dihydroxyacid Dehydratase
The enzyme dihydroxy-acid dehydratase () catalyzes the chemical reaction :2,3-dihydroxy-3-methylbutanoate \rightleftharpoons 3-methyl-2-oxobutanoate + H2O This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coenzyme A (CoA) biosynthesis. Nomenclature This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ... of this enzyme class is 2,3-dihydroxy-3-methylbutanoate hydro-lyase (3-methyl-2-oxobutanoate-forming). Other names in common use include * acetohydroxyacid dehydratase, * α,β-dihydroxyacid dehydratase, * 2,3-dihydroxyisovalerate dehydratase, * α,β-dihydroxyisovalerate dehydratase, * dihydroxy acid dehydrase, ...
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